Crystal of fibroblast growth factor receptor 1 in complex with fibroblast growth factor

ABSTRACT

The determination and use of three dimensional structures of receptor protein tyrosine kinases and/or their ligands are described. One particular group of such structures includes three dimensional structures of the extracellular domain of RPTKs. The three dimensional structures of RPTKs can faciliate the design and identification of modulators of RPTK function. Other such structures can include of RPTK ligands, such as stem cell factor or a fragment thereof. Modulators of RPTK function can be used to treat diseases that are mediated by inappropriate RPTK activity.

This application is a 371 of PCT/US00/23744 filed Aug. 30, 2000, which claims priority to Ser. No. 60/151,810, filed Aug. 30, 1999.

CROSS REFERENCE TO RELATED APPLICATIONS

This application claims priority under 35 U.S.C. § 119(e) of U.S. Provisional Application Ser. No. 60/151,810, filed Aug. 30, 1999, the disclosure of which is herein incorporated by reference in its entirety.

BACKGROUND

The following description of the background of the invention is provided simply as an aid in understanding the invention and is not admitted to describe or constitute prior art to the invention.

Receptor protein tyrosine kinases (“RPTKs”) include a large and diverse family of enzymes. The RPTK family contains multiple subfamilies, one of which is the fibroblast growth factor receptor (FGFR) subfamily. Another subfamily is the type III receptor tyrosine kinase (RTK) subfamily whose members include platelet-derived growth factor receptors a and β (“PDGFR α” and “PDGFR β”), macrophage colony-stimulating factor receptor (M-CSFR), c-kit (also referred to as SCF receptor (“SCFR”)) and the flt3 receptor. The members of this RTK subfamily contain five immunoglobulin-like (Ig) domains in their extracellular ligand binding domains followed by a single transmembrane domain and a cytoplasmic tyrosine kinase domain interrupted by a large kinase-insert. For a review of RPTKs, see Schlessinger and Ullrich, 1992, Neuron 9: 383–391; for a review describing the FGFR subfamily, see Givol and Yayon, 1992, FASEB J. 6 (15): 3362–3369.

All RPTKs enzymatically transfer a high energy phosphate from adenosine triphosphate to a tyrosine residue in a target protein. These phosphorylation events regulate certain cellular phenomena in signal transduction processes. Cellular signal transduction processes contain multiple steps that convert an extracellular signal into an intracellular signal. The intracellular signal is then converted into a cellular response. RPTKs are components in many signal transduction processes. Typically, an RPTK regulates the flow of a signal in a particular step in the process by phosphorylating a downstream molecule. This phosphorylation modulates the downstream molecule's activity by turning it either “on” or “off,” causing excessive or deficient signalling by the downstream molecule. Excessive signalling can lead to such abnormalities as uncontrolled cell proliferation, which is characteristic of such disorders as cancer, angiogenesis induced by various tumors, atherosclerosis, and arthritis. Alternatively, cellular proliferation can be induced therapeutically, for example angiogenesis may be used to ameliorate coronary artery disease by inducing collateral vascularization.

Ligand-induced dimerization of RPTKs is an important step in the RPTK-mediated signal transduction process. For review of the importance of dimerization of RPTKs, see Lemmon and Schlessenger, 1994, Trends in Biochem. Sci. 19: 459463; and Ullrich and Schlessenger, 1990, Cell 61:203–212. Some growth factors, for example platelet-derived growth factor (“PDGF”) and stem cell factor (“SCF”), are dimeric molecules that, by themselves, induce dimerization of their specific receptors. In contrast, other growth factors, such as fibroblast growth factors (FGFs), are monomeric molecules that must act in concert with other molecules to induce dimerization of their specific receptors. See Schlessenger et al., 1995, Cell 83: 357–360; Spivak-Kroizman et al., 1994, Cell 79: 1015–1024; Ornitz et al., 1992, Mol. Cell. Biol. 12: 240–247. In particular, FGFs typically function in concert with soluble or cell surface-bound heparin sulfate-containing proteoglycans (HSPGs).

The FGFR subfamily consists of at least 21 structurally related polypeptides, designated FGFR1 through FGFR21, that are expressed in embryonic, fetal, and adult vertebrates. FGFR1 through FGFR4, are known as “high affinity FGFRs,” due to their ability to bind appropriate fibroblast growth factors with a high affinity. These high affinity FGFRs are characterized by an extracellular ligand-binding domain which comprises three immunoglobulin (IG)-like domains (known as D1, D2, and D3), a single transmembrane helix, and a cytoplasmic domain containing tyrosine kinase activity. See Lee et al., 1989, Science 245: 57–60; Jaye et al., 1992, J. Mol. Biol. 227: 840–851; Johnson & Williams, 1993, Adv. Cancer. Res. 60: 1–41. Each of the four high affinity FGFRs binds to a specific subset of FGFs. Ornitz et al., 1996, J. Biol. Chem. 271: 15292–15297.

Naturally occuring variants of the high affinity FGFRs-lacking D1, or D1 and the linker region between D1 and D2 known as the “acid box,” have been identified. These varient FGFRs retain the ability to bind appropriate FGFs with high affinity, suggesting that the D2 and D3 regions are sufficient to confer FGF binding ability and specificity. See Crumley et al., 1991, Oncogene 6: 2255–2262; Dionne et al., 1990, EMBO J. 9: 2685–2692; Johnson and Williams, 1993, Adv. Cancer. Res. 60: 141. In particular, D3 has been shown to play a critical role in the binding specificity of FGFRs. See Bottaro, et al., 1990, J. Biol. Chem. 265: 12767–12770; Miki et al., 1992, Proc. Natl. Acad. Sci. 89: 246–250; Dell et al., 1992, J. Biol. Chem. 267: 21225–21229; Yayon et al., 1992 EMBO J. 11: 1885–1890.

Recently, three dimensional structures of the intracellular catalytic domains of various PTKs have been described in International Publication No. WO 98/07835, U.S. patent application Ser. No. 60/034,168, filed Dec. 19, 1996, and U.S. Pat. No. 5,942,428, issued on Aug. 24, 1999, each of which is hereby incorporated herein by reference in its entirety including all claims, drawings, tables, and figures.

Despite recent advances in the understanding of signal transduction and function of the receptor PTKs and their ligands, there remains a need in the art for the atomic-level characterization and analysis of such molecules, particularly with respect to the design and synthesis of novel and improved therapeutic molecules.

SUMMARY

The present invention relates to the three dimensional structures of receptor protein tyrosine kinases and/or their ligands. These molecular structures may include an RPTK or ligand thereof, alone or as a complex including one or more ligands. In particular, this application relates to molecular structures comprising a polypeptide which includes the extracellular domain of a receptor protein tyrosine kinase, alone and in complexes comprising one or more ligands. In another aspect, the application describes molecular structures comprising a polypeptide which includes the receptor binding core of a growth factor, such as stem cell facter, alone or in a complex with one or more ligands such as a receptor protein tyrosine kinase.

The present application concerns solving and using the three dimensional structures of receptor protein tyrosine kinases, and more particularly to structures including the extracellular domain of receptor protein tyrosine kinases, alone and in complexes comprising one or more ligands. As an example, X-ray crystallograpic techniques are used herein to determine the three dimensional structure of certain RPTK extracellular domains bound to certain ligands, such as FGF molecules or SCF molecules, at atomic resolution. The application also concerns solving and using the three dimensional structures of stem cell factor, and more particularly to structures including the receptor binding core of stem cell factor, alone and in complexes comprising one or more ligands.

The three dimensional structures described herein elucidate specific interactions between receptor protein tyrosine kinases and/or ligands bound to them. The coordinates that define the three dimensional structures of receptor protein tyrosine kinases are useful for determining three dimensional structures of receptor RPTKs with unknown structure. In addition, the coordinates are also useful for designing and identifying modulators of receptor protein tyrosine kinase function. These modulators are potentially useful as therapeutics for treating or preventing disease, including (but not limited to) cell proliferative diseases, such as cancer, tumorigenic angiogenesis, atherosclerosis, and arthritis. Alternatively, cellular proliferation can be induced therapeutically, for example angiogenesis may be used to ameliorate coronary artery disease by inducing collateral vascularization. Thus in a first aspect, the invention features a crystalline form of a polypeptide corresponding to all or a portion of the extracellular domain of an RPTK. In certain embodiments, the invention features a crystalline form of an RPTK bound to a ligand or ligand analog. In typical embodiments, the RPTK is an FGFR, such as FGFR1 or FGFR2, and the ligand is an FGF, such as FGF1 or FGF2. In particularly suitable embodiments, the polypeptide comprises residues 150–360 of FGFR1 or residues 150–360 of FGFR2, the sequences of which are shown in FIG. 4. The ligand can be a fibroblast growth factor, such as an FGF1 including the amino acid sequence as shown in FIG. 17 or an FGF2 including the amino acid sequence as shown in FIG. 17.

The term “crystalline form,” in the context of the invention, refers to a crystal formed from an aqueous solution comprising a purified polypeptide. In certain embodiments, a crystal is formed from an aqueous solution comprising all or part of the extracellular domain of an RPTK. A crystalline form of a polypeptide is characterized as being capable of diffracting x-rays in a pattern defined by one of the crystal forms depicted in Blundel et al., 1976, Protein Crystallography, Academic Press, and in Hahn, 1996, The International Tables for Crystallography, Volume A, Fourth Edition, Kluwer Academic Publishers. In preferred embodiments, a crystalline form may also be formed from a purified polypeptide corresponding to all or part of the extracellular domain of an RPTK in a complex with one or more ligands or ligand analogs, as defined herein.

A crystalline form of an RPTK may also comprise a crystal formed from an aqueous solution comprising a purified polypeptide corresponding to all or part of the extracellular domain of an RPTK, with or without a complexed ligand or ligand analogue, into which one or more heavy atoms are introduced. Preferably, introduction of a heavy atom results in as minimal a change to the original crystalline structure as possible. A heavy atom can be introduced into the protein crystal by well known techniques. Preferred reagents for introduction of heavy atoms are platinum tetrachloride, mercuric acetate, ethyl mercury thiosalicylate, iridium hexachloride, gadolinium sulfate, samarium acetate, gold chloride, uranyl acetate, mercury chloride, and ethyl mercury chloride.

The term “receptor protein tyrosine kinase,” or “RPTK,” as used herein refers to an enzyme comprising an intracellular catalytic domain capable of transferring the high energy phosphate of adenosine triphosphate to a tyrosine residue located on a protein target, an extracellular domain that serves as a receptor for a specific ligand or set of ligands, and a membrane-spanning domain linking the intracellular and extracellular domains. In vivo, the binding of a ligand to its receptor results in receptor dimerization and activation of the intracellular catalytic domain. Preferred RPTKs of the invention are PDGFR, SCFR, EGFR, VEGFR, HGFR, neurotrophinR, HER2, HER3, HER4, InsulinR, IGFR, CSFIR, FLK, KDR, VEGFR2, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, or MUSK. More preferably, a receptor PTK of the invention is a member of the FGFR family, such as FGFR1, FGFR2, FGFR3, and FGFR4. Certain receptor PTKs have no known ligand, and are referred to as “orphan receptor PTKs.”

The term “FGFR1” refers to one member of multiple receptor PTKs that are homologous to one another, and which bind FGF. In this context, the term “homologous” preferably refers to about 70% or greater amino acid identity between two members of the FGFR family, more preferably at least about 80% amino acid identity, and most preferably at least about 90% amino acid identity. The term “FGFR1” includes human FGFR1 which comprises or consists of the amino acid sequence of residues 150–360 of FGFR1 as shown in FIG. 4. “Homologous” in this and other contexts also includes molecules of similarity sufficient to indicate relation by a common origin or archetype.

As used herein, the term “extracellular domain” refers to all or a portion of the region of an RPTK that exists outside the plasma membrane of a cell. Preferably, an extracellular domain is anchored to the plasma membrane by a polypeptide region that associates with the plasma membrane, and most preferably by a polypeptide region that is embedded within or crosses the plasma membrane. An extracellular domain can also be a soluble domain that is not anchored to the plasma membrane of a cell. Most preferably, an extracellular domain comprises one or more binding sites for one or more ligands.

RPTK extracellular domains can comprise one or more known structural motifs. Preferably, these structural motifs can be one or more of the following: cysteine-rich regions, fibronectin III-like domains, Ig-like domains, EGF-like domains, factor VIII-like domains, and Kringle domains. Most preferred are RPTKs comprising one or more IG-like domains. For example, FGFR1, FGFR2, FGFR3, and FGFR4 each contain three IG-like domains, labeled D1, D2, and D3. Other preferred RPTKs comprising IG-like domains include, but are not limited to, PDGFR, c-Kit, Flk1, Flk2, Flk4, KLG, TrkA, TrkB, TrkC, Axl, Tie, c-Eyk, and Elk.

The term “ligand” as used herein refers to a molecule that specifically binds to a receptor. In various embodiments, ligands are growth factors, cytokines, lymphokines, or hormones. Preferred ligands include, but are not limited to, epidermal growth factors, insulin, platelet-derived growth factors, stem cell factors, vascular endothelial growth factors, hepatocyte growth factors, and neurotrophins. Particularly preferred ligands are fibroblast growth factors.

The term “fibroblast growth factor” as used herein refers to a family of polypeptide growth factors that share extensive sequence homologies and a common structural fold. At the time of the invention, the FGF family contains about 21 known members, named FGF1 through FGF21. Those skilled in the art will understand that other members of the FGF family may be later identified and used in practicing the present invention. FGFs bind to FGFRs, and to HSPGs. Preferred FGFs are FGF1, FGF2, FGF3, and FGF4.

The term “ligand analog” as used herein refers to a molecule that is structurally or functionally similar to a ligand and that binds to the ligand binding site on a polypeptide. A ligand analog may be structurally similar to a ligand if the analog results from the substitution, addition, or deletion of one or more atoms, functional groups, or amino acid residues of a ligand. A ligand analog is functionally similar to a ligand if the ligand analog binds to the ligand binding site of the ligand receptor, or if binding of the ligand analog to the ligand receptor results in a similar biochemical event(s) to those resulting from ligand binding. Such a ligand analog may also be referred to as a ligand “mimic.”

Binding of a ligand analog may also result in an inhibition of one or more biochemical events which result from ligand binding, or may act as a competitor of ligand binding. Such a ligand analog may also be referred to as an “inhibitor.” A ligand analog may also bind to the putative ligand binding site of an orphan receptor PTK.

A ligand analog may preferably bind to its ligand receptor with lower, equal, or greater affinity than does the corresponding ligand. In certain embodiments, a ligand analog may be a mutant ligand. The term “mutant” is defined herein.

The term “bind” as used herein refers to a specific interaction of two or more molecules. Binding preferably refers to noncovalent binding. Such binding is typically mediated by one or more of hydrogen-bonding, van der Waals interactions, aromatic interactions, electrostatic interactions, and hydrophobic interactions. In certain embodiments, binding can refer to covalent binding of two or more molecules.

The term “catalytic domain” refers to a region of a protein that can exist as a separate entity from the protein, but that retains complete or partial catalytic function. The catalytic domain of a protein tyrosine kinase is characterized as having considerable amino acid identity to the catalytic domain of other protein tyrosine kinases. The catalytic domain of a protein tyrosine kinase is also characterized as being a polypeptide that is soluble in solution.

The term “considerable amino acid identity” preferably refers to at least about 30°/identity, more preferably at least about 35% identity, and most preferably at least about 40°/identity. These degrees of amino acid identity refer to the identity between different protein tyrosine kinase families. Amino acid identity for members of a given protein tyrosine kinase family range from about 55% to about 90%.

The term “identity” as used herein refers to a property of sequences that measures their similarity or relationship. Identity is measured by dividing the number of identical residues in the two sequences by the total number of residues and multiplying the product by 100. Thus, two copies of exactly the same sequence have 100% identity, but sequences that are less highly conserved and have deletions, additions, or replacements have a lower degree of identity. Two sequences may also be homologous to one another. The term “homologous” is defined herein, and can include, but is not limited to molecules (e.g., proteins) of similarity sufficient to indicate relation by a common origin or archetype. Those skilled in the art will recognize that several computer programs are available for determining sequence identity and homology, including BLAST (Altschul, et al., 1990, J. Mol. Biol. 215:403410) and FASTA (Pearson and Lipman, 1988, Proc. Natl. Acad. Sci. USA 85:2444–2448).

The term “functional” refers to the ability of a portion of a protein to retain all or partial function of the intact protein. For example, a functional RPTK catalytic domain may retain the ability to convert a substrate into a product by phosphorylating the substrate, while a functional RPTK extracellular domain may retain the ability to bind to its ligand.

In certain embodiments, a polypeptide can exist as an extracellular domain, even though it is not functional. For example, a polypeptide corresponding to an extracellular domain may not comprise all of the structures necessary for binding a ligand or ligand analog. In these embodiments, a measure of an RPTK extracellular domain can be a polypeptide that is homologous to other RPTK extracellular domains.

In another embodiment, the crystal comprises a polypeptide, which includes an extracellular domain of a receptor protein tyrosine kinase, and a ligand bound to the extracellular domain. For example, the receptor protein tyrosine kinase can be a fibroblast growth factor receptor, such as FGFR1 or FGFR2, and the ligand can be a fibroblast growth factor, such as FGF1 or FGF2. The crystal may also include a sulfated oligosaccharide bound to the receptor protein tyrosine kinase and/or a ligand bound thereto. The size (and thus molecular weight) of the sulfated oligosaccharide may vary. Examples of suitable sulfated oligosaccharide which may be contained in the crystal include a sulfated disaccharides, hexasaccharides, octasaccharides, decasaccharides, dodecasaccharides. Preferably, the sulfated oligosaccharide is sulfated mucooligosaccharide, such as heparin. In a particular aspect of this embodiment, the crystal includes a FGF:FGFR:heparin ternary complex. For example, the crystal can include a FGF:FGFR:heparin ternary complex such as an FGF1:FGFR1:heparin ternary complex, an FGF2:FGFR:heparin ternary complex, an FGF1:FGFR2:heparin ternary complex, or an FGF2:FGFR2:heparin ternary complex.

In certain other aspects, a crystal may comprise a polypeptide which includes the receptor binding core of a stem cell factor. The receptor binding core generally has a three dimensional structure which includes a four-helix bundle and two strands. Stem cell factors and fragments containing the receptor binding core typically crystallize in a form which includes a homodimer of the polypeptide. While the monomers which make up the homodimer may be covalently linked, e.g., by one or more intermolecular disulfide bonds, the SCF crystals described herein include a noncovalent homodimer. The SCF homodimer forms orthorhombic crystal which has unit cell dimensions: a=72.47 Å, b=83.45 Å and c=89.15 Å. The SCF homodimer may also be crystallized (e.g., in the presence of to form monoclinic crystals. Monoclinic crystals of a noncovalent SCF homodimer were used to obtain the atomic structural coordinates shown in Table 4. These atomic coordinates are for crystals formed from a homodimer of a polypeptide which contains amino acid residues 1–141 of stem cell factor. These crystals have C2 symmetry. Crystals of this type may also include an RPTK, such as c-kit (SCFR) bound to a stem cell factor or fragment thereof. Preferably, the crystal includes c-kit bound to the receptor binding core of a stem cell factor.

The term “polypeptide” refers to an amino acid chain representing a portion of, or the entire sequence of, amino acid residues comprising a protein.

The term “association” refers to a condition of proximity between a chemical entity or compound, or portions or fragments thereof, and RPTK, or portions or fragments thereof. The association may be non-covalent, i.e., where the juxtaposition is energetically favored by, e.g., hydrogen-bonding, van der Waals, electrostatic or hydrophobic interactions, or it may be covalent.

The terms “heavy atom” and “heavy metal atom” refer to an atom that is a transition element, a lanthanide metal, or an actinide metal. Lanthanide metals include elements with atomic numbers between 57 and 71, inclusive. Actinide metals include elements with atomic numbers between 89 and 103, inclusive. In preferred embodiments, a crystal of the invention can comprise one or more heavy metal atoms. Such a crystal is referred to herein as a “derivative crystal.”

In another aspect, the invention features a crystalline form of a polypeptide corresponding to the D2-D3 region of an RPTK extracellular domain. In preferred embodiments, the invention features a crystalline form of the D2-D3 region of a receptor PTK extracellular domain bound to a ligand or ligand analog. In preferred embodiments, the RPTK is an FGFR, such as FGFR1 or FGFR2, and the ligand is an FGF, preferably FGF1 or FGF2. In particularly preferred embodiments, the polypeptide comprises residues 150–360 of FGFR1 or residues 150–360 of FGFR2 the sequences of which are shown in FIG. 4. The ligand may counterpart protein or a mimic thereof. For example, where the RPTK includes the extracellular binding domain of FGFR1 or FGFR2, the ligand can be a fibroblast growth factor, such as an FGF1 including the amino acid sequence as shown in FIG. 17 or an FGF2 including the amino acid sequence as shown in FIG. 17.

The term “D2-D3 region” as used herein refers to the second and third Ig-like domains of an FGFR1 The term “Ig-like domain” is well known to those of skill in the art. In certain embodiments, the D2-D3 region of the invention may not comprise the entire second and third Ig-like domains, but contain sufficient residues to provide a binding site for the ligand of the FGFR. Most preferably, the term “D2-D3 region” refers to proteins which include residues 150–360 of human FGFR1.

The term “mutant” refers to a polypeptide which is obtained by replacing at least one amino acid residue in a native RPTK or polypeptide ligand with a different amino acid residue. Mutation can also be accomplished by adding and/or deleting amino acid residues within the native polypeptide or at the N- and/or C-terminus of a polypeptide. Preferably, a mutant polypeptide has substantially the same three-dimensional structure as the native polypeptide.

The term “having substantially the same three-dimensional structure” as used herein refers to a set of atomic structure coordinates that have a root mean square deviation (r.m.s.d.) of less than or equal to about 2 Å when superimposed with the atomic structure coordinates of the native polypeptide from which the mutant is derived, when at least about 50% to 100% of the Cα atoms of the native tyrosine kinase are included in the superposition.

In another aspect, the invention relates to a crystalline form of an RPTK extracellular domain bound to a ligand defined by the structural coordinates set forth in Table 1 or Table 2.

The term “atomic structural coordinates” as used herein refers to a data set that defines the three dimensional structure of a molecule or molecules. Structural coordinates can be slightly modified and still render nearly identical three dimensional structures. A measure of a unique set of structural coordinates is the root-mean-square deviation of the resulting structure. Structural coordinates that render three dimensional structures that deviate from one another by a root-mean-square deviation of less than about 1.5 Å may be viewed by a person of ordinary skill in the art as identical. Hence, the structural coordinates set forth in Tables 1–4 and 6 are not limited to the values defined therein.

The use of X-ray crystallography can elucidate the three dimensional structure of crystalline forms of the invention. Typically, the first characterization of crystalline forms by X-ray crystallography can determine the unit cell shape and its orientation in the crystal. The term “unit cell” refers to the smallest and simplest volume element of a crystal that is completely representative of the unit of pattern of the crystal. The dimensions of the unit cell are defined by six numbers: dimensions a, b and c and angles α, β and γ. A crystal can be viewed as an efficiently packed array of multiple unit cells. Detailed descriptions of crystallographic terms are described in Hahn, 1996, The International Tables for Crystallography, Volume A, Fourth Edition, Kluwer Academic Publishers; and Shmueli, The International Tables for Crystallography, Volume B, First Edition, Kluwer Academic Publishers.

In another aspect, the invention features a crystalline form of a polypeptide corresponding to the D2-D3 region of a receptor PTK extracellular domain bound to a ligand or ligand analog, where the crystal is characterized by having tetragonal unit cells and space group symmetry P4₁2₁2. In preferred embodiments, the RPTK is an FGFR, preferably FGFR1, and the ligand is an FGF, preferably FGF2. In particularly preferred embodiments, the polypeptide includes residues 150–360 of FGFR1 or residues 150–360 of FGFR2, the sequences of which are shown in FIG. 4. Most preferably, the invention features a crystalline form of FGFR1 D2-D3 bound to FGF2, where the tetragonal unit cells of the crystal have dimensions of about a=98.5 Å, b=98.5 Å, c=197.0 Åand β=90°.

In yet another aspect, the invention features a crystalline form of a polypeptide corresponding to the D2-D3 region of a receptor PTK extracellular domain bound to a ligand or ligand analog, where the crystal is characterized by having tetragonal unit cells and space group symmetry β1. In preferred embodiments, the RPTK is an FGFR, preferably FGFR1, and the ligand is an FGF, preferably FGF1. In particularly preferred embodiments, the polypeptide comprises residues 150–360 of FGFR1 or residues 150–360 of FGFR2, the sequences of which are shown in FIG. 4. Most preferably, the invention features a crystalline form of FGFR1 D2-D3 bound to FGF1, where the tetragonal unit cells of the crystal have dimensions of about a=62.55 Å, b=64.06 Å, c=64.14 Å, α=93.40°, β=111.17°, and γ=97.18°.

In yet another aspect, the invention features a crystalline form of a polypeptide corresponding to the D2-D3 region of a receptor PTK extracellular domain bound to a ligand or ligand analog, where the crystal is characterized by having triclinic unit cells and space group symmetry β1. In preferred embodiments, the RPTK is an FGFR, such as FGFR2, and the ligand is an FGF, such as FGF2. In particularly preferred embodiments, the polypeptide comprises residues 150–360 of FGFR2, the sequence of which are shown in FIG. 4, and FGF2 has the sequence set forth in FIG. 17. For example, there is a crystalline form of FGFR2 D2-D3 bound to FGF2 having triclinic unit cells with dimensions of about a=72.20 Å, b=71.68 Å, c=90.92 Å, α=90.53°, β89.98°, and γ89.99°.

The term “space group” refers to the symmetry of a unit cell. In a space group designation (e.g., P4₁2₁2, or P1) the capital letter indicates the lattice type and the other symbols represent symmetry operations that can be carried out on the unit cell without changing its appearance.

The term “lattice” in reference to crystal structures refers to the array of points defined by the vertices of packed unit cells.

The term “symmetry operations” refers to geometrically defined ways of exchanging equivalent parts of a unit cell, or exchanging equivalent molecules between two different unit cells. Examples of symmetry operations are screw axes, centers of inversion, and mirror planes.

By “isolated” in reference to a polypeptide is meant a polymer of, for example, 6, 12, 18 or more amino acids linked to each other by chemical (e.g., peptide) bonds, including polypeptides that are isolated from natural or recombinant sources or that are chemically synthesized. The isolated polypeptides of the present invention are unique in the sense that they are not found in a pure or separated state in nature. Use of the term “isolated” indicates that a naturally occurring sequence, or an analog thereof, has been removed from its normal cellular environment. Thus, the sequence may be in a cell-free solution or placed in a different cellular environment. The term does not imply that the sequence is the only amino acid chain present, but that it is essentially free (about 90–95% pure at least) of other material.

The term “enriched” as used herein in reference to a polypeptide refers to a specific amino acid sequence constituting a significantly higher fraction of the total of polypeptides present in the cells or solution of interest than in the cells or solution from which the sequence was taken. Preferably, a polypeptide is enriched about 2-fold, about 3-fold, about 5-fold, about 10-fold, about 20-fold, about 50-fold, or about 100-fold. Enrichment may be effected by preferential reduction in the amount of other polypeptides, or by a preferential increase in the amount of the specific polypeptide of interest, or by a combination of the two. However, it should be noted that “enriched” does not imply that there are no other polypeptides present, just that the relative amount of the polypeptide of interest has been significantly increased. The term “significant” here is used to indicate that the level of increase is useful to the person making such an increase, and generally means an increase relative to other amino acids of about at least 2 fold, more preferably about 2-fold, about 3-fold, about 5-fold, about 10-fold, about 20-fold, about 50-fold, about 100-fold, or more.

It is also advantageous for some purposes that an amino acid sequence be in purified form. The term “purified” as used herein in reference to a polypeptide does not refer to absolute purity (such as a homogeneous preparation); instead, it refers to a polypeptide that is relatively purer than in the natural environment. Preferably, a polypeptide is purified about 2-fold, about 3-fold, about 5-fold, about 10-fold, about 20-fold, about 50-fold, or about 100-fold. Most preferably, purification of at least one order of magnitude, preferably two or three orders, and more preferably four or five orders of magnitude is expressly contemplated. In preferred embodiments, the substance is free of contamination at a functionally significant level.

In another aspect, the invention features a method for creating crystalline forms described herein. The method may utilize the polypeptides described herein to form a crystal.

The method comprises the steps of:

(a) mixing a volume of polypeptide solution with a reservoir solution; and

(b) incubating the mixture obtained in step (a) over the reservoir solution in a closed container, under conditions suitable for crystallization.

Preferably, the polypeptide solution comprises about 1 mg/ml to about 50 mg/ml of the polypeptide to be crystallized, and most preferably about 1 mg/ml, 2 mg/ml, 5 mg/ml, about 10 mg/ml, about 15 mg/ml, about 20 mg/ml, about 25 mg/ml, about 30 mg/ml, about 35 mg/ml, about 40 mg/ml, about 45 mg/ml, and about 50 mg/ml. The polypeptide solution is preferably buffered to between about pH 6.5 and about pH 9.5, most preferably about pH 8.5. In preferred embodiments, the solution also comprises salt, preferably in the form of KCl or NaCl, between about 1 mM and about 500 mM, most preferably about 150 mM. In certain embodiments, the reservoir solution preferably comprises between about 0.5 and about 3 M ammonium sulfate, most preferably about 1.6 M ammonium sulfate, and between about 5% and about 50% glycerol, most preferably 20% glycerol. In other embodiments, the reservoir solution preferably comprises between about 5% and about 50% polyethylene glycol, and most preferably about 20%, and between 0.05 M and 0.5 M Li₂SO₄, most preferably about 0.2 M. The reservoir solution is preferably buffered to between about pH 6.5 and about pH 9.5, and most preferably about pH 8.5. These processes are described in detail in the section entitled “Detailed Description of the Invention.”

In another aspect, the invention features a three dimensional representation of a structure of an RPTK extracellular domain, alone or in complex with a ligand or ligand analog. In preferred embodiments, the invention features a three dimensional representation of a structure of the D2-D3 region of a receptor PTK extracellular domain bound to a ligand or ligand analog. In preferred embodiments, the RPTK is an FGFR, such as FGFR1 or FGFR2, and the ligand is an FGF, preferably FGF1 or FGF2. In one group of preferred embodiments, the polypeptide comprises residues 150–360 of FGFR1 or residues 150–360 of FGFR2, the sequences of which are shown in FIG. 4. The ligand can be a fibroblast growth factor, such as an FGF1 including the amino acid sequence as shown in FIG. 17 or an FGF2 including the amino acid sequence as shown in FIG. 17.

The term “three dimensional representation” as used herein refers to any non-natural representation of one or more molecules which utilize a three dimensional coordinate space. The skilled artisan will recognize that the atomic structural coordinates in Tables 1–4 and 6, for example, use a three dimensional coordinate space, and thus are three dimensional representations. In preferred embodiments, a three dimensional representation can be a model prepared from the atomic coordinates of one or more molecules. In particularly preferred embodiments, a three dimensional representation can be a model prepared from the atomic coordinates of one or more molecules that exists in a computer's memory and/or that is displayed on a computer's screen. The coordinates disclosed herein provide the skilled person with the information needed to study molecular structures and interactions. Comparable data can be obtained by crystallizing the molecules in view of the teachings contained herein and conducting x-ray analysis in accordance with the teachings contained herein. Such data so obtained are within the scope of the present invention. Moreover, variations made to the data contained herein are within the scope of the present invention.

In another aspect, the invention features a recombinant DNA encoding an RPTK extracellular domain. For example, the recombinant DNA can include a coding strand which includes a nucleotide sequence coding for amino acid residues 150–360 of FGFR1 or residues 150–360 of FGFR2, the sequences of which are shown in FIG. 4.

In yet another aspect, the invention relates to methods of determining three dimensional structures of RPTK extracellular domains with unknown structure by utilizing known atomic structural coordinates of an RPTK extracellular domain. These methods can relate to homology modeling, molecular replacement, and nuclear magnetic resonance methods.

In preferred embodiments, the invention relates to a method of determining three dimensional structures of RPTK extracellular domains with unknown structures by homology modelling. These methods use the known atomic structural coordinates of an RPTK extracellular domain in conjunction with the amino acid sequences of receptor PTKs having unknown three dimensional structures. The methods comprise the steps of: (a) aligning an amino acid sequence of an RPTK with unknown structure with that of an RPTK with known atomic structural coordinates, where alignment is achieved by matching homologous regions of the amino acid sequences; (b) transferring the atomic structural coordinates of each of the homologous amino acids from the known atomic structural coordinates to a computer representation of a structure of the corresponding amino acids in the RPTK sequence with unknown structure; and (c) determining low energy conformations of the resulting RPTK structure.

Preferably, the known atomic structural coordinates are of an RPTK extracellular domain bound to a ligand or ligand analog. More preferably, the known atomic structural coordinates are of an FGFR extracelluar domain, preferably FGFR1, bound to an FGF, preferably FGF1 or FGF2. Most preferably, the known atomic structural coordinates are the coordinates set forth in Table 1 or Table 2.

The term “amino acid sequence” describes the order of amino acids in the amino acid chain comprising a polypeptide corresponding to all or a portion of an RPTK. In preferred embodiments, the amino acid sequence describes the order of amino acids in all or a portion of the extracellular domain of an RPTK.

The term “aligning” describes matching the beginning and the end of two or more amino acid sequences. Homologous amino acid sequences are placed on top of one another during the alignment process.

The term “homologous” as used herein in reference to protein sequences describes amino acids in two sequences that are identical or have similar side-chain chemical groups (e.g., aliphatic, aromatic, polar, negatively charged, or positively charged). Thus, protein sequences of similarity sufficient to indicate relation by a common origin or archetype are considered to possess homology, for instance. Examples of homologous amino acids are provided below.

The term “corresponding” refers to an amino acid that is aligned with another in the sequence alignment mentioned above.

The term “determining the low energy conformation” describes a process of changing the conformation of the RPTK structure such that the structure is of low free energy. The RPTK structure may or may not have a molecule(s), such as a ligand or ligand analog, bound to it.

The term “low free energy” describes a state where the molecules are in a stable state as measured by the process. A stable state is achieved when favorable interactions are formed within the complex.

The term “favorable interactions” refers to, among other things, hydrophobic, aromatic, and ionic forces, and hydrogen bonds.

The term “compound” refers to an organic molecule. The term “organic molecule” refers to a molecule which has at least one carbon atom in its structure. The compound can have a molecular weight of less than 6 kDa. Both the geometry of the compound and the interactions formed between the compound and the polypeptide preferably govern high affinity binding between the two molecules. High affinity binding is preferably governed by a dissociation equilibrium constant on the order of 10⁻⁶ M or less

The term “binding site” refers to a location on an enzyme or polypeptide chain to which one or more molecules may bind. In preferred embodiments, a binding site can be a ligand binding site, a HSPG binding site, or an interaction surface between two receptors which form a dimer upon ligand binding.

The term “interactions” refers to hydrophobic, aromatic, and ionic forces and hydrogen bonds formed between atoms. Such interactions can be “intramolecular,” or within the same molecule, or “intermolecular,” or between separate molecules.

The term “cofactor” refers to a compound that may, in addition to the substrate, bind to a protein and undergo a chemical reaction. Multiple co-factors are nucleotides or nucleotide derivatives, such as phosphate and nicotinamide derivatives of adenosine.

The term “substrate” refers to a compound that reacts with an enzyme. Enzymes can catalyze a specific reaction on a specific substrate. For example, RPTKs can phosphorylate specific protein and peptide substrates on tyrosine moieties. In addition, nucleotides can act as substrates for protein kinases.

The term “substrate analog” refers to a compound that is structurally similar, but not identical, to a substrate. The substrate analog may be a nucleotide analog. Examples of nucleotide analogs are described below.

The term “allosteric effector” refers to a compound that causes allosteric interactions in a protein. The term “allosteric interactions” refers to interactions between separate sites on a protein. The sites can be different from the active site. The allosteric effector can enhance or inhibit catalytic activity by binding to a site that may be different than the active site.

The term “co-crystal” refers to a crystal where the polypeptide is in association with one or more compounds.

The term “ATP” refers to the chemical compound adenosine triphosphate.

The term “non-hydrolyzable” refers to a compound having a covalent bond that does not readily react with water. Examples of non-hydrolyzable analogs of ATP are AMP-PNP and AMP-PCP, whose structures are well known to those skilled in the art.

The term “AMP-PNP” refers to adenylyl imidodiphosphate, a non-hydrolyzable analog of ATP.

The term “AMP-PCP” refers to adenylyl diphosphonate, a non-hydrolyzable analogue of ATP.

“Alkyl” refers to a straight-chain, branched or cyclic saturated aliphatic hydrocarbon. Preferably, the alkyl group has 1 to 12 carbons. More preferably, it is a lower alkyl of from 1 to 7 carbons, more preferably 1 to 4 carbons. Typical alkyl groups include methyl, ethyl, propyl, isopropyl, butyl, isobutyl, tertiary butyl, pentyl, hexyl and the like. The alkyl group may preferably be optionally substituted with one or more substituents selected from the group consisting of hydroxyl, cyano, alkoxy, ═O, ═S, NO₂, halogen, N(CH₃)₂ amino, and SH.

“Alkenyl” refers to a straight-chain, branched or cyclic unsaturated hydrocarbon group containing at least one carbon—carbon double bond. Preferably, the alkenyl group has 2 to 12 carbons. More preferably it is a lower alkenyl of from 2 to 7 carbons, more preferably 2 to 4 carbons. The alkenyl group may preferably be optionally substituted with one or more substituents selected from the group consisting of hydroxyl, cyano, alkoxy, ═O, ═S, NO₂, halogen, N(CH₃)₂ amino, and SH.

“Alkynyl” refers to a straight-chain, branched or cyclic unsaturated hydrocarbon containing at least one carbon—carbon triple bond. Preferably, the alkynyl group has 2 to 12 carbons. More preferably it is a lower alkynyl of from 2 to 7 carbons, more preferably 2 to 4 carbons. The alkynyl group may preferably be optionally substituted with one or more substituents selected from the group consisting of hydroxyl, cyano, alkoxy, ═O, ═S, NO₂, halogen, N(CH₃)₂ amino, and SH.

“Alkoxy” refers to an “O-alkyl” group.

“Aryl” refers to an aromatic group which has at least one ring having a conjugated pi-electron system and includes carbocyclic aryl, heterocyclic aryl and biaryl groups. The aryl group may preferably be optionally substituted with one or more substituents selected from the group consisting of halogen, trihalomethyl, hydroxyl, SH, OH, NO₂, amine, thioether, cyano, alkoxy, alkyl, and amino.

“Alkaryl” refers to an alkyl that is covalently joined to an aryl group. Preferably, the alkyl is a lower alkyl.

“Carbocyclic aryl” refers to an aryl group wherein the ring atoms are carbon.

“Heterocyclic aryl” refers to an aryl group having from 1 to 3 heteroatoms as ring atoms, the remainder of the ring atoms being carbon. Heteroatoms include oxygen, sulfur, and nitrogen. Thus, heterocyclic aryl groups include furanyl, thienyl, pyridyl, pyrrolyl, N-lower alkyl pyrrolo, pyrimidyl, pyrazinyl, imidazolyl and the like.

“Amide” refers to —C(O)—NH—R, where R is alkyl, aryl, alkylaryl or hydrogen.

“Thioamide” refers to —C(S)NH—R, where R is alkyl, aryl, alkylaryl or hydrogen.

“Amine” refers to a —N(R′)R″ group, where R′ and R″ are independently selected from the group consisting of alkyl, aryl, and alkylaryl.

“Thioether” refers to —S—R, where R is alkyl, aryl, or alkylaryl.

“Sulfonyl” refers to —S(O—R, where R is aryl, C(CN)═C-aryl, CH₂CN, alkylaryl, sulfonamide, NH-alkyl, NH-alkylaryl, or NH-aryl.

The term “acyl” denotes groups —C(O)R, where R is alkyl as defined above, such as formyl, acetyl, propionyl, or butyryl.

In other preferred embodiments, the invention relates to methods of determining three dimensional structures of RPTK extracellular domains with unknown structures by applying the known atomic structural coordinates of an RPTK extracellular domain to incomplete X-ray crystallographic data sets for RPTK extracellular domains having unknown three dimensional structures. The methods comprise the steps of: (a) determining the positions of atoms in the unit cell by matching diffraction data from two crystals, where one data set is from a crystal comprising an RPTK of unknown structure and the other is from a crystal comprising an RPTK having known atomic structural coordinates; and (b) determining a low energy conformation of the resulting RPTK structure.

Preferably, the complete diffraction data is from a crystal of an RPTK extracellular domain bound to a ligand or ligand analog. More preferably, the complete diffraction data is from a crystal of an FGFR extracelluar domain, preferably FGFR1, bound to an FGF, preferably FGF1 or FGF2.

The diffraction data set from the crystal comprising an RPTK of unknown structure may be a complete data set or an incomplete data set. The term “incomplete data set” as used herein relates to a X-ray crystallographic data set that does not have enough information to give rise to a three dimensional structure.

In other preferred embodiments, the invention relates to methods of determining three dimensional structures of receptor PTK extracellular domains with unknown structure by applying the known atomic structural coordinates of an RPTK extracellular domain to nuclear magnetic resonance (NMR) data of RPTK extracellular domains having unknown three dimensional structures. The methods comprise the steps of: (a) determining the secondary structure of an RPTK extracellular domain of unknown three dimensional structure using NMR data; and (b) simplifying the assignment of through-space interactions of amino acids using the known atomic structural coordinates of an RPTK. The RPTK extracellular domain of unknown three dimensional structure may or may not be complexed with compounds, ligands or modulators.

Preferably, the known atomic structural coordinates are of an RPTK extracellular domain bound to a ligand or ligand analog. More preferably, the known atomic structural coordinates are of an FGFR extracelluar domain, preferably FGFR1, bound to an FGF, preferably FGF1 or FGF2. Most preferably, the known atomic structural coordinates are the coordinates set forth in Table 1 or Table 2.

The term “secondary structure” describes the arrangement of amino acids in a three dimensional structure, such as in α-helix or β-sheet elements.

The term “through-space interactions” defines the orientation of the secondary structural elements in the three dimensional structure and the distances between amino acids from different portions of the amino acid sequence.

The term “assignment” defines a method of analyzing NMR data and identifying which amino acids give rise to signals in the NMR spectrum.

In another aspect, the invention features methods of identifying potential modulators of PTK function. By identifying one or more potential modulators from a larger group of molecules, it is possible to reduce the number of molecules that must be tested using costly and time-consuming biological assays. Thus, the methods described herein for identifying potential modulators of PTK function can provide increased efficiencies in identifying actual modulators of PTK function.

These potential modulators are preferably identified by docking a three dimensional representation of a structure of a compound with a three dimensional representation of the RPTK extracellular domain. The computer representation of the RPTK extracellular domain can be defined by atomic structural coordinates. In certain embodiments, one or more modulators are docked into the ligand binding site of the RPTK extracellular domain, and/or into the binding site for heparin sulfate-containing proteoglycans (HSPGs) of the RPTK extracellular domain.

In preferred embodiments, the method of identifying potential modulators of RPTK function comprises the steps of: (a) providing a three dimensional representation of the atomic structural coordinates of an RPTK and docking a three dimensional representation of a compound from a computer data base with the three dimensional representation of the RPTK; (b) determining a conformation of the resulting complex having a favorable geometric fit and favorable complementary interactions; and (c) identifying compounds that best fit the RPTK as potential modulators of RPTK function. The initial RPTK structure may or may not have one or more compounds, ligands, or modulators bound to it.

Preferably, the atomic structural coordinates are of an RPTK extracellular domain bound to a ligand or ligand analog. More preferably, the atomic structural coordinates are of an FGFR extracelluar domain, preferably FGFR1, bound to an FGF, preferably FGF1 or FGF2. Most preferably, the atomic structural coordinates are the coordinates set forth in Table 1 or Table 2.

The term “modulator of RPTK function” as used herein refers to a compound or ligand analog which alters the catalytic activity of an RPTK. A modulator of RPTK function can either stimulate or inhibit RPTK catalytic activity. For example, inhibitory modulators may be one or more compounds or ligand analogs that disrupt dimerization of an RPTK, prevent dimerization of an RPTK, or prevent binding of an RPTK to its ligand or to HSPGs. Alternatively, a stimulatory modulator may be one or more compounds or ligand analogs that stabilize dimer formation, or mimic the activity of the ligand of an RPTK, or mimic the activity of HSPGs.

The term “chemical group” refers to moieties that can form hydrogen bonds, hydrophobic, aromatic, or ionic interactions.

The term “docking” refers to a process of placing a compound, ligand or ligand analog in close proximity with an RPTK. In certain embodiments, docking can refer to placing a three dimensional representation of the compound, ligand, or ligand analog in close proximity with a three dimensional representation of the RPTK. The term can also refer to a process of finding low energy conformations of the resulting compound/RPTK, ligand/RPTK, or ligand analog/RPTK complex.

The term “favorable geometric fit” refers to a conformation of the compound/RPTK, ligand/RPTK, or ligand analog/RPTK complex where the surface area of the compound, ligand, or ligand analog is in close proximity with a surface of the RPTK-site without forming unfavorable interactions. Unfavorable interactions can be steric hindrances between atoms in the bound molecule and atoms in the RPTK.

The term “favorable complementary interactions” relates to hydrophobic, aromatic, ionic, and hydrogen bond donating, and hydrogen bond accepting forces formed between the compound, ligand, or ligand analog and the RPTK.

The term “potential” qualifies the term “modulator of RPTK function” because the potential modulator of RPTK function may not yet have been tested for activity in vitro or in vivo.

The term “best fit” describes compounds, ligands, or ligand analogs that complexed the most surface area and/or form the most favorable complementary interactions with the receptor PTK in a given experiment. The term “best fit” can also refer to a subset of compounds, ligands, or ligand analogs from amongst a larger group of compounds, ligands, or ligand analogs which complex the most surface area and/or form the most favorable complementary interactions with the receptor PTK. In preferred embodiments, a molecule which exhibits a best fit is in the 70^(th) percentile or better of molecules tested in terms of complexing the most surface area and/or forming the most favorable complementary interactions, more preferably a molecule which exhibits a best fit is in the 80^(th) percentile or better of molecules tested, and most preferably, a molecule which exhibits a best fit is in the 90^(th) percentile or better of molecules tested.

Other preferred embodiments of the invention are methods of identifying potential modulators of receptor PTK function. The method involves utilizing a three dimensional structure of a receptor PTK. The method comprises the steps of: (a) modifying a three dimensional representation of a receptor PTK having one or more compounds, ligands, or ligand analogs bound to it, where the three dimensional representations of the compounds, ligands, or ligand analogs and the receptor PTK are defined by atomic structural coordinates; (b) determining a conformation of the resulting complex having a favorable geometric fit and favorable complementary interactions; and (c) identifying the compounds, ligands, or ligand analogs that best fit the receptor PTK active-site as potential modulators of receptor PTK function.

Preferably, the atomic structural coordinates are of an RPTK extracellular domain bound to a ligand or ligand analog. More preferably, the atomic structural coordinates are of an FGFR extracelluar domain, preferably FGFR1, bound to an FGF, preferably FGF1 or FGF2. Most preferably, the atomic structural coordinates are the coordinates set forth in Table 1 or Table 2.

The term “modifying” refers to replacing, deleting, or adding one or more chemical groups. Computer representations of the chemical groups can be selected from a computer data base.

Yet another preferred embodiment of the invention is a method of identifying potential modulators of RPTK function by operating modulator construction or modulator searching computer programs on the compounds, ligands, or ligand analogs complexed with the RPTK. The method comprises the steps of: (a) providing a three-dimensional representation of one or more compounds, ligands, or ligand analogs complexed with an RPTK, where the computer representations of the compounds, ligands, or ligand analogs and the receptor PTK are defined by atomic structural coordinates; and (b) searching a data base for compounds, ligands, or ligand analogs similar to the compounds, ligands, or ligand analogs using a compound searching computer program, or replacing portions of the compounds, ligands, or ligand analogs complexed with the RPTK with similar chemical structures from a data base using a compound construction computer program, where the representations of the compounds are defined by structural coordinates. The skilled artisan will recognize that a number of suitable computer programs are available for compound searching and construction, including UNITY™ (Tripos, Inc.) and CATALYST® (MSI, Inc.)

Preferably, the atomic structural coordinates are of an RPTK extracellular domain bound to a ligand or ligand analog. More preferably, the atomic structural coordinates are of an FGFR extracelluar domain, preferably FGFR1, bound to an FGF, preferably FGF1 or FGF2. Most preferably, the known atomic structural coordinates are the coordinates set forth in Table 1 or Table 2.

The term “operating” as used herein refers to utilizing the three-dimensional conformation of molecules defined by the processes described herein in various computer programs.

The terms “similar compound,” “similar ligand,” and “similar ligand analog” refer to a compound, ligand, or ligand analog that has a similar geometric structure as compounds, ligands, or ligand analogs that can bind to a receptor PTK. The similar molecule can also have similar chemical groups as a molecule that is either bound to an RPTK or once bound to an RPTK. The similar chemical groups can form complementary interactions with the RPTK.

The term “compound searching computer program” describes a computer program that searches computer representations of compounds, ligands, or ligand analogs from a computer data base that have similar three dimensional structures and similar chemical groups as a compound of interest.

The term “similar chemical structures” as used herein refers to one or more chemical groups that share similar a similar geometry with one or more portions of another molecule. In preferred embodiments, a similar chemical structure shares a similar geometry with a molecule that is in a complex with an RPTK, or shares a similar geometry with a molecule that has been removed from an RPTK structure. Similar chemical structures can also refer to chemical groups that can form one or more complementary interactions with an RPTK that are similar to those formed between and an RPTK and a complexed molecule.

The term “replacing structures” refers to removing one or more portions of a molecule that is in a complex with an RPTK, or removing one or more portions of a molecule that has been removed from an RPTK, and connecting the broken bonds to produce a similar molecule.

The term “compound construction computer program” describes a computer program that replaces computer representations of chemical groups in a compound, ligand, or ligand analog with groups from a computer data base.

The term “similar three dimensional structure” describes two molecules with nearly identical shape and volume.

The methods for using the crystalline forms and three dimensional structures of the invention can relate to a broad range of protein kinases. Thus, in preferred embodiments, the invention relates to an RPTK. The RPTK is preferably PDGFR, EGFR, SCFR, VEGFR, HGFR, neurotrophinR, HER2, HER3, HER4, InsulinR, IGFR, CSFIR, FLK, KDR, VEGFR2, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, MUSK, members of the FGFR family, such as FGFR1, FGFR2, FGFR3, and FGFR4, or an orphan receptor PTK.

In another aspect, the invention features a potential modulator of RPTK function identified by methods disclosed in the invention.

Another aspect of the invention is a method for synthesizing a potential modulator of RPTK function or its pharmaceutically acceptable salts, isomers, metabolites, esters, amides, or prodrugs by a standard synthetic method known in the art. Synthetic procedures are discussed below.

In another aspect, the invention features methods for identifying a modulator of RPTK function. The method comprises the steps of: (a) administering a potential modulator of RPTK function, ligand, ligand analog, or compound to cells; (b) comparing the level of RPTK phosphorylation between cells not administered the potential modulator, ligand, ligand analog, or compound and cells administered the potential modulator; and (c) identifying the potential modulator, ligand, ligand analog, or compound as a modulator of RPTK function based on the difference in the level of receptor PTK phosphorylation. The skilled artisan will recognize that the difference in PTK phosphorylation required for a potential modulator, ligand, ligand analog, or compound to be identified as a modulator of RPTK function will depend on the particular RPTK, the specificity of the modulator, the nature of the disorder associated with the RPTK function, etc.

The term “cells” refers to any type of cells either primary or cultured. Primary cells can be extracted directly from an organism while cultured cells rapidly divide and can be cultured in many successive rounds. Cells can be grown in a variety of containers including, but not limited to flasks, dishes, and well plates.

The term “administer,” as used in reference to cells, refers to a method of delivering a potential modulator, ligand, ligand analog, or compound to cells. The compound can be prepared using a carrier such as dimethyl sulfoxide (DMSO) in an aqueous solution. The aqueous solution comprising the compound, also termed an “aqueous preparation”, can be simply mixed into the medium bathing the layer of cells or microinjected into the cells themselves. The compounds may be administered to the cells using a suitable buffered solution.

The term “suitable buffered solution” refers to an aqueous preparation of the compound that comprises a salt that can control the pH of the solution at low concentrations. Because the salt exists at low concentrations, the salt preferably does not alter the function of the cells.

The term “RPTK phosphorylation” refers to the presence of phosphate on the RPTK. Phosphates on RPTKs can be identified by antibodies that bind them specifically with high affinity.

In another aspect, the invention features a method of identifying a potential modulator of RPTK function as a modulator of RPTK function. The method comprises the steps of: (a) administering a potential modulator of RPTK function to cells; (b) comparing the level of cell growth between cells not administered the potential modulator and cells administered the potential modulator; and (c) identifying the potential modulator as a modulator of RPTK function based on the difference in cell growth.

The term “cell growth” refers to the rate at which a group of cells divides. Cell division rates can be readily measured by methods utilized by those skilled in the art.

Another aspect of the invention features a method of diagnosing a disease by identifying cells harboring a RPTK with inappropriate activity. The method comprises the steps of: (a) administering a modulator of RPTK function to cells; (b) comparing the rate of cell growth between cells not administered the modulator and cells administered the modulator; and (c) diagnosing a disease by characterizing cells harboring a RPTK with inappropriate activity from the effect of the modulator on the difference in the rate of cell growth. The modulator can be identified by the methods of the invention.

The term “inappropriate activity” refers to an RPTK that regulates a step in a signal transduction process at a higher or lower rate than normal cells. Aberrations in the rate of signal transduction can be caused by alterations in the stimulation of an RPTK by a growth factor, alterations in the activity of RPTK-specific phosphatase, over-expression of a RPTK in a cell, or mutations in the catalytic region of the RPTK itself.

The term “signal transduction process” describes the steps in a cascade of events where an extracellular signal is transmitted into an intracellular signal.

The term “RPTK-specific phosphatase” describes an enzyme that dephosphorylates a particular RPTK and thereby regulates that RPTK's activity.

Another aspect of the invention is a method of treating a disease associated with a RPTK with inappropriate activity in a cellular organism, where the method comprises the steps of: (a) administering the modulator of RPTK function to the organism, where the modulator is in an acceptable pharmaceutical preparation; and (b) activating or inhibiting the RPTK function to treat the disease.

The term “organism” relates to any living being comprised of at least one cell. An organism can be as simple as one eukaryotic cell or as complex as a mammal.

The term “administering”, in reference to an organism, refers to a method of introducing the compound to the organism. The compound can be administered when the cells or tissues of the organism exist within the organism or outside of the organism. Cells existing outside the organism can be maintained or grown in cell culture dishes. For cells harbored within the organism, many techniques exist in the art to administer compounds, including (but not limited to) oral, parenteral, dermal, ocular, subcutaneous, and rectal applications. For cells outside of the patient, multiple techniques exist in the art to administer the compounds, including (but not limited to) cell microinjection techniques, transformation techniques, and carrier techniques.

The term “pharmaceutically acceptable composition” refers to a preparation comprising the modulator of RPTK activity. The composition is acceptable if it does not appreciably cause irritations to the organism administered the compound.

In preferred embodiments of the of the invention, the receptor PTK is selected from the group consisting of PDGFR, SCFR, EGFR, VEGFR, HGFR, neurotrophinR, HER2, HER3, HER4, InsulinR, IGFR, CSFIR, FLK, KDR, VEGFR2, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, MUSK, members of the FGFR family, such as FGFR1, FGFR2, FGFR3, and FGFR4, and orphan receptor PTKs.

The summary of the invention described above is non-limiting and other features and advantages of the invention will be apparent from the following detailed description, and from the claims.

BRIEF DESCRIPTION OF THE FIGURES

FIG. 1 provides a ribbon diagram of the structure of a dimer of FGFR1 D2-D3 complexed with FGF2. Two views are related by a rotation of about 90° about the vertical axis. The D2 and D3 domains are shown in green and blue, respectively, the short linker connecting D2 and D3 is shown in gray, and the FGF2 molecules are shown in orange.

FIG. 2 provides a ribbon diagram of the structure of FGFR1 D2-D3 complexed with FGF1. The D2 and D3 domains are shown in green and blue, respectively, the short linker connecting D2 and D3 is shown in gray, and FGF1 is shown in orange.

FIG. 3 provides a topology diagram of the Ig folds of FGFR1 D2 and D3 in comparison to the Ig fold of telokin.

FIG. 4 provides a sequence alignment of the D2-D3 region of human FGFR1, FGFR2, FGFR3, and FGFR4.

FIG. 5 shows ribbon diagrams of the FGF1-FGFR1 and FGF2-FGFR2 complexes with the Ig-like domains 2 (D2) and 3 (D3) are shown in green and cyan, respectively. The short linker that connects D2 and D3 is colored gray. FGF 1 and FGF2 are shown in orange. The secondary structure assignments for FGFR1 and FGFR2 were obtained with the program PROCHECK (Laskowski et al., J. Appl. Cryst., 26,283–291 (1993)). The beta strands for D2 and D3 are labeled according to the strand nomenclature for the canonical I-set member telokin. The helix between betaA and betaA′, gA, is a 3₁₀ helix. In both FGF1-FGFR1 and FGF2-FGFR2 structures, the betaC-betaC′ loops in D3 are disordered. In addition, most of the segment between betaC′ and betaE in D3 of FGF1-FGFR1 is disordered as well. In the FGF2-FGFR2 structure, this segment is well ordered and is colored purple. The amino- and carboxy-termini are denoted by NT and CT. The disulfide bonds in D2 and D3 are shown in ball-and-stick rendering with sulfur atoms colored yellow. The beta strands of FGF1 are labeled from 1 to 12 according to published nomenclature (Faham et al., Curr. Opin. Struct. Biol. 8, 578–586 (1998)). This figure was created using the programs Molscript (Kraulis, J. Appl. Crystallogr. 24,946–950(1991)) and Raster3D (Merrit et al., Methods Enzymol. 277, 505–524 (1997)).

FIG. 6 shows Space-filling models of the FGF1-FGFR1 and FGF2-FGFR2 complexes. The view and the coloring for D2, D3, the linker and FGFs are the same as in FIG. 5. To better visualize the binding interfaces on FGFs and on FGFRs, the molecules are pulled away from each other and rotated 90° about the vertical axis as indicated (left and right panels). Residues in FGF1 and FGF2 are colored with respect to the FGFR regions with which they interact. FGF1 and FGF2 residues that interact with D2 are colored green, residues that interact with the linker region are colored gray, and residues that interact with D3 are colored cyan. FGF2 residues that interact with the betaC′-betaE segment (shown in purple) of FGFR2 are colored red. The residues in FGFR1 and FGFR2 that interact with FGF1 and FGF2, respectively, are colored orange. In addition, in the FGF2-FGFR2 structure, receptor residues in the betaC′-betaE segment that contact FGF2 are in red. Ligand and receptor residues are considered to be in the FGF-FGFR interface if at least one pair of atoms (side chain or main chain) has an inter-atomic distance of 3.8 Å or less. This figure was created using the programs Molscript and Raster3D.

FIG. 7 shows a stereo view of detailed interactions in the hydrophobic interface between FGF2 and D2 of FGFR2

FIG. 8 shows a stereo view of detailed interactions in the hydrophobic interface between between FGF1 and D2 of FGFR1.

FIG. 9 shows a stereo view of detailed interactions of the conserved network of hydrogen bonds between FGF2 and FGFR2 in the vicinity of Arg251 in the D2-D3 linker.

FIG. 10 shows a stereo view of detailed interactions the network of hydrogen bonds between FGF1 and FGFR1 in the vicinity of Arg250 in the D2-D3 linker.

FIG. 11 shows a stereo view of detailed interactions in the interface between FGF2 and the betaF-betaG loop of D3 in the FGF2-FGFR2 structure. At the right side of each stereo pair, a view of the whole structure in the exact orientation as in stereo views is shown and the region of interest is highlighted. Only side chains of interacting residues are shown. Color coding is the same as in FIG. 7. Dotted lines represent hydrogen bonds.

FIG. 12 shows a stereo view of detailed interactions in the interface between N-terminal sequences (prior to beta1) of FGF2 and D3 in the FGF2-FGFR2 structure. Views and coding are the same as in FIG. 11.

FIG. 13 shows a stereo view of detailed interactions in the interface between FGF2 and the betaC′-betaE segment (shown in purple) of D3 in the FGF2-FGFR2 structure. Views and coding are the same as in FIG. 11.

FIG. 14 shows a stereo view of detailed interactions in the interface between FGF1 and D3 in the FGF1-FGFR1 structure. Views and coding are the same as in FIG. 11.

FIG. 15 shows Structure-based sequence alignment of the ligand binding domains of D2 and D2-D3 linker of human FGF receptors (SEQ ID NOS 5–8, respectively).

FIG. 16 shows Structure-based sequence alignment of the ligand binding domains of D3 of human FGF receptors (SEQ ID NOS 9–16, respectively).

FIG. 17 shows structure-based sequence alignment of FGFs (SEQ ID NOS 17–35, respectively, in order of appearance) performed using the CLUSTALW program (Thompson et al., Nucleic Acids Res. 22, 4673–4680 (1994)). All of the FGFs used in this alignment are from human, with the exception of FGF15, for which only the chicken sequence is available. The secondary structure assignment is according to the published nomenclature, with the beta strands labeled from 1 through 12 (Faham et al., Curr. Opin. Struct. Biol. 8, 578–586 (1998)). The location and the length of the beta strands are shown on the top of the sequence alignment. FGF residues are colored with respect to the region on FGFR with which they interact: FGF residues that interact with D2 are colored green, residues that interact with the linker region are colored gray, and residues that interact with D3 are colored cyan. FGF residues that interact with the betaC′-betaE segment in D3 are colored red. A period indicates sequence identity to FGF2. A dash represents a gap introduced to optimize the alignment. A tilde at the C-terminus of FGF indicates that there are additional sequences down stream to the last amino acid shown. A star indicates that numbering does not start at the initiation methionine. Residue numbering for FGF2 is according to Springer et al., J. Biol. Chem. 269, 26879–26884 (1994). Residue numbering for FGF1 is according to Zhu et al., Science 251, 90–93 (1991). A checkmark indicates FGF residues that have been shown by mutagenesis to be important for receptor binding.

FIG. 18 depicts the locations of the mutations in the human FGFR2 gene that lead to skeletal disorders are mapped onto a ribbon representation the FGF2-FGFR2 structure. Side chains of the residues are colored with respect to the type of substitution. In yellow are mutations that substitute a cysteine with another amino acid or vice versa, resulting in the creation of unpaired cysteines. In red are mutations that are expected to destabilize the tertiary structure of D3 and thus disfavor the formation of the correct intra-domain disulfide bridge. In green are mutations that are predicted to affect ligand-binding affinity or specificity.

FIG. 19 depicts the overall structure of SCF (constructed by Molscript and Raster3D (Kraulis, J. Appl. Crystallogr. 24, 946–950 (1991); Merrit et al., Methods Enzymol. 277, 505–524 (1991))) and its relation with other cytokines by showing a ribbon representation of the SCF structure, in two views related by a rotation of approximately 90°. The termini and secondary structures are labeled; the strands are rendered as arrows, the helices as ribbons, and the loop regions as tubes. The two-fold axis is marked with a diamond.

FIG. 20 depicts the sequence alignment based on secondary structures of SCF, M-CSF and IL-5 (SEQ ID NOS 36–44, respectively, in order of appearance). Secondary structure assignments for M-CSF and IL-5 are from PDB databank. beta-Strands are yellow and helices are marked bright green.

FIG. 21 shows a stereo view of the dimeric interface of SCF constructed by Molscript and Raster3D (Kraulis, J. Appl. Crystallogr. 24, 946–950 (1991); Merrit et al., Methods Enzymol. 277, 505–524(1991)). For clarity, only side-chains of residues at the core of the interface are shown. The coding of the secondary structures is the same as used in FIG. 19, the strands are rendered as arrows, the helices as ribbons, and the loop regions as tubes.

FIG. 22 shows 2Fo-Fc electron density created by O (Jones et al., Acta Crystallogr. A 47, 110–119 (1991)), contoured at 1.2, for the hydrogen bond circle of Tyr26 and Asp25′ at the dimeric interface.

FIG. 23 depicts a model of covalent SCF dimer constructed by Molscript and Raster3D (Kraulis, J. Appl. Crystallogr. 24, 946–950 (1991); Merrit et al., Methods Enzymol. 277, 505–524 (1991)). The non-covalent (native) dimer is on the left and a model for the covalent SCF dimer is on the right. Each protomer is colored either orange or green. The disulfide bonds are shown in ball-and-stick with sulfur atoms colored in yellow.

FIG. 24 depicts a potential binding site on SCF for c-kit and a model of SCF:SCFR complex created by GRASP Nicolls et al., Proteins 11, 281–296 (1991)). The molecular surface of SCF and proposed c-kit binding regions, in two views related by a rotation of approximately 90° are shown. A hydrophobic crevice at both tails is colored yellow. Two basic patches are colored blue and the acidic patch is colored red.

FIG. 25 shows sequence alignments of human, rat, mouse, dog and pig SCFs (SEQ ID NOS 45–49, respectively). Residues of the acidic patch are colored red and residues of the two basic patches are colored blue. Stars mark amino acid residues that are altered in rodents. The secondary structures are marked below the sequences with ‘H’ representing helices and ‘E’ representing beta strands.

FIG. 26 shows a proposed model of the SCF in complex with Ig-like domains 2–5 of the extracellular domain of c-kit (labeled D2 to D5) created by GRASP (Nicolls et al., Proteins 11, 281–296 (1991)). The SCF dimer is represented in a worm model and the c-kit model by a molecular surface.

FIG. 27 depicts an electron density map of decasaccharides soaked into preformed crystals of an FGF2-FGFR1 complex showing the location of decasaccharides in the dimeric assemblage. Only the Cα traces of D2s (cyan) and FGFs (orange) are shown. The decasaccharides are rendered in white sticks.

FIG. 28 depicts a stereoview of an FoFc electron density map of an FGF2-FGFR1 complex shown in FIG. 27 computed after simulated annealing with decasaccharide omitted from the atomic model. The map is computed at 3.0 Å resolution and contoured at 1.8 σ. Sugar rings are labeled A through H starting at the non-reducing end of the decasaccharide. Atom coloring is as follows: oxygens in red, sulfurs in yellow, nitrogens in blue, and carbons in gray. This figure was constructed using Bobscript (Esnouf, J. Mol. Graph. Model 15, 132–134 (1997). FIG. 29 shows a stereoview of the detailed interactions between ordered decasaccharide rings (A–F), FGF and FGFR. Only the side chains of interacting residues are shown. The two D2s of the adjoining FGFRs are colored cyan and green respectively. Atom coloring is the same as in FIG. 27. The carbon atoms in FGFRs have the same coloring as the D2 to which they belong. Dotted lines represent hydrogen bonds.

FIG. 30 shows a schematic diagram of interactions between decasaccharide (heparrin), FGF and FGFR in the ternary complex. Only the relevant functional groups and backbone atoms of the interacting amino acids are shown. Dashed lines represent hydrogen bonds. Hashed lines represent hydrophobic interactions. The sugar rings of heparin are labeled A through F starting at the non-reducing end. The backbone carbon atoms of heparin are numbered according to IUPAC nomenclature. The type and the number of interacting residues are colored based on the molecule to which they belong.

FIG. 31 shows the results of a separation on a Superdex 200 column (Pharmacia) of dimer formation for a set of mixtures of various ratios of homogeneously-sulfated hexasaccharide with purified 1:1 FGF1-FGFR2 complex. The following reaction mixture were used: A, control (no hexasaccharide added); B, hexasaccharide:FGF1-FGFR2 complex molar ratio of 0.5:1; C, hexasaccharide:FGF1-FGFR2 complex molar ratio of 1:1; D, and hexasaccharide:FGF1-FGFR2 complex molar ratio of 2.85:1. The positions of monomers and dimers are indicated by the letters “M” and “D” respectively. The letter “T” shows the position of the tight monomeric ternary 1:1:1 hexasaccharide: FGF1:FGFR2 complex. The letter “L” shows the position of free FGF1.

FIG. 32 depicts a molecular surface representation of the “two end” model of the dimeric 2:2:2 FGF2-FGFR1-heparin ternary complex. The view is from the top (same view as FIG. 27) looking down into the heparin-binding canyon. The FGF2 surface is shown in orange and D2 in green. Only the first 6 sugar rings of the decasaccharides are rendered in ball-and-stick and the non-reducing and reducing ends are labeled.

FIG. 33 shows a schematic illustration of a computer based system which can be used for displaying, studying, comparing, manipulating, interpreting and/or extrapolating data from the crystallographic analysis of molecular structures, such as the molecular structures of RPTKs, their ligands and related complexes.

BRIEF DESCRIPTION OF THE CRYSTALLOGRAPHIC ATOMIC STRUCTURAL COORDINATES

The crystallographic structural coordinates are located at the end of the section entitled “Examples” and before the claims. Table 1 provides the atomic structure coordinates of crystals of FGFR1-D2-D3 complexed with FGF2 of the invention as determined by X-ray crystallography. Table 2 provides the atomic structure coordinates of crystals of FGFR1-D2-D3 complexed with FGF1 of the invention as determined by X-ray crystallography. Table 4 provides the atomic structure coordinates of crystals of an SCF (1–141) non-covalent homodimer. Table 6 provides the atomic structure coordinates of crystals of a dimeric 2:2:2 FGF2:FGFR1:heparin ternary complex.

The columns (from left to right) in these tables are descriptions of the atoms by number and type, amino acid and number containing the atom, the x coordinate, y coordinate, z coordinate, bond connectivity, and temperature factor. All of these parameters are well defined in the art.

DETAILED DESCRIPTION OF THE INVENTION

The present invention is directed to the determination and use of three dimensional structures of receptor protein tyrosine kinases. The three dimensional structures of receptor PTKs can facilitate the design and identification of modulators of receptor PTK function.

Protein tyrosine kinases (PTKs) comprise a large and diverse class of enzymes. Schlessinger and Ullrich, 1992, Neuron 9: 383–391. The PTK family is subdivided into members that are receptors and those that are non-receptors. The receptor PTK (RPTK) family contains multiple subfamilies, one of which is the fibroblast growth factor receptor (FGFR) PTK which is a molecule implicated in regulating angiogenesis a well as cellular proliferation and differentiation. Givol and Yayon, 1992, FASEB J. 6 (15): 3362–3369.

FGFR1 through FGFR4, are known as “high affinity FGFRs,” due to the ability to bind fibroblast growth factors with a high affinity. These high affinity FGFRs are characterized by an extracellular ligand-binding domain which comprises three immunoglobulin (IG)-like domains (known as D1 through D3), a single transmembrane helix, and a cytoplasmic domain containing tyrosine kinase activity. See Lee et al., 1989, Science 245: 57–60; Jaye et al., 1992, J. Mol. Biol. 227: 840–851; Johnson & Williams, 1993, Adv. Cancer. Res. 60: 1–41. FGFRs can mediate cellular functions by their role in one or more cellular signal transduction processes. Cellular signal transduction processes comprise a cascade of multiple steps that convert an extracellular signal into an intracellular signal.

RPTK-mediated signal transduction is initiated by binding of a specific extracellular ligand to the extracellular domain, followed by receptor dimerization, and subsequent autophosphorylation of the RPTK. Preferred ligands are epidermal growth factors, insulin, platelet-derived growth factors, vascular endothelial growth factors, fibroblast growth factors, hepatocyte growth factors, and neurotrophins. The FGF subfamily presently contains about 18 members, named FGF1 through FGF18, which bind to FGFRs, and to HSPGs. Those skilled in the art can identify presently unknown members of the FGF subfamily by sequence homology to known subfamily members, and/or by the presence of a common protein fold. Each of the four high affinity FGFRs binds to a specific subset of FGFs. Ornitz et al., 1996, J. Biol. Chem. 271: 15292–15297.

Once an RPTK is autophosphorylated, the phosphate groups are binding sites for intracellular signal transduction molecules which leads to the formation of protein complexes at the cell membrane. These complexes facilitate an appropriate cellular effect (e.g., cell division, metabolic effects to the extracellular microenvironment) in response to the ligand that began the cascade of events.

RPTKs function as binding sites for several intracellular proteins. Intracellular RPTK binding proteins are divided into two principal groups: (1) those which harbor a catalytic domain; and (2) those which lack such a domain but serve as adapters and associate with catalytically active molecules. Songyang et al., 1993, Cell 72:767–778. SH2 (src homology) domains are common adaptors found in proteins which directly bind to the RPTK. SH2 domains are harbored by RPTK binding proteins of both groups mentioned above. Fantl et al., 1992, Cell 69:413423; Songyang et al., 1994,Mol. Cell. Biol. 14:2777–2785); Songyang et al., 1993, Cell 72:767–778; and Koch et al., 1991, Science 252:668–678.

The specificity of the interactions between RPTKs and the SH2 domains of their binding proteins is determined by the amino acid residues immediately surrounding the phosphorylated tyrosine residue. Differences in the binding affinities of SH2 domains is correlated with the observed differences in substrate phosphorylation profiles of downstream molecules in the signal transduction process. Songyang et al., 1993, Cell 72:767–778. These observations suggest that the function of each RPTK is determined not only by its pattern of expression and ligand availability but also by the array of downstream signal transduction pathways that are activated by a particular receptor. Thus, RPTKs provide a controlling regulatory role in signal transduction processes as a consequence of autophosphorylation.

RPTK-mediated signal transduction regulates cell proliferative, differentiation, and metabolic responses in cells. Therefore, inappropriate RPTK activity can result in a wide array of disorders and diseases. These disorders, which are described below, may be treated by the modulators of RPTK function designed or identified by the methods disclosed herein.

The present invention also relates to crystalline polypeptides corresponding to the extracellular domain of receptor tyrosine kinases. Such receptor protein tyrosine kinases are not covalently cross-linked, but are understood to undergo ligand-induced dimerization. Preferably, the crystalline extracellular domains are of sufficient quality to allow for the determination of a three-dimensional X-ray diffraction structure to a resolution of about 1.5 Å to about 3 Å, and most preferably about 2.8 Å. The invention also relates to methods for preparing and crystallizing the polypeptides. The polypeptides themselves, as well as information derived from their crystal structures can be used to analyze and modify tyrosine kinase activity as well as to identify compounds that interact with the extracellular domain.

The polypeptides of the invention are most preferably designed on the basis of the structure of a region in the extracellular domain of the RPTKs that contains the ligand binding domain. By way of illustration, FIG. 4 shows the amino acid sequence alignment of the ligand binding D2-D3 domains of human FGFR1, FGFR2, FGFR3, and FGFR4. The applicants have discovered and determined the boundaries of the extracellular domain required for crystallization of the resulting polypeptide. Surprisingly, these boundaries are very similar to a naturally occurring variant of FGFR1 which retains approximatly full ligand binding capacity and specificity. See Johnson et al., Mol Cell. Biol., 1990 10: 4728–4736.

The resulting crystal structures consists of a unit cell comprising a dimer of two FGFR1 D2-D3 domains, each bound to an FGF molecule. The dimeric structure is stabilized by interactions between the two D2 domains, and by interactions between the FGF molecule in one member of the dimer and the D2 domain of the other member of the dimer. These contacts which stabilize the dimeric structure within the crystal are believed to be similar or identical to contacts which result in dimerization and activation of FGFR1 in vivo. Thus, the crystal structures of the invention provides for the first time a detailed view of the events leading to ligand-induced dimerization and activation of RPTKs.

The crystal structures also disclose a possible role for the acid box region of the extracellular domain of RPTKs in dimerization and activation. The acid box is a continuous stretch of acidic residues in the linker between D1 and D2. Models inferred from the crystal structures of the invention imply that the acid box may interact with the heparin binding region of D2, competing with heparin for binding. Surprisingly, these models imply that loss of the of the acid box/D2 interaction may permit heparin-induced dimerization and activation of FGFR1 in the absence of FGF.

The understanding of dimerization and activation at the atomic level can allow the design of modulators of RPTK function, for example molecules which contribute to or disrupt receptor/ligand binding or intradimer contacts. Such modulators may provide useful treatments for various RPTK diseases.

I. PTK Associated Diseases

PTK-associated diseases and disorders include, but are not limited to, blood vessel proliferative disorders, fibrotic disorders, and mesangial cell proliferative disorders. Blood vessel proliferative disorders refer to angiogenic and vasculogenic disorders generally resulting in abnormal proliferation of blood vessels. The formation and spreading of blood vessels play important roles in a variety of physiological processes such as embryonic development, corpus luteum formation, wound healing and organ regeneration. They also play a pivotal role in cancer development, for example in Kaposi's sarcoma. Other examples of blood vessel proliferation disorders include arthritis, where new capillary blood vessels invade the joint and destroy cartilage, ocular diseases, like diabetic retinopathy, where new capillaries in the retina invade the vitreous, bleed and cause blindness, and von Hippel-Lindau disease (VHL), which is characterized by a predisposition for retinal angiomas, hemangioblastomas in the central nervous system, renal cell carcinomas, pheochromocytomas, and islet cell tumors of the pancreas. Conversely, disorders related to the shrinkage, contraction or closing of blood vessels are implicated in such diseases as restenosis.

Fibrotic disorders refer to the abnormal formation of extracellular matrix. Examples of fibrotic disorders include hepatic cirrhosis and mesangial cell proliferative disorders. Hepatic cirrhosis is characterized by the increase in extracellular matrix constituents resulting in the formation of a hepatic scar. Hepatic cirrhosis can cause diseases such as cirrhosis of the liver. An increased extracellular matrix resulting in a hepatic scar can also be caused by viral infection such as hepatitis.

Mesangial cell proliferative disorders refer to disorders brought about by abnormal proliferation of mesangial cells. Mesangial proliferative disorders include various human renal diseases, such as glomerulonephritis, diabetic nephropathy, malignant nephrosclerosis, thrombotic microangiopathy syndromes, transplant rejection, and glomerulopathies. The PDGF-R has been implicated in the maintenance of mesangial cell proliferation. Floege et al., 1993, Kidney International 43:47S–54S.

RPTKs are directly associated with the cell proliferative disorders described above. For example, some members of the RPTK family have been associated with the development of cancer. Some of these receptors, like EGFR (Tuzi et al., 1991, Br. J. Cancer 63:227–233; Torp et al., 1992, APMIS 100:713–719) HER2/neu (Slamon et al., 1989, Science 244:707–712) and PDGF-R (Kumabe et al., 1992, Oncogene 7:627–633) are over-expressed in many tumors and/or persistently activated by autocrine loops. In fact, RPTK over-expression (Akbasak and Suner-Akbasak et al., 1992, J. Neurol. Sci. 111:119–133; Dickson et al., 1992, Cancer Treatment Res. 61:249–273; Korc et al., 1992, J. Clin. Invest. 90:1352–1360) and autocrine loop stimulation (Lee and Donoghue, 1992, J. Cell. Biol. 118:1057–1070; Korc et al., supra; Akbasak and Suner-Akbasak et al., supra) account for the most common and severe cancers. For example, EGFR is associated with squamous cell carcinoma, astrocytoma, glioblastoma, head and neck cancer, lung cancer and bladder cancer. HER2 is associated with breast, ovarian, gastric, lung, pancreas and bladder cancer. PDGFR is associated with glioblastoma, lung, ovarian, and prostate cancer. The RPTK c-met is generally associated with hepatocarcinogenesis and thus hepatocellular carcinoma. Additionally, c-met is linked to malignant tumor formation. More specifically, c-met has been associated with, among other cancers, colorectal, thyroid, pancreatic and gastric carcinoma, leukemia and lymphoma. Additionally, over-expression of the c-met gene has been detected in patients with Hodgkin's disease, Burkitt's disease, and the lymphoma cell line.

The IGF-I RPTK, in addition to being implicated in nutritional support and in type-II diabetes, is also associated with several types of cancers. For example, IGF-I has been implicated as an autocrine growth stimulator for several tumor types, e.g. human breast cancer carcinoma cells (Arteaga et al., 1989, J. Clin. Invest. 84:1418–1423) and small lung tumor cells (Macauley et al., 1990, Cancer Res. 50:2511–2517). In addition, IGF-I, integrally involved in the normal growth and differentiation of the nervous system, appears to be an autocrine stimulator of human gliomas. Sandberg-Nordqvist et al., 1993, Cancer Res. 53:2475–2478. The importance of the IGF-R and its modulators in cell proliferation is further supported by the fact that many cell types in culture (fibroblasts, epithelial cells, smooth muscle cells, T-lymphocytes, myeloid cells, chondrocytes, osteoblasts, the stem cells of the bone marrow) are stimulated to grow by IGF-I. Goldring and Goldring, 1991, Eukaryotic Gene Expression 1:301–326. A series of recent publications suggest that IGF-R plays a central role in the mechanisms of transformation and, as such, could be a preferred target for therapeutic interventions for a broad spectrum of human malignancies. Baserga, 1995, Cancer Res. 55:249–252; Baserga, 1994, Cell 79:927–930; Coppola et al., 1994, Mol. Cell. Biol. 14:45884595.

The association between abnormalities in RPTKs and disease are not restricted to cancer, however. For example, RPTKs are associated with metabolic diseases like psoriasis, diabetes mellitus, wound healing, inflammation, and neurodegenerative diseases. EGFR is indicated in corneal and dermal wound healing. Defects in InsulinR and IGFR are indicated in type-II diabetes mellitus. A more complete correlation between specific RPTKs and their therapeutic indications is set forth in Plowman et al., 1994, DN&P 7:334–339.

The instant invention is directed in part towards designing modulators of RPTK function that could indirectly kill tumors by cutting off their source of sustenance. Normal vasculogenesis and angiogenesis play important roles in a variety of physiological processes such as embryonic development, wound healing, organ regeneration and female reproductive processes such as follicle development in the corpus luteum during ovulation and placental growth after pregnancy. Folkman and Shing, 1992, J. Biological Chem. 267:10931–34. However, many diseases are driven by persistent unregulated or inappropriate angiogenesis. For example, in arthritis, new capillary blood vessels invade the joint and destroy the cartilage. In diabetes, new capillaries in the retina invade the vitreous, bleed and cause blindness. Folkman, 1987, in: Congress of Thrombosis and Haemostasis (Verstraete, et. al, eds.), Leuven University Press, Leuven, pp. 583–596. Ocular neovascularization is the most common cause of blindness and dominates approximately twenty (20) eye diseases.

Moreover, vasculogenesis and/or angiogenesis can be associated with the growth of malignant solid tumors and metastasis. A tumor must continuously stimulate the growth of new capillary blood vessels for the tumor itself to grow. Furthermore, the new blood vessels embedded in a tumor provide a gateway for tumor cells to enter the circulation and to metastasize to distant sites in the body. Folkman, 1990, J. Natl. Cancer Inst. 82:4–6; Klagsbrunn and Soker, 1993, Current Biology 3:699–702; Folkman, 1991, J. Natl., Cancer Inst. 82:4–6; Weidner et al., 1991, New Engl. J. Med. 324:1–5.

Several polypeptides with in vitro endothelial cell growth promoting activity have been identified. Examples include acidic and basic fibroblastic growth factor (αFGF, βFGF), vascular endothelial growth factor (VEGF) and placental growth factor. Unlike αFGF and βFGF, VEGF has recently been reported to be an endothelial cell specific mitogen. Ferrara and Henzel, 1989, Biochem. Biophys. Res. Comm. 161:851–858; Vaisman et al., 1990, J. Biol. Chem. 265:19461–19566.

Thus, identifying the specific receptors that bind FGF or VEGF is important for understanding endothelial cell proliferation regulation. Two structurally related receptor PTKs that bind VEGF with high affinity are identified: the flt-1 receptor (Shibuya et al, 1990, Oncogene 5:519–524; De Vries et al., 1992, Science 255:989–991) and the KDR/FLK-1 receptor (VEGFR2), discussed in the U.S. patent application Ser. No. 08/193,829. In addition, a receptor that binds FGF is identified. Jaye et al., 1992, Biochem. Biophys. Acta 1135:185–199). Consequently, these RPTKs most likely regulate endothelial cell proliferation.

FGFRs play important roles in angiogenesis, wound healing, embryonic development, and malignant transformation. Basilico and Moscatelli, 1992, Adv. Cancer Res. 59:115–165. Four high affinity mammalian FGFRs (FGFR14) have been described and additional diversity is generated by alternative RNA splicing within the extracellular domains. Jaye et al., 1992, Biochem. Biophys. Acta 1135:185–199. Like other RPTKs, dimerization of FGF receptors is essential for their activation. Soluble or cell surface-bound heparin sulfate proteoglycans act in concert with FGF to induce dimerization (Schlessinger et al., 1995, Cell 83:357–360), which leads to autophosphorylation of specific tyrosine residues in the cytoplasmic domain. Mohammadi et al., 1996, Mol. Cell Biol. 16:977–989.

Mutations in three human FGF receptor genes, FGFR1, FGFR2, and FGFR3, have been implicated in a variety of human genetic skeletal disorders. Mutations in FGFR1 and FGFR2 result in the premature fusion of the flat bones of the skull and cause the craniosynostosis syndromes, such as Apert (FGFR2) (Wilkie et al., 1994, Nat. Genet. 8:269–274), Pfeiffer (FGFR1 and FGFR2) (Muenke et al., 1994, Nat. Genet. 8:269–274), Jackson-Weiss (FGFR2) (Jabs et al., 1994, Nat. Genet. 8:275–279) and Crouzon (FGFR2) (Jabs et al., 1994, Nat. Genet. 8:275–279) syndromes. In contrast, mutations in FGFR3 are implicated in long bone disorders and cause several clinically related forms of dwarfism including achondroplasia (Shiang et al., 1994, Cell 78:335–342), hypochondroplasia (Bellus et al., 1995, Nat. Genet. 10:357–359) and the neonatal lethal thanatophoric dysplasia (Tavormina et al., 1995, Nat. Genet. 9:321–328). It has been shown that these mutations lead to constitutive activation of the tyrosine kinase activity of FGFR3 (Webster et al., 1996, EMBO J. 15:520–527). Furthermore gene-targeting experiments in mice have revealed an essential role for FGFR3 in developmental bone formation (Deng et al., 1996, Cell 84:911–921).

Another major role proposed for FGFs in vivo is the induction of angiogenesis (Folkman and Klagsbrun, 1987, Science 236:442). Therefore, inappropriate expression of FGFs or of their receptors or aberrant function of the tyrosine kinase activity could contribute to several human angiogenic pathologies such as diabetic retinopathy, rheumatoid arthritis, atherosclerosis and tumor neovascularization (Klagsbrun and Edelman, 1989, Arteriosclerosis 9:269). Moreover, FGFs are thought to be involved in malignant transformation. Indeed, the genes coding for the three FGF homologues int-2, FGF-5 and hst-1/K-fgf were originally isolated as oncogenes. Furthermore, the cDNA encoding FGFR1 and FGFR2 are amplified in a population of breast cancers (Adnane et al., 1991, Oncogene 6:659–663). Over-expression of FGF receptors has been also detected in human pancreatic cancers, astrocytomas, salivary gland adenosarcomas, Kaposi's sarcomas, ovarian cancers and prostate cancers.

Evidence, such as the disclosure set forth in copending U.S. application Ser. No. 08/193,829, strongly suggests that VEGF is not only responsible for endothelial cell proliferation, but also is a prime regulator of normal and pathological angiogenesis. See generally, Klagsburn and Soker, 1993, Current Biology 3:699–702; Houck et al., 1992, J. Biol. Chem. 267:26031–26037. Moreover, it has been shown that KDR/FLK-1 and flt-I are abundantly expressed in the proliferating endothelial cells of a growing tumor, but not in the surrounding quiescent endothelial cells. Plate et al., 1992, Nature 359:845–848; Shweiki et al., 1992, Nature 359:843–845.

The invention is directed to designing and identifying modulators of RPTK functions that could modify the inappropriate activity of a RPTK involved with a clinical disorder. The rational design and identification of modulators of RPTK functions can be accomplished by utilizing the structural coordinates that define a RPTK three dimensional structure.

II. Modulators of PTK functions as Therapeutics for Disease

As a consequence of the disorders discussed above, scientists in the biomedical community are searching for modulators of RPTK functions that down-regulate signal transduction pathways associated with inappropriate RPTK activity.

Several small molecule modulators of RPTK functions have been identified which can traverse the cell membrane and do not hydrolyze in acidic environments. For example, bis monocyclic, bicyclic or heterocyclic aryl compounds (PCT WO 92/20642), vinylene-azaindole derivatives (PCT WO 94/14808) 1-cyclopropyl-4-pyridyl-quinolones (U.S. Pat. No. 5,330,992), styryl compounds (U.S. Pat. No. 5,217,999), styryl-substituted pyridyl compounds (U.S. Pat. No. 5,302,606), certain quinazoline derivatives (EP Application No. 0 566 266 A1), seleoindoles and selenides (PCT WO 94/03427), tricyclic polyhydroxylic compounds (PCT WO 92/21660), and benzylphosphonic acid compounds (PCT WO 91/15495) are described as RPTK inhibitors.

Although some modulators of RPTK function are known, many of these are not specific for RPTK subfamilies and will therefore cause multiple side-effects as therapeutics. Certain compounds of the oxindolinone/thiolindolinone family, however, are believed to be specific for the FGF receptor subfamily (U.S. patent application Ser. No. 08/702,232, filed Aug. 23, 1996, invented by Tang et al., entitled “Indolinone Combinatorial Libraries and Related Products and Methods for the Treatment of Disease”). In addition, compounds of the oxindolinone/thiolindolinone family are non-hydrolyzable in acidic conditions and can be highly bioavailable. These modulators of RPTK function, however, target the catalytic domain of the FGFR subfamily, and thus are not directed towards affecting receptor RPTK dimerization and activation via inteactions in the extracellular domain.

III. Crystalline Tyrosine Kinases

Crystalline RPTKs of the invention include native crystals, derivative crystals and co-crystals. The native crystals of the invention generally comprise substantially pure polypeptides corresponding to the extracellular domain of an RPTK in crystalline form. In preferred embodiments, the crystals of the invention comprise polypeptides corresponding to the extracellular domain of an RPTK in a complex with a ligand.

It is to be understood that the crystalline extracellular domains of the invention are not limited to naturally occurring or native extracellular domains. Indeed, the crystals of the invention include mutants of native extracellular domains. Mutants of native extracellular domains are obtained by replacing at least one amino acid residue in a native extracellular domain with a different amino acid residue, or by adding or deleting amino acid residues within the native polypeptide or at the N- or C-terminus of the native polypeptide, and have substantially the same three-dimensional structure as the native extracellular domain from which the mutant is derived.

Similarly, in certain embodiments in which the extracellular domain is bound to a ligand, the crystals of the invention include mutants of native extracellular domains and mutant ligands. As discussed above, mutant ligands can be obtained by replacing at least one amino acid residue in a polypeptide ligand with a different amino acid residue, or by adding or deleting amino acid residues within the native polypeptide or at the N- or C-terminus of the native polypeptide, and have substantially the same three-dimensional structure as the native ligand from which the mutant is derived.

By having substantially the same three-dimensional structure is meant having a set of atomic structure coordinates that have a root-mean-square deviation (rmsd) of less than or equal to about 2A when superimposed with the atomic structure coordinates of the native extracellular domain and/or ligand from which the mutant is derived when at least about 50% to 100% of the Cα atoms of the polypeptide are included in the superposition. For example, FIG. 3 shows that 68 common Cα atoms in the D2 and D3 regions of FGFR1 and telokin, a canonical IG-fold polypeptide, can be superimposed with a rms deviation of 0.8 Å.

Amino acid substitutions, deletions and additions which do not significantly interfere with the three-dimensional structure of a polypeptide will depend, in part, on the region of the polypeptide where the substitution, addition or deletion occurs. In highly variable regions of the molecule, non-conservative substitutions as well as conservative substitutions may be tolerated without significantly disrupting the three-dimensional structure of the molecule. In highly conserved regions, or regions containing significant secondary structure, conservative amino acid substitutions may be preferred.

Conservative amino acid substitutions are well-known in the art, and include substitutions made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity and/or the amphipathic nature of the amino acid residues involved. For example, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; amino acids with uncharged polar head groups having similar hydrophilicity values include the following: leucine, isoleucine, valine; glycine, alanine; asparagine, glutamine; serine, threonine; phenylalanine, tyrosine. Other conservative amino acid substitutions are well known in the art.

For RPTK extracellular domains obtained in whole or in part by chemical synthesis, the selection of amino acids available for substitution or addition is not limited to the genetically encoded amino acids. Indeed, the mutants described herein may contain non-genetically encoded amino acids. Conservative amino acid substitutions for many of the commonly known non-genetically encoded amino acids are well known in the art. Conservative substitutions for other amino acids can be determined based on their physical properties as compared to the properties of the genetically encoded amino acids.

In some instances, it may be particularly advantageous or convenient to substitute, delete and/or add amino acid residues to a native extracellular domain in order to provide convenient cloning sites in a DNA, such as a cDNA, encoding the polypeptide, to aid in purification of the polypeptide, and for crystallization of the polypeptide. Such substitutions, deletions and/or additions which do not substantially alter the three dimensional structure of the native tyrosine kinase domain will be apparent to those of ordinary skill in the art.

It should be noted that the mutants contemplated herein need not exhibit ligand binding activity. Indeed, amino acid substitutions, additions or deletions that interfere with the ligand binding activity of the RPTK extracellular domain but which do not significantly alter the three-dimensional structure of the domain are specifically contemplated by the invention. Such crystalline polypeptides, or the atomic structure coordinates obtained therefrom, can be used to identify compounds or molecules that bind to the native domain. These compounds or molecules may affect the activity of the native domain.

The derivative crystals of the invention generally comprise a crystalline RPTK extracellular domain polypeptide in covalent association with one or more heavy metal atoms. The polypeptide may correspond to a native or a mutated tyrosine kinase domain. Heavy metal atoms useful for providing derivative crystals include, by way of example and not limitation, gold, mercury, etc.

The co-crystals of the invention generally comprise a crystalline RPTK extracellular domain polypeptide in association with one or more compounds or other molecules. The association may be covalent or non-covalent. Such molecules include, but are not limited to, ligands, ligand analogs, cofactors, substrates, substrate analogues, inhibitors, activators, allosteric effectors, polypeptides, etc.

IV. Three Dimensional Structure Determination Using X-ray Crystallography

X-ray crystallography is a method of solving the three dimensional structures of molecules. The structure of a molecule is calculated from X-ray diffraction patterns using a crystal as a diffraction grating. Three dimensional structures of protein molecules arise from crystals grown from a concentrated aqueous solution of that protein. The process of X-ray crystallography can include the following steps:

(a) synthesizing and isolating a polypeptide;

(b) growing a crystal from an appropriate solution comprising the polypeptide with or without a compound, modulator, ligand, or ligand analog; and

(c) collecting X-ray diffraction patterns from the crystals, determining unit cell dimensions and symmetry, determining electron density, fitting the amino acid sequence of the polypeptide to the electron density, and refining the structure.

Production of Polypeptides

The native and mutated tyrosine kinase domain polypeptides described herein may be chemically synthesized in whole or part using techniques that are well-known in the art (see, e.g., Creighton, 1983). Alternatively, methods which are well known to those skilled in the art can be used to construct expression vectors containing the native or mutated tyrosine kinase domain polypeptide coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro recombinant DNA techniques, synthetic techniques and in vivo recombination/genetic recombination. See, for example, the techniques described in Maniatis et al., 1989 and Ausubel et al., 1989.

A variety of host-expression vector systems may be utilized to express the RPTK extracellular domain coding sequence. These include but are not limited to microorganisms such as bacteria transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing the RPTK extracellular domain coding sequence; yeast transformed with recombinant yeast expression vectors containing the RPTK extracellular domain coding sequence; insect cell systems infected with recombinant virus expression vectors (e.g., baculovirus) containing the RPTK extracellular domain coding sequence; plant cell systems infected with recombinant virus expression vectors (e.g., cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV) or transformed with recombinant plasmid expression vectors (e.g., Ti plasmid) containing the RPTK extracellular domain coding sequence; or animal cell systems. The expression elements of these systems vary in their strength and specificities.

Depending on the host/vector system utilized, any of a number of suitable transcription and translation elements, including constitutive and inducible promoters, may be used in the expression vector. For example, when cloning in bacterial systems, inducible promoters such as pL of bacteriophage λ, plac, ptrp, ptac (ptrp-lac hybrid promoter) and the like may be used; when cloning in insect cell systems, promoters such as the baculovirus polyhedrin promoter may be used; when cloning in plant cell systems, promoters derived from the genome of plant cells (e.g., heat shock promoters; the promoter for the small subunit of RUBISCO; the promoter for the chlorophyll a/b binding protein) or from plant viruses (e.g., the 35S RNA promoter of CaMV; the coat protein promoter of TMV) may be used; when cloning in mammalian cell systems, promoters derived from the genome of mammalian cells (e.g., metallothionein promoter) or from mammalian viruses (e.g., the adenovirus late promoter; the vaccinia virus 7.5K promoter) may be used; when generating cell lines that contain multiple copies of the receptor PTK extracellular domain DNA, SV40-, BPV- and EBV-based vectors may be used with an appropriate selectable marker.

Methods describing methods of DNA manipulation, vectors, various types of cells used, methods of incorporating the vectors into the cells, expression techniques, protein purification and isolation methods, and protein concentration methods are disclosed in detail with respect to the protein PYK-2 in U.S. Pat. Nos. 5,837,524, 5,837,815, and PCT publication WO 96/18738, each of which is incorporated herein by reference in its entirety, including all claims, figures, and drawings. Those skilled in the art will appreciate that such descriptions are applicable to the present invention and can be easily adapted to it.

Crystal Growth

Crystals are grown from solutions containing the purified and concentrated polypeptide by a variety of techniques. These techniques include batch, liquid, bridge, dialysis, vapor diffusion, and hanging drop methods. McPherson, 1982, John Wiley, New York; McPherson, 1990, Eur. J. Biochem. 189:1–23; Webber, 1991, Adv. Protein Chem. 41:1–36, incorporated by reference herein in its entirety, including all figures, tables, and drawings.

Generally, the crystals of the invention are grown by adding precipitants to the concentrated solution of the polypeptide corresponding to the RPTK extracellular domain, with or without bound compound, modulator, ligand, or ligand analog. The precipitants are added at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.

For one of the exemplary crystals of the invention, it has been found that hanging drops containing about 2.0 μL of RPTK extracellular domain polypeptide with a bound ligand provide crystals suitable for high resolution X-ray structure determination. Preferably, crystals are grown by mixing equal volumes of protein solution (10 mg/mL in 25 mM Tris-HCl, pH 8.5, and 150 mM NaCl) and reservoir buffer (1.6 M (NH₄)₂SO₄, 20% v/v glycerol and 100 mM Tris-HCl, pH 8.5), and suspending a hanging drop of the resulting solution over 0.5 mL reservoir buffer at 20° C. In preferred embodiments, the protein solution comprises 10 mg/mL FGFR1 D2-D3 domain bound to an FGF2 molecule.

In another exemplary crystal of the invention, crystals are grown by mixing one volume of protein solution (1 mg/mL in 25 mM Tris-HCl, pH 8.5, and 150 mM NaCl) with four volumes of reservoir buffer (20% PEG 4000, 0.2 M Li2SO4, and 0.1 M Tris-HCl, pH 8.5), and suspending a hanging drop of the resulting solution over 0.5 mL reservoir buffer at 20° C. In preferred embodiments, the protein solution comprises 1 mg/mL FGFR1 D2-D3 domain bound to an FGF 1 molecule.

Those of ordinary skill in the art will recognize that the above-described crystallization conditions can be varied. Such variations may be used alone or in combination, and include polypeptide solutions containing polypeptide concentrations between about 1 mg/ml and about 50 mg/ml, Tris-HCl concentrations between about 10 mM and about 200 mM, dithiothreitol concentrations between about 0 mM and about 20 mM, pH ranges between about 5.5 and about 9.5; and reservoir solutions containing polyethylene glycol concentrations between about 10% and about 50% (w/v), polyethylene glycol molecular weights between about 1000 and about 20,000, (NH₄)₂SO₄ concentrations between about 0.1 M and about 2.5 M, ethylene glycol or glycerol concentrations between about 0% and about 20% (v/v), bis-Tris concentrations between about 10 mM and about 200 mM, pH ranges between about 5.5 and about 9.5 and temperature ranges between about 0° C. and about 25° C. Other buffer solutions may be used such as HEPES buffer, so long as the desired pH range is maintained.

Derivative crystals of the invention can be obtained by soaking native crystals in mother liquor containing salts of heavy metal atoms. It has been found that soaking a native crystal in a solution containing about 0.1 mM to about 5 mM thimerosal, 4-chloromeruribenzoic acid or KAu(CN)₂ for about 2 hr to about 72 hr provides derivative crystals suitable for use as isomorphous replacements in determining the X-ray crystal structure of the RPTK extracellular domain polypeptide.

Co-crystals of the invention can be obtained by soaking a native crystal in mother liquor containing one or more compounds, ligands, or ligand analogs that bind the receptor PTK extracellular domain, as described above, or can be obtained by co-crystallizing the RPTK extracellular domain polypeptide in the presence of one or more binding compounds, ligands, or ligand analogs.

Crystals comprising a polypeptide corresponding to a RPTK extracellular domain complexed with a compound, ligand, or ligand analog can be grown by one of two methods. In the first method, the compound, ligand, or ligand analog is added to the aqueous solution containing the polypeptide corresponding to the RPTK extracellular domain before the crystal is grown. In the second method, the compound, ligand, or ligand analog is soaked into an already existing crystal of a polypeptide corresponding to a RPTK extracellular domain.

Crystalline FGFR Extracellular Domain/FGF Complexes

The overall structures of the FGF1-FGFR1 and FGF2-FGFR2 complexes are similar to the previously determined FGF2-FGFR1 structure (FIG. 5) (Plotnikov et al., 1999). The FGFR ligand-binding domain consists of two Ig-like domains connected by a short linker. The three-dimensional folds of D2 and D3 in both the FGF1-FGFR1 and FGF2-FGFR2 structures resemble that of the I-set prototype member telokin, in which a β sandwich is formed by two layers of β sheets (Holden et al., 1992). A highly conserved disulfide bond is buried in the hydrophobic core of D2 and D3 and bridges the two β sheets. In both structures, the βC–βC′ loop in D3 is disordered (FIG. 5).

The main difference between the structures of FGF1-FGFR1 and FGF2-FGFR2 is the conformation of the segment connecting βC′ and PE in D3 (FIG. 5). In the FGF2-FGFR2 structure, this segment is well ordered and interacts with FGF2, while in the FGF1-FGFR1 structure, this segment is disordered and is not included in the atomic model. In the previously determined structure of FGF2-FGFR1, this segment is also well ordered and interacts with the ligand (Plotnikov et al., 1999). At the C-terminal end of this segment in the FGF2-FGFR1 structure, a short α helix (αD) has been assigned by PROCHECK (Laskowski et al., 1993). In the present FGF2-FGFR2 structure, the polypeptide chain at the C-terminal end adopts a very similar conformation, but is not assigned as a α helix.

It has previously been reported that both FGF1 and FGF2 adopt a β-trefoil fold which consists of three copies of a four-stranded antiparallel β sheet (FIG. 5). Superposition of receptor-bound FGF1 and FGF2 with the free FGF1 and FGF2 indicates that no significant conformational changes occur in FGF1 and FGF2 upon receptor binding. In addition, as with the crystal structures of free FGF1 and FGF2, ordered sulfate ions are found in the heparin-binding sites of both FGF1 and FGF2. As in the determined crystal structure of FGF2-FGFR1, the ligands in both the FGF1-FGFR1 and FGF2-FGFR2 structures interact with residues of the receptors in D2, in D3 and in the linker that connects D2 and D3 (FIG. 6).

In one illustrative embodiment, the invention provides crystals of FGFR1 D2-D3 domain bound to an FGF2 molecule. The D2-D3 domain of this embodiment consists of residues 142–365, and thus is missing the D1 domain, the acid box, and the linker between D3 and the transmembrane helix. Each D2-D3 domain is bound to a single FGF2 molecule. The crystals were obtained by the methods provided in the Examples. The FGFR1 D2-D3/FGF2 crystals, which may be native crystals, derivative crystals or co-crystals, have tetragonal unit cells (i.e., unit cells wherein a=b≠c) and space group symmetry P4₁2₁2. There are two FGFR1 D2-D3/FGF2 complexes in the asymmetric unit, related by an approximate two-fold axis. The unit cell has dimensions of a=b=98.5 Å, c=197.0 Å and β=90°.

The FGF-D2 Interface

The interface between FGF and D2 in both complexes is mainly hydrophobic (FIGS. 7 and 8). A solvent-exposed hydrophobic surface in FGF packs against a highly conserved hydrophobic surface at the bottom of D2 in FGFR. In the FGF2-FGFR2 structure, Tyr24, Leu140, and Met142 in FGF2 make hydrophobic contacts with Ala168 in FGFR2. Leu140, Tyr103 and the aliphatic portion of the Asn102 side chain in FGF2 make hydrophobic contacts with Pro 170 in FGFR2. Phe31 of FGF2 is engaged in hydrophobic interactions with Leu166 of FGFR2. Leu166, Ala168 and Pro170 of FGFR2 are located in βA′ at the bottom of D2. Val249, located in the C-terminal end of βG in D2, is also in the FGF2-D2 interface and interacts with Leu140 and Met142 in FGF2. Several hydrogen bonds further fortify the mainly hydrophobic FGF2-D2 interface: the hydroxyl group of Tyr24 in FGF2 forms two hydrogen bonds with backbone atoms of Leu166 and Ala168 in FGFR2, and Tyr103 makes a hydrogen bond via a water molecule with the backbone of Ala168.

The observed interactions between FGF2 and FGFR2 in the FGF2-D2 interface are entirely consistent with mutagenesis studies on FGF2. It is demonstrated that individual replacements with alanine of Tyr24, Tyr103, Leu140 and Met140, all of which located in the FGF2-D2 interface (FIG. 7), results in a large decrease in FGFR1 binding affinity (Springer et al., 1994).

Within each D2-D3/FGF2 complex of the illustrative embodiment, FGF2 interacts extensively with D2, D3, and the linker between the two domains. While a single hydrogen bond is noted between Tyr-24 in FGF2 and Leu-165 in FGFR1, the majority of interactions between D2 and FGF2 are hydrophobic. For example, hydrophobic contacts can be seen between Tyr-24 and Met-142 of FGF2 and Ala 167 of D2, between Asn-102, Tyr-103, and Leu-140 of FGF2 and Pro-169 of D2, and between Leu-140 of FGF2 and Val-248 of FGFR1. It is noteworthy that Ala 167, Pro-169, and Val-248 are conserved amongst FGFRs 1–4, and thus may represent a therapeutically important site in members of the FGFR subfamily.

Comparison of the FGF-D2 interfaces in the structures of FGF2-FGFR2 and FGF1-FGFR1 reveals a close similarity (FIGS. 7 and 8). FGF2 and FGF1 differ in only two positions in the FGF-D2 interface: Met142 in FGF2 is replaced by a homologous hydrophobic residue Leu135 in FGF1, and Asn102 in FGF2 is substituted by His93 in FGF1. However, this latter substitution may not affect the binding of FGF1 to D2, since only the aliphatic portion of this residue interacts with FGFR and not the actual functional group.

The FGF-Linker Interface

The D2-D3 linker is highly conserved among FGFRs (FIG. 15). The hydrogen bonds between FGFs and the linker region play a critical role in binding of FGFs to FGFRs (FIGS. 9 and 10). In the FGF2-FGFR2 structure, an invariant arginine located in the D2-D3 linker, Arg251 (in FGFR2), forms hydrogen bonds with the side chain of Asn104 and the backbone carbonyl oxygen of Asn102 (FIG. 9). Indeed, replacement of Asn104 in FGF2 with an alanine causes a 400-fold reduction in the binding affinity of FGF2 for FGFR1 (Zhu et al., 1997), revealing the importance of the interaction between Asn104 and FGFR.

A sequence alignment of the 19 available FGFs shows that the majority of FGFs have an asparagine in the position corresponding to Asn104 of FGF2 (FIG. 17). However, FGF8, FGF 17 and FGF 18 have a threonine residue at this position, whose side chain is shorter than asparagine. It is predicted that these FGFs will not form a direct hydrogen bond with the key linker arginine residue, and therefore will exhibit lower binding affinity towards FGFRs. Interestingly, FGF11, FGF 12, FGF13, and FGF14 have a valine in place of Asn104 of FGF2 (FIG. 17). This substitution is expected to cause a strong decrease in FGFR binding.

The hydrogen bond between Arg251 and FGF2 takes place in a hydrophobic pocket composed of the aliphatic side chains of highly conserved Val249 and Pro253 in FGFR2 and Leu98 and Pro141 in FGF2 (FIG. 9). The proximity to this hydrophobic environment will most likely stabilize this hydrogen bond. Moreover, the intramolecular hydrogen bonds between Arg251 and the invariant Asp283 in FGFR2 and Asn104 and Tyr106 in FGF2 serve to restrict the rotational freedom of the guanidium group of Arg251 and amide group of Asn104 (FIG. 9). These interactions may increase the ligand-binding affinity by lowering the entropy of FGF-FGFR complex formation. Indeed, substitution of Tyr106 with a phenylalanine in FGF2 caused a 5-fold reduction in receptor binding (Zhu et al., 1995).

The FGF-linker interfaces in both FGF1-FGFR1 and FGF2-FGFR2 structures are highly conserved (FIGS. 9 and 10). Moreover, the hydrophobic environment surrounding the critical hydrogen bond between FGFR-invariant linker arginine and FGF is nearly identical in both structures (FIGS. 9 and 10). A sequence alignment of all known members of the FGF and FGFR families, reveals that residues in FGF and FGFR that constitute the FGF-D2 and FGF-linker interfaces are conserved among the 4 mammalian FGFRs (FIG. 15) and the 19 available FGFs (FIG. 17). Based on our structures and the sequence alignment, we propose that the FGF-D2 and FGF-linker interfaces described above represents a general conserved binding interface for all FGF-FGFR complexes.

Interactions between FGF2 and the linker between D2 and D3 in the illustrative embodiment include hydrogen bonds between Asn-102 and Asn-104 of FGF2 with Arg-250 of FGFR1, and a hydrophobic interaction between Leu-98 of FGF2 and Val-248 of FGFR1. Arg-250 is invariant in the FGFR subfamily, and thus may also represent a therapeutically important site.

The FGF-D3 Interface

While the FGF-D2 and the FGF-linker interfaces are conserved in FGF-FGFR complexes, a large part of the FGF-D3 interface is highly divergent, thus revealing the determinants of FGF-binding specificity. FIGS. 11–14 depict the interactions between FGF and the upper part of the D3 module. These interactions are mediated mainly by the βB′-βC, βC′-βE, and βF-βG loops of FGFRs. While residues in the βB′-βC are highly conserved, the amino acid sequences of the βC′-βE and βF-βG loops are significantly divergent among FGFRs (FIG. 16). Notably, alternative splicing occurs at the junction between βC′ and the βC′-βE loop. Thus, the βC′-βE and βF-βG loops are located in the second half of D3, which is subject to alternative splicing. Interactions of D3 with FGF involve several regions of FGF including the most divergent regions at the N-terminal segment outside of the 1-trefoil core (prior to 1) and at the central segment consisting of β4 and the β4-β5 loop. In contrast to the FGF-D2 interface which is dominated by hydrophobic interactions, most of the interactions in the FGF-D3 interface are mediated by hydrogen bonds. Moreover, many of the hydrogen bonds between FGF and D3 are made via water molecules. The polar nature of this FGF-D3 interface is consistent with the notion that this interface plays a critical role in FGF-FGFR binding specificity.

The conserved interactions between FGF2 and the βB′–βC loop in D3 are mediated by four hydrogen bonds (one direct, three water-mediated) between an FGF-invariant glutamic acid residue, Glu96 in FGF2, and FGFR-invariant Gln285 in the βB′-βC loop of D3 (FIGS. 9 and 11). A water-mediated hydrogen bond between the side chain of Asn104 and the backbone carbonyl oxygen of Asp283 is also made in this interface (FIG. 9). The significance of Glu96 in FGF2 for FGFR binding was confirmed by a 1000-fold reduced receptor binding affinity of an FGF2 mutant containing an alanine in place of Glu96 (Zhu et al., 1995).

In contrast to the interface between FGF and the βB′-βC loop, the interactions between FGF and the βC′-βE loop in D3 are highly variable. A major difference between the crystal structures of FGF2-FGFR2 and FGF1-FGFR1 is the conformation of the βC′-βE segment (FIG. 5). In the FGF2-FGFR2 structure, the βC′-βE loop is well ordered and forms several specific contacts with residues in β4 of FGF2 (FIG. 13). This loop, on the other hand, is disordered in the crystal structure of FGF1-FGFR1 (FIG. 5). This difference reflects the lack of interaction between this loop and FGF1 and is not the result of crystal packing; this segment is ordered in all the four FGF2-FGFR2 complexes in the unit cell and disordered in both FGF1-FGFR1 complexes in the unit cell. As a result of this difference, the total accessible surface area buried in the FGF1-FGFR1 complex is 2200 Å² as compared to 2700 Å² in the FGF2-FGFR2 complex.

A total of five hydrogen bonds are formed at the interface between FGF2 and the βC′-βE segment in the FGF2-FGFR2 structure (FIG. 13). Two hydrogen bonds are formed between the side chain of Gln56 of FGF2 and Asp321 of FGFR2, and two hydrogen bonds are made between the side chain of Glu58 of FGF2 and backbone atoms of Val317 and Asn318 in FGFR2. A fifth hydrogen bond is made between the backbone of Ala57 in FGF2 and the side chain of Asp321 via an ordered water molecule. Hydrophobic contacts between the side chain of Val317 in FGFR2 and the side chains of Tyr73, Val88, and Phe93 in FGF2 fortify this interface (FIG. 13). Mutagenesis experiments support the involvement of both Val88 and Phe93 in receptor binding. Replacement of Val88 and Phe93 with alanine in FGF2 cause a 10-fold and 80-fold reduction in receptor binding affinity, respectively (Zhu et al., 1998).

It is possible that the βC′-βE loop exists in several different conformations and that interactions with different FGFs will modulate its secondary structure. In the crystal structures of FGF2-FGFR2 and FGF2-FGFR1, the βC′-βE segment forms a small hydrophobic plug by means of interactions between three residues in this region (Ala315, Thr319 and Ile324) along with Ile288 located in βC in D3. It is conceivable that in the unoccupied receptors, the side chains of these residues are not sufficiently hydrophobic to form a stable core. In the occupied receptors, on the contrary, interactions with FGF2 may facilitate the positioning of these hydrophobic residues leading to formation of a more stable structure. In FGF1, the residue corresponding to Gln56 of FGF2 is a serine (FIG. 17), whose side chain is not long enough to form hydrogen bonds with Asp320 in FGFR1. A loss of these hydrogen bonds may increase the flexibility of the βC′-βE segment. This region is disordered in the FGF1-FGFR1 structure (FIG. 5 and FIG. 10).

On the basis of the structural analysis described above, it is proposed that FGF1 does not engage in any specific contacts with the βC′-βE loop, providing a potential explanation for why FGF1 binds indiscriminately to most FGFRs including the various alternatively-spliced forms, thus functioning as a universal ligand for all known FGFRs.

The crystal structure of an FGF1-FGFR2 complex was recently reported (Stauber et al., 2000). In contrast to the FGF1-FGFR1 structure described here, in the FGF1-FGFR2 structure the βC′-βE loop is ordered and makes several contacts with FGF1. Based on this structure changes in the primary sequence of the βC′-βE loop (as a result of alternative splicing) would clearly affect FGF1 binding. This structural feature, however, does not agree with the well-documented universal binding characteristics of FGF1.

The βC′-βE loop of all known FGFRs, irrespective of exon IIIb or IIIc, contains a highly conserved potential N-glycosylation site (Asn318 in FGFR2). The results described herein confirm that Asn318 is glycosylated in the extracellular domain of FGFR2 when expressed in insect cells. In the crystal structure of FGF1-FGFR2 (Stauber et al., 2000), the side chain of Asn318 makes two hydrogen bonds with FGF1. This peculiarity along with the specificity conundrum led us to consider whether the interactions between the βC′-βE loop and FGF1, observed in this structure, could be due to crystal packing and thus not reflect the situation in vivo.

Analysis of the relative disposition of D2 and D3 in all the FGF-FGFR structures revealed that the linkage between D2 and D3 is flexible, and the angle between the two domains is not dictated solely by the contacts between the two domains and the ligand. That is, crystal packing also affects the relative disposition of the two domains. Although the FGF1-FGFR1 (reported in this manuscript) and FGF1-FGFR2 (Stauber et al., 2000) structures feature a common ligand, superimposition of the Cα atoms of D2 between the two structures reveals a 7.8° difference in the relative orientation of D3 and D2. As a consequence, the βC′-βE loop in the FGF1-FGFR2 structure is closer to the ligand, and it is conceivable that the interactions between the βC′-βE loop and FGF1 in this structure are the result of crystal packing. In the FGF1-FGFR1 structure, the βC′-βE loop is disordered in both complexes in the asymmetric unit, providing two independent instances in which the βC′-βE loop does not engage FGF1.

Analysis of the lattice contacts in FGF1-FGFR2 structure provides a plausible mechanism by which crystal packing might have contributed to the observed interactions between the βC′-βE loop and FGF1. In this structure, the D2s of two symmetry mates insert into the space between the two D3s of the primary dimer, and appear to push the D3s closer to the FGF1 molecules.

Interactions Between FGFR and FGF which Stabilize Dimerization

The D2-D3/FGF2 dimer observed in the crystal structure of one illustrative embodiment is stabilized by interactions between each FGFR in the dimer, and by interactions between the FGF bound to one FGFR and the other receptor in the dimer. The ligand-receptor contacts which stabilize dimerization are largely weak van der Waals interactions between residues Asp-99, Ser-100, Asn-101, Pro-132, Gly-133, and Leu-138 of FGF2 and Pro-199, Asp-200, Ile-203, Gly-204, Gly-205, Ser-219, and Val-221 of FGFR1. Also noted are hydrogen bonds between Pro-132 of FGF2 and Gly-204 of FGFR1, and Lys-26 of FGF2 and Asp-218 of FGFR1.

In contrast, the receptor—receptor contacts which stabilize dimerization include a hydrophobic contact between Ala-171 residues of each receptor, hydrogen bonds between Lys 172, Thr-173, and Asp-218 of each receptor, and van der Waals interactions between Ala-171 and Lys-172 of each receptor. The present invention describes a receptor—receptor interface which was not postulated previously, involving residues conserved in the FGFR subfamily.

Disruption of the contacts which stabilize dimerization, for example by a molecule(s) which prevents the formation of one or more contacts, may provide a means of inhibiting RPTK function. Alternatively, a molecule(s) which further stabilize dimer formation may provide a means of stimulating RPTK function.

Structural Basis for the Role of Alternative Splicing in FGF-Binding Specificity Role of the βC′-βE Segment

A comparison of the amino acid sequences of FGFs and FGFRs in the interface between βC′-βE loop and FGFs shows significant diversity (FIG. 16 and FIG. 17). Moreover, alternative splicing occurs at the end of βC′, resulting in major changes in the primary sequence and length of the βC′-βE loop. For example, the amino acid sequence of the βC′-βE loop in KGFR/FGFR2(IIIb) has seven substitutions and is two amino acids shorter than the corresponding region in FGFR2(IIIc) (FIG. 16). Significantly, the three residues (Ala3 15, Thr319, and Ile324) in FGFR2(IIIc) that participate in formation of the βC′-βE hydrophobic plug are replaced by residues (Ser315, Ser319, and Ala322) in KGFR/FGFR2(IIIb) that are less likely to form a hydrophobic plug (FIG. 16). The result of these changes, the βC′-βE loop in KGFR will not be able to interact efficiently with FGF2. This proposal is supported by binding experiments of FGF2 to a mutant FGFR2, in which its βC′-βE loop is replaced with the corresponding region from KGFR. The affinity of FGF2 towards this mutant is reduced by an order of magnitude (Gray et al., 1995). Conversely, insertion of the two residues and/or amino acid substitutions in the βC′-βE loop of KGFR did not affect FGF 1 binding but abolished KGF/FGF7 binding (Wang et al., 1995b). Moreover, replacement of the corresponding region in FGFR1(IIIc) conferred upon the mutant receptor the ability to bind KGF (Wang et al., 1999), while wild type FGFR1(IIIc) does not bind KGF/FGF7. These data indicate that there may be steric clashes between KGF/FGF7 and the βC′-βE segment in FGFR2(IIIc) resulting in the reduced affinity of KGF/FGF7 to FGFR2(IIIc). On the contrary, the βC′-βE segment of KGFR/FGFR2(IIIb) may interact more efficiently with KGF/FGF7. The latter hypothesis is supported by the finding that a synthetic peptide derived from KGFR/FGFR2(IIIb) encompassing the βC′-βE segment competes specifically with the binding of KGF/FGF7 to KGFR/FGFR2(IIIb) (Bottaro et al., 1993). Final validation of these proposals, however, awaits a crystal structure of KGF/FGF7 in complex with KGFR/FGFR2(IIIb).

The structural findings described herein are also consistent with the identification of a central segment in KGF/FGF7 (residues 91–110) necessary for specific recognition and activation of KGFR (Reich-Slotsky et al., 1995). This region mainly corresponds to β4 and the β4-β5 loop in FGF2 (FIG. 6), which in the crystal structure of FGF2-FGFR2 make specific contacts with βC′-βE and βF-βG loop in D3, respectively (FIGS. 13 and 11, respectively). Taken together, the structural data provide a molecular explanation as to how alternative splicing switches specificity in FGFR2/KGFR system.

Although alternative splicing plays a major role in specificity, similarly spliced variants of FGFRs also exhibit differential binding specificity (Ornitz et al., 1996). It was shown that FGF2 binds strongly to FGFR1(IIIc) and FGFR2(IIIc) but poorly to FGFR3(IIIc) and FGFR4 (Chellaiah et al., 1999; Vainikka et al., 1992). A survey of amino acid sequences of the βC′-βE loop of these receptors shows that the βC′-βE loop of FGFR4 as with KGFR/FGFR2(IIIb) is two amino acids shorter than the corresponding loop in FGFR1-3 (FIG. 16). Based on the results described herein, it is predicted that this loop in FGFR4 can not efficiently interact with FGF2. This will result in reduced FGF2 binding affinity to FGFR4 as compared to FGFR1. The βC′-βE loop of FGFR3 differs from that of FGFR1 by two amino acid substitutions (FIG. 16). Significantly, in FGFR3 the residue corresponding to Val317 of FGFR2 is an alanine, an amino acid with a smaller side chain than valine (FIG. 16). This will result in a weaker hydrophobic interaction with FGF2, affecting the affinity of FGF2 towards FGFR3. Indeed, when these residues in FGFR3 were replaced with the corresponding residues in FGFR1, the resultant FGFR3 mutant exhibited comparable binding affinity towards FGF2 (Chellaiah et al., 1999). The interactions between FGF and the βC′-βE loop in the crystal structure (FIG. 13) provide a molecular explanation for how specificity is regulated by the primary sequence composition of the βC′-βE loop.

Role of the βF-βG Loop

The βF-βG loop in D3 also plays an important role in the modulation of FGF binding specificity. In the FGF2-FGFR2 structure, Ser347 of FGFR2, located in OF-OG loop, makes two water mediated-hydrogen bonds with Glu96 and Leu98 of FGF2 (FIG. 11). A water-mediated hydrogen bond between Gly345 in FGFR2 and Gly61 in FGF2 and a direct hydrogen bond between the backbone of Asn346 in FGFR2 and the side chain of Arg60 in FGF2 provide additional contacts in this region (FIG. 11). Residues Arg60 and Gly61 are located in the β4-β5 loop in FGF2 (FIG. 17). Comparison of amino acid sequences shows that FGFs display considerable sequence variation at the position of Arg60 of FGF2. Residue Gly61, on the other hand, is highly conserved in FGFs (FIG. 17). The βF-βG loop is invariant in the IIIb and IIIc forms of FGFRs (FIG. 16). However, Gly345 and Ser347 of FGFR2(IIIc) are replaced by Ser342 and Tyr345 in KGFR/FGFR2(IIIb). Replacement of Ser347 in FGFR2 by a tyrosine in KGFR/FGFR2(IIIb) may result in steric clashes with FGF2 leading to reduced binding affinity of FGF2 to KGFR/FGFR2(IIIb). This proposal is consistent with ligand binding properties of a double mutant KGFR, in which Tyr345 and Gln348 in KGFR were replaced by serine and isoleucine as in FGFR2. This mutant receptor acquired significant binding affinity towards FGF2 as compared to the parent molecule (Gray et al., 1995). Interestingly, mutation of an invariant asparagine located in the βF-βG (Asn344 in KGFR) to an alanine abolished binding ability of KGFR/FGFR2(IIIb) towards all FGFs tested (Gray et al., 1996). These results are expected based on our FGF-FGFR strcutures: in FGF2-FGFR2 structure the corresponding asparagine (Asn346) makes two intramolecular hydrogen bonds with backbone atoms of Ile348 and Gly349 in FGFR2. These hydrogen bonds play an important role in maintaining the local fold of the βF-βG loop. Substitution of Asn346 with an Ala residue will interfere with the folding of this loop resulting in possible steric clashes with all FGFs. Taken together, the structural data provide a plausible molecular explanation for how alternative splicing in D3 regulates FGF binding specificity towards different receptor isoforms.

The Role of the N-Terminal Segment of FGF

In the crystal structures of the receptor-bound FGF1 and FGF2, residues upstream of β1 are found to be disordered (Eriksson et al., 1991; Blaber et al., 1996; Zhu et al., 1991). However, in the crystal structures of the receptor-bound FGF1 and FGF2 these residues are ordered and in proximity to D3 of FGFRs (FIGS. 12 and 14). In the FGF2-FGFR2 structure, the side chain of Phe17 is located in a shallow hydrophobic pocket in D3 that is formed by Pro286, Ile288 and Val280 (FIG. 12). Moreover, Phe17 forms several hydrogen bonds via backbone atoms with Ser282 and Gln285 in D3. Lys18 in FGF2 also makes several hydrogen bonds with the side chains of Lys279 and Glu325 and with the backbone of Val280 in D3 (FIG. 12). In agreement with these structural observations, it has been shown that a synthetic peptide consisting of residues 13–18 of FGF2 (prior to β1) competes with the binding of FGF2 to FGFR (Yayon et al., 1993). The amino acids ⁷NYKKPKL¹³ (SEQ ID NO: 202) located at the junction between the N-terminal segment and β1 in FGF1 have been proposed to signal the nuclear accumulation of FGF1 that occurs during sustained exposure of cells to FGF1 (Imamura et al., 1990). In the FGF1-FGFR1 structure, Tyr8 located in this amino acid stretch inserts into a shallow hydrophobic pocket formed by the side chains of Val279, Pro285 and Ile287. The structural data described herein provide a direct role for this region in receptor binding. Deletion mutagenesis experiments support our structural finding. FGFR1 molecules lacking this amino acid stretch have a 250-fold reduced ability to bind FGFR (Imamura et al., 1990). A structure-based sequence alignment of FGFs reveals significant sequence diversity in the segment upstream of β1 in FGFs, suggesting that this region may also play a role in determining FGF binding specificity (FIG. 17).

In view of the interactions between residues prior to PI of FGFs and residues in D3 of FGFRs, it is possible that additional N-terminal residues that are not included in the currently analyzed FGF1 or FGF2 may also play a role in the determining specificity. To test this hypothesis, the crystal structure of full length FGF2 in complex with FGFR2 was determined (data not shown). In this crystal structure, however, all the residues N-terminal to Phe17 are disordered, suggesting that this region does not play a major role in FGFR binding. The significance of the N-terminal residues of FGF2 remains unclear.

FGFR Mutations Responsible for Human Skeletal Disorders

Mutations in the extracellular domains of FGFR1 and FGFR2 have been identified in patients with birth defects involving craniosynostosis (premature fusion of the cranial sutures) such as Pfeifer, Crouzon, Jackson-Weiss, and Apert syndromes (reviewed by Naski and Ornitz, 1998; Burke et al., 1998). These mutations cluster in three regions: in the D2-D3 linker, in D3 and in the linker connecting D3 to the transmembrane helix. These mutations can be classified into two groups: (1) Most of these mutations are substitutions of a cysteine with another amino acid or vice versa, resulting in the creation of unpaired cysteines. This leads to ligand-independent dimerization and activation via formation of an intermolecular disulfide bond between receptor molecules. (2) There are mutations that do not involve cysteine substitutions. Nevertheless, it is thought that these mutations must also result in constitutive activation (ligand-independent) of the affected receptors because they cause similar disease phenotypes as those mutations that create free cysteines. The precise molecular mechanisms by which these mutations lead to receptor activation are less clear.

To understand the molecular bases for the effects of these mutations on FGFR function, we have mapped these mutations onto the three-dimensional structure of FGF2FGFR2 (FIG. 18). Based on our structural data we predict that many mutations in D3, although not directly involving cysteines, could destabilize the tertiary structure of D3 and disfavor the formation of the intra-domain disulfide bridge, thus increasing the likelihood of disulfide bridging between receptor molecules (FIG. 18). Perhaps this notion is best exemplified by the substitution of Trp290 with glycine or arginine. Residue Trp290 is located in the core of D3, adjacent to the disulfide bridge, and replacement of this residue with either of the two amino acids will likely reduce the stability of D3 (FIG. 18).

Mutations of two highly conserved residues Ser252 and Pro253 in the D2-D3 linker of FGFR2 are responsible for all the known cases of Apert syndrome. Mutation of the equivalent proline in FGFR1 (Pro252) has been reported in some cases of Pfeifer syndrome. Based on our structural data we predict that these mutations introduce specific interactions between FGFR and FGF. Indeed, Anderson et al. (1998) have shown that, compared with wild type FGFR2, mutant FGFR2 molecules bearing the Apert mutations exhibit a selective increase in affinity towards FGF2, leading to enhanced signaling where availability of ligand is limiting (Anderson et al., 1998).

As described above, the amino acid stretch between βC′ and βE plays a critical role in determining specificity. Residue Asp321 makes three hydrogen bonds with FGF2 (FIG. 13). Replacement of Asp321 with alanine, which is detected in some cases of Pfeifer syndrome, will therefore reduce the affinity of FGF2 towards FGFR2. It is conceivable, that this amino acid substitution will increase the affinity of FGFR2 for other members of the FGF family. Substitution of Ala35, also located in the βC′-βE loop, with a serine is also associated with Pfeifer syndrome. Residue Ala315 participates in the formation of the hydrophobic βC′-βE plug. This substitution can destabilize the hydrophobic plug and may affect ligand binding specificity.

Heparin-Binding Canyon

In the crystal structure of the illustrative embodiment, a highly positively charged “canyon” that continues onto the top side of both ligands is formed by the interaction of the two D2 regions in the dimer. The canyon receives its positive potential from lysines 160, 163, 172, 175, and 177 of FGFR1. This canyon may represent the site of heparin binding. FGF2 also contains a high affinity heparin binding site, consisting of Asn-27, Lys-125, Gln-134, and Arg-120, and heparin increases the apparent affinity of FGF2 for FGFR1. Thus, these residues may represent a useful therapeutic target, for example using a molecule(s) which affects the affinity of a receptor PTK for its ligand.

It has been postulated that heparin traverses this canyon and bridges the two 1:1 FGF:FGFR complexes. A recently reported crystal structure of another dimeric assemblage of two FGF1:FGFR2 complexes lends additional support to this model (Stauber et al., Proc. Natl. Acad. Sci. USA 97,49–54 (2000)).

Based on the dimeric structure, manual docking experiments have shown that a maximally active dodecasaccharide perfectly traverses the canyon and engages both the high- and low-affinity heparin binding sites of the ligands. In contrast, an octasaccharide placed centrally into the canyon can only interact with the low-affinity heparin binding sites of the ligands. A canyon-docked hexasaccharide is unable to interact with any heparin binding sites of the ligands, implying that oligosaccharides smaller than an octasaccharide do not possess biological activity. There has been some controversy, however, in determining the minimal length of heparin necessary for FGF signaling. It has been proposed that the shortest biologically active heparin oligosaccharide is an octasaccharide and that an increase in heparin length parallels an increase in biological activity up to a dodecasaccharide. However, other studies report that hexasaccharides are biologically active and that even disaccharides possess biological activity.

The inability of this model to fully reconcile all of the previous literature led us to further characterize the role of heparin in FGF signaling. The determination of the crystal structure of a ternary FGF2-FGFR1-heparin complex is described herein. Interactions between heparin, FGF and FGFR provide a molecular basis for the dual role of heparin in augmenting 1:1 FGF:FGFR affinity and promoting dimerization of two FGF-FGFR complexes. Moreover, the unexpected 2:2:2 stoichiometry of FGF:FGFR:heparin observed in the structure led us to propose an new model that also accounts for FGF-dependent FGFR activation by short heparin analogs.

While the heparin binding residues in D2 of FGFRs are highly conserved, the heparin binding residues of the FGF family are known to display considerable diversity (Faham et al., Curr. Opin. Struct. Biol. 8, 578–586 (1998); Venkataraman et al., Proc. Natl. Acad. Sci. USA 96, 3658–3663 (1999)). Moreover, the β1-β2 heparin binding loop is of variable length in different FGFs. As a result of this heterogeneity, it is likely that different FGFs require heparan sulfates of distinct sulfation and/or length to exert their optimal biological activity. In fact, it has been demonstrated that FGF2 requires 2-O-sulfate for heparin binding but not 6-O-sulfate. In contrast, FGF1 requires both sulfate groups to bind to heparin (Ishihara, 1994). Pericellular HSPGs from different cells exhibit significant heterogeneity in sulfation patterns, carbohydrate content and length. These variations could have a profound effect on FGF-FGFR interactions. Moreover, remodeling of the extracellular matrix during development may be a means to regulate the biological activities of FGFs.

The heparin binding mode in the present structure disputes the previous findings regarding the minimal length requirement for heparin to promote FGF-FGFR dimerization as well as the stoichiometry of FGF:FGFR:heparin interactions. The tripartite interactions between FGF, FGFR and heparin observed in the crystal structure suggest that heparin hexasaccharides are sufficient to promote receptor dimerization. Therefore, we decided to test the ability of a hexasaccharide to promote dimerization of FGF-FGFR complexes in vitro. Homogeneously-sulfated hexasaccharide was mixed at various molar ratios with a purified 1:1 FGF1:FGFR2 complex and the reaction mixtures were analyzed by size exclusion chromatography to quantitate dimerization (FIG. 31). Addition of hexasaccharide at a molar ratio of 0.5:1 hexasaccharide:complex dimerized half of the FGF1-FGFR2 complexes (FIG. 31, Panel B). Hexasaccharide at a molar ratio of 1:1 hexasaccharide:complex led to the quantitative dimerization of all the FGF1-FGFR2 complexes (FIG. 31, Panel C). Excess hexasaccharide reduced dimerization and resulted in the appearance of a peak which elutes slightly earlier than the control (FIG. 31, Panel D). This peak corresponds to the ternary 1:1:1 hexasaccharide:FGF1:FGFR2 complex. It is noteworthy that in the absence of heparin, FGF-FGFR complexes tend to dissociate under size exclusion chromatography conditions, indicating that heparin increases the affinity of FGF for FGFR and stabilizes dimer formation. Hence, the biochemical experiments presented in FIG. 31 support the observed mode of heparin binding in the crystals.

Based upon the crystal structure and supporting biochemical experiments described herein, a new “two end” model by which heparin induces FGF-dependent FGFR dimerization (see FIG. 32) is proposed. According to this model, heparin interacts via its non-reducing ends with both FGF and FGFR and promotes the formation of a stable 1:1:1 FGF:FGFR:heparin ternary complex. A second 1:1:1 FGF:FGFR:heparin ternary complex is then recruited to the first complex via direct FGFR:FGFR contacts, secondary interactions between FGF in one ternary complex and FGFR in the other ternary complex, and indirect heparin-mediated FGFR—FGFR contacts. In the absence of heparin the direct receptor—receptor contacts and secondary ligand-receptor interactions are not sufficient for appreciable dimerization. Clearly, heparin augments direct FGFR—FGFR and secondary FGF-FGFR interactions.

The proposed “two end” model presented in this report is consistent with the chemical architecture of heparan sulfate chains, which are linked by the reduced end (O1) to the protein core of HSPG. Furthermore, heparan sulfate can be roughly divided into low and high sulfate regions (Gambarini et al., Mol. Cell Biochem. 124, 121–129 (1993)). The low sulfate region is proximal to the protein core. The high sulfate region is located towards the non-reducing end (O4) that corresponds to the non-reducing ends of the decasaccharides bound in the center of the canyon in our structure. Moreover, the chemical nature of the highly sulfated non-reducing ends resemble heparin and are made up of tri-sulfated disaccharide units (IdoA,2S-GlcNS,6S) considered to be the building block of HSPG (Gambarini et al., Mol. Cell Biochem. 124, 121–129 (1993)). In fact, these highly sulfated regions of heparan sulfate have been shown to be the major determinants of the potentiating effect of heparan sulfate on FGF1 mitogenic activity (Gambarini et al., Mol. Cell Biochem. 124,121–129 (1993)).

A survey of the nature of the tripartite interactions between FGF, FGFR and heparin shows that about half of these interactions are mediated through carboxylate, linker and ring oxygens of heparin. Therefore, the results presented here afford a structural basis for the reported ability of certain synthetic non-sulfated heparan-derived di- and tri-saccharides to promote FGF-dependent FGFR activation in vivo (Ornitz et al., 1995). Synthesis of heparin molecules with a homogeneous sulfation pattern is difficult. On the basis of the structure presented here, it is possible to design small molecule heparin analogs in which the sulfate groups are replaced with similar functional groups. Thus, our structural studies establish a framework for the rational design of heparin mimetics capable of modulating FGF activity. Given the important roles FGF play in angiogenesis and their biological processes, synthetic heparin agonists and antagonists may have potential therapeutic value.

Crystalline FGFR Extracellular Domain/FGF1 complexes

In a second illustrative embodiment, the invention provides crystals of FGFR1 D2-D3 domain bound to an FGF1 molecule. The D2-D3 domain of this embodiment again consists of residues 142–365, and each D2-D3 domain is bound to a single FGF1 molecule. The crystals were obtained by the methods provided in the Examples. The FGFR1 D2-D3/FGF1 crystals, which may be native crystals, derivative crystals or co-crystals, have triclinic unit cells, and space group symmetry β1. There are two FGFR1 D2-D3/FGF1 complexes in the asymmetric unit, related by an approximate two-fold axis. The unit cell has dimensions of about a=62.55 Å, b=64.06 Å, c=64.14 Å, α=93.40°, β=111.17°, and γ97.18°.

Binding Interactions Between FGFR and FGF1

Within each D2-D3/FGF1 complex of the illustrative embodiment, FGF1 interacts extensively with D2, D3, and the linker between the two domains. A single hydrogen bond is noted between Tyr-15 in FGF 1 and Leu-165 in FGFR1, but the majority of interactions between D2 and FGF 1 are hydrophobic. For example, hydrophobic contacts can be seen between Tyr-15 and Leu-133, and Leu-135 of FGF1 and Ala 167 of D2, between Tyr-94, Leu-133, and His-93 of FGF1 and Pro-169 of D2, and between Phe-22 of FGF1 and Val-248 of FGFR1. These contacts are similar to the contacts described herein for the D2-D3/FGF2 crystal.

Interactions between FGF1 and the linker between D2 and D3 in the illustrative embodiment include hydrogen bonds between His-93 and Asn-95 of FGF 1 with Arg-250 of FGFR1. Again, these contacts are similar to the contacts described herein for the D2-D3/FGF2 crystal.

Additionally, several regions of FGF1 interact with D3, including Tyr-8, which inserts into a hydrophobic pocket in D3 formed by Val 279, Pro-285, and Ile-287. Additionally, Tyr-8 participates in a hydrogen bond with Gln-284 of FGFR1. In a region which is diverse amongst the members of the FGF family, residues 46,48–51, and 54 of FGF1 form van der Waals contacts with Gln-284, Pro-285, His-286, Gly-344, and Asn-345 of FGFR1 Ala-57 of FGF2, and Glu-49 in FGF1 forms a hydrogen bond with His-286 of FGFR1. As was described herein for the D2-D3/FGF2 crystals, this latter region may be important in defining the binding specificity of FGFRs, and thus may be a therapeutically important site.

Determining Unit Cell Dimensions and the Three Dimensional Structure of a Polypeptide or Polypeptide Complex

Once the crystal is grown, it can be placed in a glass capillary tube and mounted onto a holding device connected to an X-ray generator and an X-ray detection device. Collection of X-ray diffraction patterns are well documented by those in the art. Ducruix and Geige, 1992, IRL Press, Oxford, England, and references cited therein. A beam of X-rays enter the crystal and then diffract from the crystal. An X-ray detection device can be utilized to record the diffraction patterns emanating from the crystal. Although the X-ray detection device on older models of these instruments is a piece of film, modern instruments digitally record X-ray diffraction scattering.

Methods for obtaining the three dimensional structure of the crystalline form of a peptide molecule or molecule complex are well known in the art. Ducruix and Geige, 1992, IRL Press, Oxford, England, and references cited therein. The following are steps in the process of determining the three dimensional structure of a molecule or complex from X-ray diffraction data.

After the X-ray diffraction patterns are collected from the crystal, the unit cell dimensions and orientation in the crystal can be determined. They can be determined from the spacing between the diffraction emissions as well as the patterns made from these emissions. The unit cell dimensions are characterized in three dimensions in units of Angstroms (one Å=10⁻¹⁰ meters) and by angles at each vertices. The symmetry of the unit cell in the crystals is also characterized at this stage. The symmetry of the unit cell in the crystal simplifies the complexity of the collected data by identifying repeating patterns. Application of the symmetry and dimensions of the unit cell is described below.

Each diffraction pattern emission is characterized as a vector and the data collected at this stage of the method determines the amplitude of each vector. The phases of the vectors can be determined using multiple techniques. In one method, heavy atoms can be soaked into a crystal, a method called isomorphous replacement, and the phases of the vectors can be determined by using these heavy atoms as reference points in the X-ray analysis. Otwinowski, 1991, Daresbury, United Kingdom, 80–86. The isomorphous replacement method usually requires more than one heavy atom derivative. In another method, the amplitudes and phases of vectors from a crystalline polypeptide with an already determined structure can be applied to the amplitudes of the vectors from a crystalline polypeptide of unknown structure and consequently determine the phases of these vectors. This second method is known as molecular replacement and the protein structure which is used as a reference must have a closely related structure to the protein of interest. Naraza, 1994, Proteins 11:281–296. Thus, the vector information from a receptor PTK of known structure, such as those reported herein, are useful for the molecular replacement analysis of another receptor PTK with unknown structure.

Once the phases of the vectors describing the unit cell of a crystal are determined, the vector amplitudes and phases, unit cell dimensions, and unit cell symmetry can be used as terms in a Fourier transform function. The Fourier transform function calculates the electron density in the unit cell from these measurements. The electron density that describes one of the molecules or one of the molecule complexes in the unit cell can be referred to as an electron density map. The amino acid structures of the sequence or the molecular structures of compounds complexed with the crystalline polypeptide may then be fit to the electron density using a variety of computer programs. This step of the process is sometimes referred to as model building and can be accomplished by using computer programs such as TOM/FRODO. Jones, 1985, Methods in Enzymology 115:157–171.

A theoretical electron density map can then be calculated from the amino acid structures fit to the experimentally determined electron density. The theoretical and experimental electron density maps can be compared to one another and the agreement between these two maps can be described by a parameter called an R-factor. A low value for an R-factor describes a high degree of overlapping electron density between a theoretical and experimental electron density map.

The R-factor is then minimized by using computer programs that refine the theoretical electron density map. A computer program such as X-PLOR can be used for model refinement by those skilled in the art. Brunger, 1992, Nature 355:472475. Refinement may be achieved in an iterative process. A first step can entail altering the conformation of atoms defined in an electron density map. The conformations of the atoms can be altered by simulating a rise in temperature which will increase the vibrational frequency of the bonds and modify positions of atoms in the structure. At a particular point in the atomic perturbation process, a force field, which typically defines interactions between atoms in terms of allowed bond angles and bond lengths, Van der Waals interactions, hydrogen bonds, ionic interactions, and hydrophobic interactions, can be applied to the system of atoms. Favorable interactions may be described in terms of free energy and the atoms can be moved over many iterations until a free energy minimum is achieved. The refinement process can be iterated until the R-factor reaches a minimum value.

The three dimensional structure of the molecule or molecule complex is described by atoms that fit the theoretical electron density characterized by a minimum R-value. A file can then be created for the three dimensional structure that defines each atom by coordinates in three dimensions. Examples of such structural coordinate files are defined in Tables 1–4 and 6.

V. Stem Cell Factor

Stem cell factor (“SCF”) is a growth factor implicated in the stimulation of the survival, proliferation, and differentiation of hematopoietic cells. SCF is also known as mast cell growth factor (“MCGF”), steel (Sl) factor (“SLF”) or kit ligand (“KL”). SCF is believed to be critical for mast cell production and function and to play an important role in the development of melanocytes, germ cells, and intestinal pacemaker cells. SCF is believed to mediate its biological effects by binding to and activating a receptor protein tyrosine kinase designated c-kit (also referred to as SCF receptor (“SCFR”). Like other RPTK ligands, SCF induces dimerization of c-kit followed by trans-autophosphorylation of the cytoplasmic protein tyrosine kinase domain leading to subsequent recruitment of signaling proteins, tyrosine phosphorylation of substrates and activation of multiple signaling pathways.

It is believed that stem cell factor (“SCF”) can play an important role in hematopoeisis by stimulating the survival, proliferation and differentiation of mast cells, melanocytes and germ cells. SCF has been tested extensively in both animals and human because of its ability to promote hematopoietic recovery. It has been demonstrated that SCF treatments produce an increase in the number of peripheral blood neutrophiles and hematopoietic progenitor cells and modest rises in the numbers of platelets and lymphocytes. SCF, alone or in combination with other cytokines, is used to reduce the hematological damage of chemotherapy. In a separate clinical trial, SCF has also been proven to be effective in enhancing the ability of G-CSF to mobilize peripheral blood hematopoietic progenitor and stem cells. It is believed that these cells can be transplanted to reconstitute the hematopoietic system in patients receiving bone marrow ablative therapy (Nicola et al., Protein Chem. 52, 1–65 (1998)).

SCF exist naturally as membrane anchored and soluble isoforms as a result of alternative RNA splicing and proteolytic processing. The soluble form of SCF has 165 amino acids, but its receptor binding core has been mapped to the first 141 residues (Langley et al., Arch. Biochem. Biophys. 311, 55–61 (1994)). SCF functions as a non-covalent homodimer, but under physiological conditions, the majority of SCF is reported to exist as a monomer. Dimerization of SCF is a dynamic process and it may play a regulatory role in the control of SCFR binding affinity and receptor activation.

Comparison of SCF with Other Growth Factors

SCF belongs to the short-chain helical cytokine family (Bazan, 1991; Rozwarski et al., 1994), but its resemblance to the other cytokines is limited only to the overall fold. The primary structures exhibit very weak similarity and sequences can be aligned only by comparison of the secondary structures (FIG. 20). The structure of SCF is most similar to the structure of M-CSF (Pandit et al., Science 258, 1358–1362 (1992)). The core four helix bundles of the two proteins superimpose relatively well, with r.m.s. deviation of 1.98 Å for the alpha-C atoms. However, upon superimposition of the helices, the two beta-strands deviate significantly. Two loops in SCF, residues 29 to 41 and residues 90 to 98, extrude more than those of M-CSF. At the dimer interface, the SCF loop from residue 61 to 72 also extrudes further away from the core and packs against the same loop from the second protomer. The x-ray crystallography work described herein suggests that there is more contact between the two protomers of SCF as compared to the contact between the two M-CSF protomers. Furthermore, M-CSF is a covalent homodimer linked by an intermolecular disulfide bond whereas SCF is a noncovalent homodimer. Flt3 ligand is also a noncovalent homodimer, but it has an extra intramolecular disulfide bond as does M-CSF. Nevertheless, the structure of flt3 ligand (Hannum et al., Nature 368, 643–648 (1994)) can be predicted with reasonable confidence based upon the crystal structures of SCF described herein together with the previously described crystal structure of M-CSF (Pandit et al., Science 258, 1358–1362 (1992)).

In contrast to the disulfide linked PDGF and M-CSF homodimers, two other ligands of the same family of receptor tyrosine kinases, SCF functions as a non-covalent homodimer (Pandit et al., Science 258, 1358–1362 (1992)). It has been shown that the bivalency of SCF is the sole driving force responsible for dimerization of the extracellular ligand binding domain of c-kit. Hence analysis of the molecular interactions that control SCF-dimer formation are critical for understanding the mechanism of activation of c-kit.

It is known that dimerization of SCF is sensitive to pH and salt concentration changes. This property is likely due to the fact that the interface is formed in part by polar interactions via salt bridges at the periphery and by a water molecule-mediated hydrogen bonds among buried polar residues at the core of the interface. In an attempt to identify residues that play a role in SCF dimerization, a Phe63Cys mutant was generated and characterized for receptor binding activity (Hsu et al., J. Biol. Chem. 272, 6406–6415 (1997)). It was demonstrated that this mutation led to the formation of a covalent SCF dimer. However, the mutant SCF dimer was biologically inactive. The structure of the SCF interface described herein provides a plausible explanation for the lack of activity of this mutant. (see FIG. 21). In the structure, the shortest distance between the side chains of the two symmetry related Phe63 is about 8 Å with the well-coordinated water molecule between them. It is impossible to create a disulfide bond between these two residues without disrupting the secondary and tertiary structures of the SCF dimer.

Domain Swapping and the Covalent Dimer of SCF

Recombinant SCF is expressed in E. coli as inclusion bodies in a denatured form and an active SCF protein is produced by a procedure involving refolding and oxidation. It has previously been reported that a small fraction of the refolded-oxidized protein is a covalent disulfide linked form of SCF. Interestingly, the covalent SCF dimer has bben reported to bind to c-kit with slightly reduced affinity but was more potent in stimulation of hematopoietic cells. Comparison of the secondary and tertiary structures by spectroscopic methods demonstrated that the covalent dimer is indistinguishable from the non-covalent dimer (Lu et al., J. Biol. Chem. 271, 11309–11316 (1996)). Surprisingly, the disulfide linkages of the covalent dimer were found to be identical to those in the non-covalent dimer except that the disulfide linkages in the variant protein were intermolecular. That is, Cys4 and Cys43 from one protomer form disulfide bonds with Cys89 and Cys138, respectively, of the second protomer. It was thus proposed that the covalent dimer could be formed by a three-dimensional domain swapping of helices alphaA and alphaD between the two monomers (Lu et al., J. Biol. Chem. 271, 11309–11316 (1996)). A close examination of the three-dimension structure of SCF reported herein shows that the C2 symmetry of the dimer may allow these helices to be swapped between the protomers while preserving the overall structure and identical surface at the tails of each protomer. FIG. 23 shows a model generated by swapping helices alphaA and alphaD between the two protomers. Interestingly, the interactions at the core between the helices from the original dimer are preserved in the swapped model while the loops around the C2 axis and the orientation of the strands have to be adjusted. The disulfide pairs are identical in both forms except that they are intramolecular in the non-covalent dimer and intermolecular in the covalent dimer. It is worth noting that other four helix bundle cytokines such as L-5, IL-10 and IFN- are reported to form similar covalent interdigitated dimers naturally. In IL-5, helix alphaD and strand 2 of one protomer, together with helices alphaA, alphaB, alphaC and strand 1 from the other protomer, form one domain of the two-domain dimer. Indeed, because of the symmetric nature of the structure, it was possible to generate monomeric IL-5 mutants (Dickason et al., Nature 379, 652–655 (1996); Dickason et al., J Mol Med 74, 535–546 (1996); Edgerton et al., J. Biol. Chem. 272, 20611–20618 (1997)). By the same token, new type interdigitated covalent SCF dimers could be formed by introducing mutations in the loops between helix αA and strand 1 and between 2 and helix αD that favor the covalent dimer structure. These similarities in fold and dimeric symmetry among the helical cytokines probably reflect their common evolutionary origin.

Three-dimensional domain swapping is considered to be a general mechanism for the regulation of oligomer assembly, that is oligomers are formed from stable monomers by exchanging domains during evolution or under controlled laboratory conditions (Bennett et al., 1995). It has been suggested that under normal physiological conditions, the majority of soluble SCF exists as monomers. The balance between SCF monomers and dimers may be linked to the physiological requirement for activation of c-kit expressed on target cells in vivo. For therapeutic purpose, however, the more potent disulfide-linked dimer is generally preferred because it can be administered at low doses to avoid significant mast cell activation while stimulating hematopoietic recovery (Nocka et al., Blood 90, 3874–3883 (1997)).

Receptor Binding Region on SCF

SCF dimer are known to bind soluble or membrane forms of c-kit with high affinity and specificity. The binding of SCF to c-kit was analyzed by biochemical methods, by employing site-directed mutagenesis and by epitope mapping with site-specific anti-c-kit antibodies. It was reported that deletions of residues 1 to 3 from the N-terminus reduced the binding of SCF to c-kit by approximately 50%. Deletion of Cys4 inactivated SCF, whereas deletion of Cys138 and additional residues form the C-terminus only compromised SCF activity. Moreover, an SCF double mutant at Cys43Ala and Cys138Ala, which eliminate one pair of disulfide bonds, resulted in a partially active SCF as well. These experiments demonstrated that the N-terminus of SCF and the integrity of the Cys4–Cys89 disulfide bond are crucial for full CSF activity.

By analyzing the activities of a variety of SCF/M-CSF chimeric proteins, it has been shown that Arg121, Asp124, Lys127 and Asp128 are essential for SCF activity (Matous et al., Blood 88,437–444(1996)). Moreover, by using antibodies that neutralize different epitopes on SCF, it has been demonstrated that the regions flanked by amino acids 61 to 65 and 91 to 95 are also essential for SCF activity (Mendiaz et al., Eur. J. Biochem. 239, 842–849 (1996)). In general the regions mapped by biochemical methods are located in close proximity at the tail region of each SCF protomer. This region contains a deep crevice at the end of alphaC formed by side chains of the hydrophobic residues Phe102, Leu98, Pro34, Tyr32, and by the Cys43–Cys138 disulfide bridge (see FIG. 24). Next to the crevice, there are three charged patches; a positively charged patch (Arg5, Arg7, and Lys127) followed by a negatively charged patch (Asp84, Asp85, Glu88, and Glu92) and then by an additional positively charged patch (Lys91, Lys99, Lys100 and Lys103). FIG. 24 shows the locations of the positively charged and negative charged patches as well as the hydrophobic crevice. This surface may function as a receptor binding site with the charged interactions providing anchor and specificity for ligand/receptor interactions and the hydrophobic interactions providing enthalpy to complex formation.

While human and rodent SCF are highly conserved, the charged patches that may function as part of receptor binding regions are quite divergent (see FIG. 25). Residues Arg5 and Arg7 in the first positively charged patch of the human SCF are replaced by glycine and proline residues in rodents, respectively. In the second positively charged patch, residues Lys100 and Lys91 are substituted by glutamate residues in both mouse and rat. These changes could account for the difference in the binding affinity of human and murine SCF to the human c-kit that has been reported.

Natural and CHO-cell derived recombinant SCF are glycosylated on multiple asparagine, serine and threonine residues. The receptor binding properties of glycosylated SCF are consistent with the assignment of SCFR binding region shown in FIG. 24. There are four putative asparagine glycosylation sites in the functional core of SCF: Asn65, Asn72, Asn93 and Asn120. Asn72 is not glycosylated probably because its side chain is buried in the dimer interface. However, the side chains of Asn120, Asn65, and Asn93 remain accessible to the solvent in the structure and are indeed glycosylated to different extent. Asn120 is always glycosylated but this does not affect the binding of SCF to c-kit. In contrast, Asn65 and Asn93 are glycosylated in some, but not all, SCF molecules. Importantly, glycosylation of these asparagine residues has been reported to have an adverse effect on SCF binding to SCFR The structure described herein provides possible explanations for the adverse effect of glycosylation of these residues on the activity of SCF. The glycosylation of Asn93 may hinder SCF binding to c-kit as this residue is located very close to the acidic patch and to the hydrophobic crevice. On the other hand, Asn65 is located close to the dimer interface and glycosylation of this residue may interfere with SCF dimerization.

Model for SCF:SCFR Complex

The extracellular ligand binding domains of several receptor tyrosine kinases contain multiple Ig-like domains. For instance, the extracellular domains of FGF receptors contain three Ig-like domains while the extracellular domain of PDGF-receptor family to which c-kit belongs is composed of five Ig-like domains. Similarly, the extracellular domain of the VEGF-receptor has been reported to contain seven Ig-like domains. Although the ligands of these receptors are very diverse, the ligand binding regions in these three families of receptors have been mapped to Ig-like domains two and three (see, e.g., Plotnikov et al., Cell 98, 641–650 (1999)). The determination of the structures of the ligand binding domains of FGF and VEGF receptors demonstrated that FGF and VEGF bind differently to their respective receptors. In the FGF:FGFR complex the two receptors are packed side by side to one face and the ligands occupy the second face. On the other hand, the two VEGFR bind to the far ends of the VEGF-dimer creating an inverted “A” shaped complex with the ligand representing the cross bar in the “capital A”. Since SCF functions as a dimer, SCF binding to c-kit would be expected to resemble the structure which has been reported for the VEGF:VEGFR complex.

The x-ray crystal structure of the SCF dimer was used to build a model of SCF:c-kit complex formation and dimerization. Using the structure of FGFR as a template, a model for Ig-like domains 2–3 as well as 4–5 of c-kit was developed. Ig-like domains 2 and 3 were then docked to the proposed SCF binding surface adopting the mode of FGFR binding to FGF2 (Plotnikov et al., Cell 98, 641–650 (1999)). In addition, the orientation of Ig-like domains 4 and 5 was adjusted to allow for interactions between domain 4 in the complex as suggested by previous biochemical studies (Blechman et al., Cell 80, 103–113 (1995)); see FIG. 26).

c-kit belongs to the same family of RTKs that also includes M-CSFR, PDGFR alpha, PDGFR alpha and flt3. Comparison of their primary structures shows that these RTKs are much more conserved than their ligands. Indeed, the structures of PDGF-A and PDGF-B are dramatically different from the structures of M-CSF and SCF and probably also flt3 ligand. The similarity of the RTKs is also reflected in the chromosomal localizations of their human and murine genes (Kondo et al., Gene. 208, 297–305 (1998)). It is thought that this family of RTKs has evolved from a common ancestral gene that undergone several gene-duplication events. It is worth noting that RTKs that bind to and are activated by ligands with structures of four-bundle helix (i.e., M-CSF, SCF) are primarily involved in the control of hematopoeisis, whereas other members of this family of RTKs exhibit broader expression pattern and are involved in the regulation of growth and development of several tissues and organs.

Determination of the three dimensional structure of SCF would facilitate the determination of the structure of SCF in complex with the extracellular domain of c-kit, and enable the design and production of more potent forms of therapeutic SCF analogues. With the detailed structural information described herein, it may now be possible to design novel SCF variants with increased therapeutic potency.

VI. Uses of the Crystals and Atomic Structure Coordinates

The crystals of the invention, and particularly the atomic structure coordinates obtained therefrom, have a wide variety of uses. For example, the crystals described herein can be used as a starting material in any of the art-known methods of use for RPTKs. Such methods of use include, for example, identifying molecules that bind to the native or mutated extracellular domain of RPTKs. The crystals and structure coordinates are particularly useful for identifying compounds which are modulators of RPTK function as an approach towards developing new therapeutic agents (see, e.g., Levitzki and Gazit, 1995, Science 267:1782–8).

The structure coordinates described herein can also be used as phasing models for determining the crystal structures of additional native or mutated receptor PTK extracellular domains, as well as the structures of co-crystals of such domains complexed with molecules such as ligands, ligand analogs, inhibitors, activators, agonists, antagonists, polypeptides, and other molecules. The structure coordinates, as well as models of the three-dimensional structures obtained therefrom, can also be used to aid the elucidation of solution-based structures of native or mutated receptor PTK extracellular domains, such as those obtained via NMR. Thus, the crystals and atomic structure coordinates of the invention provide a convenient means for elucidating the structures and functions of receptor tyrosine kinases.

For purposes of clarity and discussion, the crystals of the invention will be described by reference to specific FGFR1 D2-D3/FGF2 and FGFR1 D2-D3/FGF1 exemplary crystals. Those skilled in the art will appreciate that the principles described herein are generally applicable to crystals of the extracellular domain of any receptor tyrosine kinase, including but not limited to receptor PTKs such as are PDGFR, EGFR, VEGFR, HGFR, neurotrophinR, HER2, HER3, HER4, InsulinR, IGFR, CSFIR, FLK, KDR, VEGFR2, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, MUSK, members of the FGFR family, such as FGFR1, FGFR2, FGFR3, and FGFR4, and orphan receptor PTKs.

VII. Structure Determination for PTKs with Unknown Structure Using Structural Coordinates

Structural coordinates, such as those set forth in Tables 1–4 and 6 can be used to determine the three dimensional structures of RPTKs with unknown structure. The methods described below can apply structural coordinates of a polypeptide with known structure to another data set, such as an amino acid sequence, X-ray crystallographic diffraction data, or nuclear magnetic resonance (NMR) data. Preferred embodiments of the invention relate to determining the three dimensional structures of receptor PTKs and related polypeptides. These include receptor PTKs such as are PDGFR, EGFR, VEGFR, HGFR, neurotrophinR, HER2, HER3, HER4, InsulinR, IGFR, CSFIR, FLK, KDR, VEGFR2, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, MUSK, members of the FGFR family, such as FGFR1, FGFR2, FGFR3, and FGFR4, and orphan receptor PTKs.

Structures Using Amino Acid Homology

Homology modeling is a method of applying structural coordinates of a polypeptide of known structure to the amino acid sequence of a polypeptide of unknown structure. This method is accomplished using a computer representation of the three dimensional structure of a polypeptide or polypeptide complex, the computer representation of amino acid sequences of the polypeptides with known and unknown structures, and standard computer representations of the structures of amino acids. Homology modeling comprises the steps of (a) aligning the amino acid sequences of the polypeptides with and without known structure; (b) transferring the coordinates of the conserved amino acids in the known structure to the corresponding amino acids of the polypeptide of unknown structure; (c) constructing structures of the rest of the polypeptide; and (d) refining the subsequent three dimensional structure. One skilled in the art recognizes that conserved amino acids between two proteins can be determined from the sequence alignment step in step (a).

The above method is well known to those skilled in the art. Greer, 1985, Science 228, 1055. Blundell et al., 1988, Eur. J. Biochem. 172, 513. A computer program currently utilized for homology modeling by those skilled in the art is the Homology module in the Insight II modeling package distributed by Molecular Simulations Inc.

Alignment of the amino acid sequence is accomplished by first placing the computer representation of the amino acid sequence of a polypeptide with known structure above the amino acid sequence of the polypeptide of unknown structure. Amino acids in the sequences are then compared and groups of amino acids that are homologous (e.g., amino acid side chains that are similar in chemical nature—aliphatic, aromatic, polar, or charged) are grouped together. This method will detect conserved regions of the polypeptides and account for amino acid insertions or deletions.

Once the amino acid sequences of the polypeptides with known and unknown structures are aligned, the structures of the conserved amino acids in the computer representation of the polypeptide with known structure are transferred to the corresponding amino acids of the polypeptide whose structure is unknown. For example, a tyrosine in the amino acid sequence of known structure may be replaced by a phenylalanine, the corresponding homologous amino acid in the amino acid sequence of unknown structure.

The structures of amino acids located in non-conserved regions are to be assigned by either using standard peptide geometries or molecular simulation techniques, such as molecular dynamics. The final step in the process is accomplished by refining the entire structure using molecular dynamics and/or energy minimization.

The homology modeling method is well known to those skilled in the art and has been practiced using different protein molecules. For example, the three dimensional structure of the polypeptide corresponding to the catalytic domain of a serine/threonine protein kinase, myosin light chain protein kinase, was homology modeled from the cAMP-dependent protein kinase catalytic subunit. Knighton et al., 1992, Science 258:130–135.

Structures Using Molecular Replacement

Molecular replacement is a method of applying the X-ray diffraction data of a polypeptide of known structure to the X-ray diffraction data of a polypeptide of unknown sequence. This method can be utilized to define the phases describing the X-ray diffraction data of a polypeptide of unknown structure when only the amplitudes are known. X-PLOR is a commonly utilized computer software package used for molecular replacement. Brunger, 1992, Nature 355:472–475. AMORE is another program used for molecular replacement. Navaza, 1994, Acta Crystallogr. A50:157–163. Preferably, the resulting structure does not exhibit a root-mean-square deviation of more than 3 Å.

A goal of molecular replacement is to align the positions of atoms in the unit cell by matching electron diffraction data from two crystals. A program such as X-PLOR can involve four steps. A first step can be to determine the number of molecules in the unit cell and define the angles between them. A second step can involve rotating the diffraction data to define the orientation of the molecules in the unit cell. A third step can be to translate the electron density in three dimensions to correctly position the molecules in the unit cell. Once the amplitudes and phases of the X-ray diffraction data are determined, an R-factor can be calculated by comparing electron diffraction maps calculated experimentally from the reference data set and calculated from the new data set. An R-factor between 30–50% indicates that the orientations of the atoms in the unit cell are reasonably determined by this method. A fourth step in the process can be to decrease the R-factor to roughly 20% by refining the new electron density map using iterative refinement techniques described herein and known to those or ordinary skill in the art.

Structures Using NMR Data

Structural coordinates of a polypeptide or polypeptide complex derived from X-ray crystallographic techniques can be applied towards the elucidation of three dimensional structures of polypeptides from nuclear magnetic resonance (NMR) data. This method is used by those skilled in the art. Wuthrich, 1986, John Wiley and Sons, New York: 176–199; Pflugrath et al., 1986, J. Molecular Biology 189:383–386; Kline et al., 1986, J. Molecular Biology 189:377–382. While the secondary structure of a polypeptide is often readily determined by utilizing two-dimensional NMR data, the spatial connections between individual pieces of secondary structure are not as readily determinable. The coordinates defining a three-dimensional structure of a polypeptide derived from X-ray crystallographic techniques can guide the NMR spectroscopist to an understanding of these spatial interactions between secondary structural elements in a polypeptide of related structure.

The knowledge of spatial interactions between secondary structural elements can greatly simplify Nuclear Overhauser Effect (NOE) data from two-dimensional NMR experiments. Additionally, applying the crystallographic coordinates after the determination of secondary structure by NMR techniques only simplifies the assignment of NOEs relating to particular amino acids in the polypeptide sequence and does not greatly bias the NMR analysis of polypeptide structure. Conversely, using the crystallographic coordinates to simplify NOE data while determining secondary structure of the polypeptide would bias the NMR analysis of protein structure.

As the analysis of polypeptide structure by NMR methods is a relatively new technique, the use of structural coordinates defining an RPTK structure will most likely be utilized more frequently in the near future. As the method progresses, the three dimensional structure analysis of polypeptides of the same size as an RPTK extracellular domain will become more frequent.

VIII. Structure-Based Design of Modulators of PTK Function Utilizing Structural Coordinates

Structure-based modulator design and identification methods are powerful techniques that can involve searches of computer data bases containing a wide variety of potential modulators and chemical functional groups. The computerized design and identification of modulators is useful as the computer data bases contain more compounds than the chemical libraries, often by an order of magnitude. For reviews of structure-based drug design and identification see Kuntz et al., 1994, Acc. Chem. Res. 27:117; Guida, 1994, Current Opinion in Struc. Biol. 4: 777; Colman, 1994, Current Opinion in Struc. Biol. 4: 868.

The three dimensional structure of a polypeptide defined by structural coordinates can be utilized by these design methods. Preferably, the structural coordinates of Table 1 or Table 2 can be utilized by this method. In addition, the three dimensional structures of RPTKs determined by the homology, molecular replacement, and NMR techniques described herein can also be applied to modulator design and identification methods. Thus, the structures of receptor PTKs, such as are PDGFR, EGFR, VEGFR, HGFR, neurotrophinR, HER2, HER3, HER4, InsulinR, IGFR, CSFIR, FLK, KDR, VEGFR2, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, MUSK, members of the FGFR family, such as FGFR1, FGFR2, FGFR3, and FGFR4, and orphan receptor PTKs, can be utilized by the methods described herein.

Design by Searching Molecular Data Bases

One method of rational modulator design searches for modulators by docking the computer representation of compounds from a data base of molecules. Publicly available data bases include:

a) ACD from Molecular Designs Limited

b) NCI from National Cancer Institute

c) CCDC from Cambridge Crystallographic Data Center

d) CAST from Chemical Abstract Service

e) Derwent from Derwent Information Limited

f) Maybridge from Maybridge Chemical Company LTD

g) Aldrich from Aldrich Chemical Company

h) Directory of Natural Products from Chapman & Hall

One such data base (ACD distributed by Molecular Designs Limited Information Systems) contains, for example, 200,000 compounds that are synthetically derived or are natural products. Methods available to those skilled in the art can convert a data set represented in two dimensions to one represented in three dimensions. These methods are enabled by such computer programs as CONCORD from Tripos Associates or DB-Converter from Molecular Simulations Limited.

Multiple methods of structure-based modulator design are known to those in the art. Kuntz et al., 1982, J. Mol. Biol. 162: 269; Kuntz et al., 1994, Acc. Chem. Res. 27: 117; Meng et al., 1992, J. Compt. Chem. 13: 505; Bohm, 1994, J. Comp. Aided Molec. Design 8: 623.

A computer program widely utilized by those skilled in the art of rational modulator design is DOCK from the University of California in San Francisco. The general methods utilized by this computer program and programs like it are described in three applications below. More detailed information regarding some of these techniques can be found in the Molecular Simulations User Guide, 1995.

A typical computer program used for this purpose can comprise the following steps:

(a) remove an existing compound, ligand, or ligand analog from the protein;

(b) dock the structure of another compound, ligand, or ligand analog into the compound binding site using the computer program (such as DOCK) or by interactively moving the compound into the active-site;

(c) characterize the space between the compound and the binding site atoms;

(d) search libraries for molecular fragments which (i) can fit into the empty space between the compound and the active-site, and (ii) can be linked to the compound; and

(e) link the fragments found above to the compound and evaluate the new modified compound.

Part (c) refers to characterizing the geometry and the complementary interactions formed between the atoms of the RPTK and the compound, ligand, or ligand analog. A favorable geometric fit is attained when a significant surface area is shared between the compound and RPTK atoms without forming unfavorable steric interactions.

One skilled in the art would note that the method can be performed by skipping parts (d) and (e) and screening a data base of many compounds.

Structure-based design and identification of modulators of RPTK function can be used in conjunction with assay screening. As large computer data base of compounds (around 10,000 compounds) can be searched in a matter of hours, the computer based method can narrow the compounds tested as potential modulators of RPTK function in cellular assays.

The above descriptions of structure-based modulator design are not all encompassing and other methods are reported in the literature:

(1) CAVEAT: Bartlett et al., 1989, in “Chemical and Biological Problems in Molecular Recognition”, Roberts, S. M.; Ley, S. V.; Campbell, M. M. eds.; Royal Society of Chemistry: Cambridge, pp182–196.

(2) FLOG: Miller et al., 1994, J. Comp. Aided Molec. Design 8:153.

(3) PRO Modulator: Clark et al., 1995, J. Comp. Aided Molec. Design 9:13.

(4) MCSS: Miranker and Karplus, 1991, Proteins: Structure, Function, and Genetics 11:29.

(5) AUTODOCK: Goodsell and Olson, 1990, Proteins: Structure, Function, and Genetics 8:195.

(6) GRID: Goodford, 1985, J. Med. Chem. 28:849.

Design by Modifying Compounds in Complex with RPTKs

Another way of identifying compounds, ligands, or ligand analogs as potential modulators is to modify an existing modulator in the polypeptide active-site. For example, the computer representation of modulators can be modified within the computer representation of a RPTK ligand binding site. Detailed instructions for this technique can be found in the Molecular Simulations User Manual, 1995 in LUDI. The computer representation of the modulator is modified by changing, deleting, or adding one or chemical groups.

Upon each modification to the compound, ligand, or ligand analog, the atoms of the modified compound, ligand, or ligand analog and the RPTK can be shifted in conformation, and the distance between the compound, ligand, or ligand analog and the RPTK atoms may be scored along with any complimentary interactions formed between the two molecules. Scoring can be complete when a favorable geometric fit and favorable complementary interactions are attained. Compounds that have favorable scores are potential modulators of RPTK function.

Design by Modifying the Structure of Compounds that Bind Receptor PTKs

A third method of structure-based modulator design is to screen compounds designed by a modulator building or modulator searching computer program. Examples of these types of programs can be found in the Molecular Simulations Package, Catalyst. Descriptions for using this program are documented in the Molecular Simulations User Guide (1995). Other computer programs used in this application are ISIS/HOST, ISIS/BASE, ISIS/DRAW) from Molecular Designs Limited and UNITY from Tripos Associates.

These programs can be operated on the structure of a compound, ligand, or ligand analog that has been removed from the active-site of the three dimensional structure of a compound, ligand, or ligand analog-completed RPTK complex. Operating the program on such a compound, ligand, or ligand analog is preferable since it is in a biologically active conformation.

A modulator construction computer program is a computer program that may be used to replace computer representations of chemical groups in a compound, ligand, or ligand analog complexed with a RPTK with groups from a computer data base. A modulator searching computer program is a computer program that may be used to search computer representations of compounds from a computer data base that have similar three dimensional structures and similar chemical groups as compounds bound to a receptor PTK.

A typical program can operate by using the following general steps:

(a) map the compounds, ligands, or ligand analogs by chemical features such as by hydrogen bond donors or acceptors, hydrophobic/lipophilic sites, positively ionizable sites, or negatively ionizable sites;

(b) add geometric constraints to the mapped features; and

(c) search data bases with the model generated in (b).

Those skilled in the art recognize that important chemical features include, but are not limited to, a hydrogen bond donor, a hydrogen bond acceptor, and/or two hydrophobic points of contact. Those skilled in the art also recognize that not all of the possible chemical features of the compound need be present in the model of (b). One can use any subset of the model to generate different models for data base searches.

IX. Organic Synthetic Techniques

The versatility of computer-based modulator design and identification lies in the diversity of structures screened by the computer programs. The computer programs can search data bases that contain 200,000 molecules and can modify modulators already complexed with a polypeptide, using a wide variety of chemical functional groups. A consequence of this chemical diversity is that a potential modulator of RPTK function may take a chemical form that is not predictable. A wide array of organic synthetic techniques exist in the art to meet the challenge of constructing these potential modulators of RPTK function. Many of these organic synthetic methods are described in detail in standard reference sources utilized by those skilled in the art. One example of such a reference is March, 1994, Advanced Organic Chemistry, Reactions, Mechanisms, and Structure, New York, McGraw Hill. Thus, the techniques required to synthesize a potential modulator of RPTK function identified by computer-based methods are readily available to those skilled in the art of organic chemical synthesis.

X. Cellular Assays Measuring the Effect of a Receptor PTK Modulator in Signal Transduction Pathways

Cellular assays can be used to test the activity of a potential modulator of RPTK function as well as diagnose a disease associated with inappropriate RPTK activity. A potential modulator of RPTK function can be tested for activity in vitro by assays that measure the effect of a potential modulator on the autophosphorylation of a particular RPTK over-expressed in a cell line. Thus, a modulator that acts as a potent inhibitor of ligand binding to the extracellular domain corresponding to a RPTK would decrease the amount of autophosphorylation catalyzed by that RPTK. Potential modulators could also be tested for activity in cell growth assays in vitro as well as in animal model assays in vivo.

In vivo assays are also useful for testing the bioactivity of a potential modulator designed by the methods of the invention.

Materials, methods, and experimental data for these assays are fully described in U.S. Pat. No. 5,792,783, and WO 96/40116 published on Dec. 19, 1996, entitled “Indolinone Compounds for the Treatment of Disease,” each of which is incorporated herein by reference in its entirety, including all drawings, figures, and tables.

XI. Administration of Modulators of Receptor PTK Function as Therapeutics for Disease

Methods of administering compounds to organisms as therapeutics for disease are fully described in U.S. Pat. No. 5,792,783, and WO 96/40116 published on Dec. 19, 1996, entitled “Indolinone Compounds for the Treatment of Disease,” each of which is incorporated herein by reference in its entirety, including all drawings, figures, and tables.

XII. Computer-Based Systems for Determining, Designing, Modeling and/or Modifying Molecular Structures

An illustrative computer based system 10 is depicted in FIG. 33 for displaying, studying, comparing, manipulating, interpreting and/or extrapolating data from the crystallographic analysis of molecular structures which include molecules, portion(s) of molecules and/or molecular interactions, such as the molecular structures of RPTKs, their ligands and related complexes depicted in FIGS. 1, 2, 5, 19, 26 and 27. Exemplary molecules are proteins and/or complexes of proteins with ligands. Exemplary molecular portions are catalytic domains of proteins, ligand/receptor binding sites of proteins, signaling regions of proteins and transport regions of proteins. Exemplary molecular interactions include binding between an enzyme and its substrate, factor/co-factor relationships, antibody/antigen binding, and protein/receptor recognition and binding, such as that occurring in signal transduction. One or more of the above types of studies are useful for elucidating and understanding natural biochemical processes and to design and screen mimetics, agonists, inhibitors, and antagonists. Thus, this aspect of the invention, among other things, permits the skilled person to understand and practice molecular modeling processes and provides the skilled person with the necessary hardware and software to create and display images that represent the multi-dimensional structure of a molecule, molecular portion or molecular interaction, as desired. Thus, these undertakings are greatly facilitated by employing computer technology.

The system 10 includes data storage entity(ies) 20, such as a memory (e.g., as archival memory and/or video memory and computer-readable medias), that retrievably stores information representing molecule, molecule portions and/or molecular interactions. The memory typically has a first-type storage region or capability 22, having recorded thereon or contained therein structural data, like a set of spatial (atomic) coordinates, specifying a location in a three dimensional space, as disclosed herein or obtained in accordance with the teachings contained herein. The memory also can have a second-type storage region or capability 24, which contains information. This information typically represents a property, characteristic or attribute of one of a plurality of amino acids, or other chemical moiety, for example. A second-type storage region or capability can be associated with the first-type storage regions in the storage entity 20 to represent a geometric and/or spatial arrangement of at least one characteristic, property or attribute of a molecule, molecule portion or molecular interaction, preferably one that represents three dimensional space. The memory can take the form of any type recognizable by the skilled person such as RAM and ROM, and other computer-readable mediums like magnetic media, optical media, magnetic-optical media, floppy disks, hard disks, mini-disks, servers, web-based systems, CD, DVD, tape, etc. Memory 22 (a type of storage region or capability) can include or contain, for example, the coordinate data shown in Tables 1, 2, 3, 4 or 6, or other coordinates obtained in accordance with the present teachings, and memory 24 (a type of storage region or capability) can include or contain associated charge or electron density data, for example. Quite commonly, the system includes a plurality of the first-type and second-type storage regions. The storage entities 20, namely the first-type storage regions or capabilities 22, said second-type storage regions or capabilities 24, and the storage devices or capabilities 34 can be regions of, for example, a shared semiconductor memory, cache, RAM, ROM, regions of a shared optical disk, regions of a shared magnetic memory, and/or be server based to be accessible by intranet and the internet, including the world wide web. Thus, the systems of the present invention include unitary systems, network-based systems, satellite communications, and internet-based systems, which can be interactively connected regardless of geography.

The system 10 also includes a processor and/or is interactively associated with a processor, interactively coupled to the data storage entity(ies) to access the first-type storage regions 22 and optionally the second-type storage regions 24, to generate image signals for depicting a visual three dimensional image of at least one characteristic of the molecule, molecule portion or molecular interaction in the three dimensional space based on data from the storage entity 20. The processor can be a general or special purpose processor with a CPU, register, memory and the like. Software, and logic architecture and circuitry, can be employed as desired. According to one embodiment, processor 26 and storage entity 20, among other things, can be in the form of a UNIX or VAX computer, such those available from Silicon Graphics, Sun Microsystems, and IBM. However, the invention is not limited to use of these types of hardware and software systems.

A display 28 is commonly interactively coupled to the processor 26 via lines or a wireless connection 30 to receive the image signals in order to depict a visual three dimensional image of at least one characteristic of a molecule, molecule portion or molecular interaction in the three dimensional space based on the data. Suitable displays for use in the system include a computer screen 32 (e.g., CRT, LCD, active and passive matrix, etc.), printer, plotter or film.

In one embodiment of the invention, the image data includes data for depicting a visual three dimensional image of a structure of molecule, molecule portion or molecular interaction in three dimensional space, such as shown in FIGS. 1, 2, 5, 19, 26 and 27. In another embodiment, the image data includes data for depicting a visual three dimensional image of a solid model representation of molecule, molecule portion or molecular interaction in three dimensional space. In still another embodiment, the image data includes data for depicting a visual three dimensional image of electrostatic surface potential of molecule, molecule portion or molecular interaction in three dimensional space. In yet another embodiment, the image data includes data for depicting a visual three dimensional stereo image of molecule, molecule portion or molecular interaction in three dimensional space.

The system 10 of the present invention may further comprise a storage device, structure, region or capability 34 that stores data representing a geometric and/or spatial arrangement of a characteristic of a composition in addition to the molecule, molecule portion or molecular interaction, such as shown in FIGS. 9, 10, 22 and 24. Storage devices or capabilities 34 can include or contain, for example, the three-dimensional X-ray coordinate data for other chemical entities, including other proteins for comparison purposes. The storage devices and capabilities 34 can take the form of any type recognizable by the skilled person such as RAM and ROM, and other computer-readable mediums like magnetic media, optical media, magnetic-optical media, floppy disks, hard disks, mini-disks, servers, CD, DVD, tape, etc. The processor 26 can be interactively coupled to the storage device or capability 34 and the display 28, and generates additional image data for depicting the geometric arrangement of the characteristic of the composition relative to said visual three dimensional image of said at least one characteristic of the molecule, molecule portion or molecular interaction on the screen 32 based on instructions. In the FIG. 33 embodiment, the storage device or capability 34 is shown as part of the storage entity 20, although other arrangements are available to the skilled person.

The computer system includes or employs instructions, which can be software or hardware based. The instructions, such as those in logic circuits and software program(s), permit the computer system to, among other things, input, handle, analyze and output data. Exemplary programs are identified herein, although the skilled person is not limited to such programs in the practice of the invention.

Typically, the system 10 also includes an operator interface 36, such as a mouse, tracker ball, touch pad, projector (including multi-dimensional projector systems), touch screen, joy stick, pointer, keyboard, modem, card and/or voice recognition system, or docking system for receiving instructions from a operator, which is interactively connected with the display 28, processor 26 and storage entity(ies) 20. Other aspects of computers and computer components are well-known, and are readily obtained.

The computer systems according to the invention, including storage entity 20 (including 22, 24, 34, and others as well) can be programmed and contain data to undertake the analyses discussed in Sections VI–IX above, for example, including the use of x-ray crystallographic data in conjunction with other analytical techniques, such as NMR.

The invention also includes computer-readable media containing various data structures and the information disclosed herein. For example, magnetic media, optical media, magnetic-optical media, floppy disks, hard disks, mini-disks, servers, CD, DVD, tape, etc. containing the coordinate data set forth in the accompanying tables and figures, when computer analyzed according to set(s) of instructions and rules provided by hardware and/or software, are useful for ascertaining the three-dimensional structures of molecules, molecular portions and molecular interactions.

EXAMPLES

The examples below are non-limiting and are merely representative of various aspects and features of the present invention. The examples provide illustrative methods for obtaining crystalline forms of protein kinase polypeptides, methods for determining three dimensional structures of these protein kinase polypeptides, and methods for identifying modulators of protein kinases using the three dimensional structures of the protein kinases.

Atomic Structural Coordinates

Tables 1–3 provide the atomic structural coordinates for a number of ligand/FGFR complex dimers. Table 5 provides the atomic structural coordinates for a SCF dimer. Table 6 provides the atomic structural coordinates for a the ternary FGF2-FGFR1-heparin complex. The following abbreviations are used in the Tables:

“Atom Type” refers to the element whose coordinates are provided. The first letter in the column defines the element.

“A.A.” refers to amino acid.

“X, Y and Z” provide the Cartesian coordinates of the element.

“B” is a thermal factor that measures movement of the atom around its atomic center.

“OCC” refers to occupancy, and represents the percentage of time the atom type occupies the particular coordinate. OCC values range from 0 to 1, with 1 being 100%.

“PRT1” or “PRT2” relate to occupancy, with PRT1 designating the coordinates of the atom when in the first conformation and PRT2 designating the coordinates of the atom when in the second or alternate conformation.

The structural coordinates for the dimers may be modified by mathematical manipulation. Such manipulations include, but are not limited to, crystallographic permutations of the raw structure coordinates, fractionalization of the raw structure coordinates, integer additions or subtractions to sets of the raw structure coordinates, inversion of the raw structure coordinates and any combination of the above.

In addition, the structural coordinates can be slightly modified and still render nearly identical three dimensional structures. Therefore, a measure of a unique set of structural coordinates is the root-mean-square deviation of the resulting structure. Structural coordinates that render three dimensional structures that deviate from one another by a root-mean-square deviation of less than 1.5 Å may be viewed as identical.

Example 1 X-ray Crystallographic Structure Determination of FGFR1 D2-D3/FGF2 Complexes

Polypeptide Synthesis and Isolation

A DNA fragment encoding residues 142–365 of human FGFR1 (“D2-D3”) was subcloned into bacterial expression vector pET-23a using NcoI and HindIII restriction sites using techniques well known to the skilled artisan. Bacterial strain BL21 (DE3) was used for expression of D2-D3, and was induced with IPTG for 5 hours. Following induction of expression, the cells were collected by centrifugation, and lysed using a French press in a buffer containing 25 mM potassium phosphate, 150 mM NaCl, 2 mM EDTA, and 10% glycerol.

A pellet containing D2-D3 was collected by centrifugation, and dissolved in 6M guanidium hydrochloride, 100 mM Tris-HCl, pH 8.0. D2-D3 was allowed to refold by dialyzing for 48 hours against a buffer containing 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 10% glycerol, and 1 mM L-cysteine. The refolded D2-D3 was chromatographed on a heparin sepharose column on which FGF2 had been previously immobilized. The resulting D2-D3/FGF2 complex was eluted from the heparin sepharose column with a buffer containing 25 mM Tris-HCl, pH 7.5, and 1.5 M NaCl.

The D2-D3/FGF2 complex was concentrated by ultrafiltration using a Centricon 10™ (Amicon) centrifugal concentrator, and further purified by size exclusion chromatography on a Superdex™ 200 column (Pharmacia) using a buffer containing 25 mM Tris-HCl, pH 7.5, and 1.5 M NaCl. Prior to crystallization, the D2-D3/FGF2 complex was concentrated to 10 mg/mL in a buffer containing 25 mM Tris-HCl, pH 7.5, and 150 mM NaCl.

Crystal Growth

Crystals of purified D2-D3/FGF2 complex were grown at 20° C. by vapor diffusion in hanging drops by mixing equal volumes of protein solution (10 mg/mL D2-D3/FGF2 complex in 25 mM Tris-HCl, pH 8.5, and 150 mM NaCl) and reservoir buffer (1.6 M (NH₄)₂SO₄, 20% v/v glycerol and 100 mM Tris-HCl, pH 8.5), and suspending a 2.0 μl hanging drop of the resulting solution over 0.5 mL reservoir buffer at 20° C.

Data Collection and Structure Determination

Diffraction data were collected from a crystalline specimen, which had been flash frozen in a dry nitrogen stream, at beamline X-4A at the National Synchrotron Light Source, Brookhaven National Laboratory. Synchrotron data were collected on a CCD detector. All data were processed using DENZO and SCALEPACK. Otwinowski, 1993, “Oscillation data reduction program,” Proceedings of the CCP4 Study Weekend, Sawyer et al., eds. (Daresbury, United Kingdom: SERC Daresbury Laboratory), 56–62.

The structure of the D2-D3/FGF2 complex was determined by molecular replacement using the program AmoRe (Navaza, 1994, Acta Cryst. A 50: 157–163) using the structures of FGF2 (2FGF, Zhang et al., 1991, Proc. Natl. Acad. Sci. 88: 3446–3450) and telokin (1TLK, Holden et al., 1992, J. Mol. Biol. 227: 840–851) as search models. Homology models were constructed from the telokin structure for the FGFR1 D2 and D3 domains. A molecular replacement solution was determined for both FGF2 molecules and one copy of D2 and D3 in the dimer, and the second copy of D2 and D3 was determined by rigid body rotation and translation of the first copy of D2 and D3 onto the second FGF2 molecule. The placement of the second copy of D2 and D3 was confirmed by rigid body refinement techniques using CNS (Brunnger et al., 1998, Acta Cryst. D 54: 905–921).

Simulated annealing and positional B-factor refinement were performed using CNS, and bulk solvent and anisotropic B-factor corrections were applied. Additionally, tight noncrystallographic symmetry constraints were imposed during refinement of the backbone atoms of FGF2, D2, and D3. RMS deviation for Cα atoms between the two copies of FGF2, D2, or D3 in the dimer was 0.04 Å.

Model building into the electon density maps was performed using the program O (Jones et al., 1991, Acta Cryst. A 47: 110–119). The atomic model of the D2-D3/FGF2 complex includes FGF2 residues 16–144 and FGFR1 residues 149–359, except in one of the FGFR1 receptors in the dimer, where residues 293–307 are disordered. The average B-factor for all atoms is 38.7 Å² for all atoms, 37.6/38.9 Å² for FGF2, and 38.3/39.1 Å² for FGFR1.

Atomic Structural Coordinates

Table 1 provides the atomic structural coordinates of the FGFR1(D2-D3)/FGF2 complex dimer complex dimer. The structure of the FGFR1(D2-D3)/FGF2 complex has been described in Plotnikov et al., Cell 98, 641–650 (1999) and the coordinates for the FGFR1(D2-D3)/FGF2 complex are available on the internet through the Protein Data Bank (assigned Protein Data Bank ID code 1CVS), the disclosures of which are herein incorporated by reference.

Example 2 X-ray Crystallographic Structure Determination of FGFR1 D2-D3/FGF1 Complexes

Polypeptide Synthesis and Isolation

A DNA fragment encoding residues 142–365 of human FGFR1 (“D2-D3”) was subcloned into bacterial expression vector pET-23a using NcoI and HindIII restriction sites using techniques well known to the skilled artisan. Bacterial strain BL21(DE3) war used for expression of D2-D3, and was induced with IPTG for 5 hours. Following induction of expression, the cells were collected by centrifugation, and lysed using a French press in a buffer containing 25 mM potassium phosphate, 150 mM NaCl, 2 mM EDTA, and 10% glycerol.

A pellet containing D2-D3 was collected by centrifugation, and dissolved in 6M guanidium hydrochloride, 100 mM Tris-HCl, pH 8.0. D2-D3 was allowed to refold by dialyzing for 48 hours against a buffer containing 50 mM Tris-HCl, pH 8.0, 150 mM NaCl, 10% glycerol, and 1 mM L-cysteine. The refolded D2-D3 was chromatographed on a heparin sepharose column on which FGF1 had been previously immobilized. The resulting D2-D3/FGF1 complex was eluted from the heparin sepharose column with a buffer containing 25 mM Tris-HCl, pH 7.5, and 1.5 M NaCl.

The D2-D3/FGF1 complex was concentrated by ultrafiltration using a CENTRICON 10™ (Amicon) centrifugal concentrator, and further purified by size exclusion chromatography on a SUPERDEX™ 200 column (Pharmacia) using a buffer containing 25 mM Tris-HCl, pH 7.5, and 1.5 M NaCl. Prior to crystallization, the D2-D3/FGF1 complex was concentrated to 1 mg/mL in a buffer containing 25 mM Tris-HCl, pH 7.5, and 10 mM NaCl.

Crystal Growth

Crystals of purified D2-D3/FGF1 complex were grown at 20° C. by vapor diffusion in hanging drops by mixing one volume of protein solution (1 mg/mL in 25 mM Tris-HCl, pH 8.5, and 150 mM NaCl) with four volumes of reservoir buffer (20% PEG 4000, 0.2 M Li2SO₄, and 0.1 M Tris-HCl, pH 8.5), and suspending a 2.0 μl hanging drop of the resulting solution over 0.5 mL reservoir buffer at 20° C.

Data Collection and Structure Determination

Diffraction data were collected from a crystalline specimen, which had been flash frozen in mother liquor containing 10% glycerol using a dry nitrogen stream, at beamline X-4A at the National Synchrotron Light Source, Brookhaven National Laboratory. Synchrotron data were collected on a CCD detector. All data were processed using DENZO and SCALEPACK. Otwinowski, 1993, “Oscillation data reduction program,” Proceedings of the CCP4 Study Weekend, Sawyer et al., eds. (Daresbury, United Kingdom: SERC Daresbury Laboratory), 56–62.

The structure of the D2-D3/FGF1 complex was determined by molecular replacement using the program AmoRe (Navaza, 1994, Acta Cryst. A 50: 157–163) using the structures of FGF1 (2AFG, Blaber et al., 1996, Biochemistry 35: 2086–2094) and telokin (1 TLK, Holden et al., 1992, J. Mol. Biol. 227: 840–851) as search models. Homology models were constructed from the telokin structure for the FGFR1 D2 and D3 domains. A molecular replacement solution was determined for two copies each of FGF1, D2, and D3 in the dimer.

Simulated annealing and positional B-factor refinement were performed using CNS, and bulk solvent and anisotropic B-factor corrections were applied. Additionall, tight noncrystallographic symmetry constraints were imposed during refinement of the backbone atoms of FGF1, D2, and D3. RMS deviation for Cα atoms between the two copies of FGF1, D2, or D3 in the dimer was 0.01 Å.

Model building into the electon density maps was performed using the program 0 (Jones et al., 1991, Acta Cryst. A 47: 110–119). The atomic model of the D2-D3/FGF1 complex includes FGF1 residues 8–138 and FGFR1 residues 147–359 except residues 294–305 and 315–323, which are disordered. The average B-factor for all atoms is 30.4 Å² for all atoms, 31.2/33.0 Å² for FGF1, and 29.1/28.7 Å² for FGFR1.

Atomic Structural Coordinates

Table 2 provides the atomic structural coordinates of the FGFR1(D2-D3)/FGF1 complex dimer. In the first FGFR1 molecule of the dimer the residue number is preceded by a 1, i.e., residue number 464 of the first FGFR1 molecule of the dimer is denoted by “1464”. The structure of the FGFR1(D2-D3)/FGF1 complex has been described in Plotnikov et al., Cell 101, 413–424 (2000) and the coordinates for the FGFR1(D2-D3)/FGF1 complex are available on the internet through the Protein Data Bank (assigned Protein Data Bank ID code 1EVT), the disclosures of which are herein incorporated by reference.

Example 3 Determination of the FGF2-FGFR2 Structure Crystallization and Data Collection

DNA fragments encoding residues 147 to 366 of FGFR2 were amplified by polymerase chain reaction (PCR) and subcloned into the bacterial expression vector pET-28a using NcoI and HindIII cloning sites and transfected into the bacterial strain BL21(DE3). Cells were induced with IPTG for 5 hours, centrifuged and the bacterial pellet was lysed in 25 mM K—Na phosphate buffer pH 7.5 containing 150 mM NaCl, 2 mM EDTA and 10% glycerol using a French press. Following centrifugation, the pellet containing primarily FGFR2 was dissolved in 6M guanidium hydrochloride and 10 mM DTT in 100 mM Tris-HCl buffer (pH 8.0). The solubilized FGFR2 protein was refolded by dialysis against 25 mM HEPES buffer pH 7.5 containing 150 mM NaCl, 10% Glycerol, and 1 mM L-Cysteine. The refolded FGFR2 protein was loaded onto heparin sepharose columns on which FGF2 (basic FGF) had previously been immobilized. The FGF2-FGFR2 complex was then eluted from the heparin sepharose column with a buffer containing 25 mM Tris-HCl (pH 7.5) and 1.5M NaCl. The FGF2-FGFR2 complex was concentrated using Centricon 10 (Amicon) filters and further purified by size exclusion chromatography (Pharmacia, Superdex 200) with a buffer containing 25 mM Tris-HCl (pH 7.5) and 1.5M NaCl. The complex migrated at a position consistent with the formation of a 1:1 FGF:FGFR complex.

Crystals were grown by vapor diffusion at 20° C. using the hanging drop method. For crystallization of the FGF2-FGFR2 complex, 2 microliters of protein solution 10 mg/ml, 25 mM Tris-HCl (pH 7.5), 150 mM NaCl) were mixed with 2 microliters of the crystallization buffer containing 10–15% PEG 4000, 10% isopropanol, and 0.1M HEPES—NaOH (pH 7.5). The FGF2-FGFR2 crystals belong to the triclinic space group P1 with unit cell dimensions a=72.20 Å, b=71.68 Å, c=90.92 Å, α=90.53°, β=89.98° and γ89.99°. There are four molecules of FGF2 and four molecules of FGFR2 in the unit cell with a solvent content of ˜58%. Diffraction data were collected from flash-frozen (in a dry nitrogen stream using mother liquor containing 10% glycerol as cryo-protectant) crystals on a CCD detector (FGF2-FGFR2) at beamline X4A at the National Synchrotron Light Source, Brookhaven National Laboratory. All data were processed using DENZO and SCALEPACK (Otwinowski et al., Methods Enzymol. 276, 307–326 (1997)).

Structure Determination and Refinement of the FGF2-FGFR2 structure

The structure of the FGF2-FGFR2 complex was determined by molecular replacement using the program AmoRe (Navaza, Acta Cryst. A 50, 157–163 (1994)) and the structure of FGF2-FGFR1 (1CVS; Plotnikov et al., Cell 98, 641–650 (1999)) as the search model. A molecular replacement solution was found for four copies of FGF2-FGFR2 complexes. Model building and refinement were performed with the programs O (Jones et al., Acta Crystallogr. A 47, 110–119 (1991)) and CNS (Brünger et al., Acta Crystallogr. D 54, 905–921 (1998)), respectively. Tight non-crystallographic symmetry restraints were imposed throughout the refinement for the backbone atoms of FGF2, D2 and D3. The structures of the FGF2-FGFR2 complex and the related FGF1-FGFR1 complex are reported together with the corresponding X-ray coordinates in Plotnikov et al., Cell 101: 413–24 (2000), the disclosure of which is herein incorporated by reference.

The atomic model for FGF2-FGFR2 consists of four FGF2 molecules, four FGFR2 molecules, four sulfate ions, and 263 water molecules. The structure of FGF2-FGFR2 was refined at 2.2 Å with an R value of 24.8% (free R value of 27.3%). Data collection and refinement statistics are given in Table 7. The atomic model includes FGF2 residues 16–145 and FGFR2 residues 148–365, 4 sulfate ions, and 263 water molecules. In all four FGFR2 molecules residues 295–306 (βC-βC′ loop in D3) are disordered. The average B-factor is 40.5 Å² for FGF2 molecules, 37.7 Å² for FGFR2 molecules, 73 Å² for sulfate ions, and 32.6 Å² for water molecules.

Atomic Structural Coordinates

Table 3 provides the atomic structural coordinates of the FGF2/FGFR2 complex dimer. The structure of the FGFR2/FGF2 complex has been described in Plotnikov et al., Cell 101, 413–424 (2000) and the coordinates for the FGFR2/FGF2 complex are available on the internet through the Protein Data Bank (assigned Protein Data Bank ID code 1 EV2), the disclosures of which are herein incorporated by reference. Table 3 contains sequence data that meets the requirements for inclusion into a Sequence Listing. Sequences SEQRES1A (p. 292) through SEQRES17H (p. 294) have been assigned SEQ ID NOS 50–157, respectively, in order of appearance, with the exceptions of nonqualifying sequences SEQRES11A, SEQRES11B, SEQRES11C, and SEQRES11D.

TABLE 7 Summary of Crystallographic Analysis Data Collection Statistics Struc- Resolu- Reflections Complete- R_(sym) ^(a) Signal ture tion (Å) (total/unique) ness (%) (%) (<l/δl>) FGF1- 25.0–2.8 49288/22330 97.9(90.5)^(b) 8.3(22.6)^(b) 8.6 FGFR1 FGF2- 25.0–2.2 206913/93440  96.3(87.8)^(b) 4.2(24.1)^(b) 16.3 FGFR2 Refinement Statistics^(c) Root-mean-square Deviations R_(cryst)/ B- Struc- Resolu- Reflec- R_(free) ^(d) Bonds Angles factors^(θ) ture tion (Å) tions (%) (Å) (°) (Å²) FGF1- 25.0–2.8 21539 24.9/30.0 0.009 1.5 2.3 FGFR1 FGF2- 25.0–2.2 84816 24.8/27.3 0.007 1.3 1.0 FGFR2 ^(a)R_(sym) = 100 × Σ_(hkl)Σ_(i)|l_(i)(hkl) − <l(hkl)>|/Σ_(hkl)Σ_(i)l_(i)(hkl). ^(b)Value in parentheses is for the highest resolution shell: 2.90–2.80 Å (FGF1-FGFR1), 2.28–2.20 Å (FGF2-FGFR2). ^(c)Atomic model: 4963 protein atoms and 4 SO₄ ions (FGF1-FGFR1) and 9818 protein atoms, 4 SO₄ ions, and 263 water molecules (FGF2-FGFR2). ^(d)R_(cryst/free) = 100 × Σ_(hkl)||F_(o)(hkl)| − |F_(c)(hkl)||/Σ_(hkl)|F_(o)(hkl)|, where F_(o) (>0δ) and F_(c) are the observed and calculated structure factors, respectively. 5% of the reflections were used for calculation of R_(free). ^(e)For bonded protein atoms.

Example 4 SCF Production and Structure Determination

Protein Expression, Refolding and Purification

Residue 1–141 of human stem cell factor (“SCF”) were expressed in E. coli as inclusion bodies as described previously (Langley et al., Arch. Biochem. Biophys. 295, 21–28 (1992)). Inclusion bodies from 1 liter of bacterial culture were dissolved in 25 to 30 ml of 6M guanidine hydrochloride solution. After the solution became clear, DTT was added to a final concentration of 40 mM and incubated at 37° C. for 30 minutes. The resulting solution was diluted into 4 liters of buffered solution (10 mM Tris, pH 8.5) and allowed to stand overnight. Refolded protein was purified by ion-exchange chromatography. Protein purity, electrophoretic mobility, and biological activity were compared to SCF that had been prepared with an established procedure (Langley et al., Arch. Biochem. Biophys. 295, 21–28 (1992)) and to a commercially available sample of SCF. Disulfide linked SCF dimers were not detected in this preparation as revealed by non-reducing gel electrophoresis (Langley et al., Arch. Biochem. Biophys. 295, 21–28 (1992)).

Crystallization and Data Collection

Crystals of SCF were grown by vapor diffusion at 20° C. using the hanging drop method. Two crystal forms are produced. Orthorhombic crystals with unit cell dimensions a =72.47 Å, b=83.45 Å and c=89.15 Å were grown by mixing 2 microliters of protein sample (15˜20 mg/ml) with 2 microliters of reservoir consisting of 25˜30% PEG 400, 0.25 M CaCl₂, and 0.1 M HEPES (pH 7.0). The addition of 1 mM SmCl₃ to the protein solution produced the monoclinic crystals that were used in the structure determination (see Table 4). Monoclinic crystals appeared within hours of set up.

Crystals for data collections were flash-frozen in liquid propane directly from the crystallization drops. Initial characterization of the SCF crystals was done at synchrotron beamlines X26C and X4A of the National Synchrotron Light Source, Brookhaven National Laboratory and the final data collection was done at Argonne National Laboratory Structural Biology Center beamline 19-ID at the Advanced Photon Source. All data were processed using DENZO and the intensities were reduced and scaled using SCALEPACK (Otwinowski et al., Methods Enzymol. 276,307–326 (1997)).

Structure Determination

A molecular replacement attempt with the data collected from the orthorhombic crystals using a model built from the alpha C atom positions of the human colony stimulating factor was not successful. Data used for the structure determination were collected from the monoclinic crystals at wavelengths 1.01 Å and 1.5 Å that are not at the absorption edge of Sm. The anomalous signal was clear from Patterson difference maps. The heavy metal position refinement and phasing was done with PHAESE (Furey et al., Methods Enzymol. 277, 590–620 (1997)). A total of three Sm sites were used for phasing while four Sm atoms were placed in the final model. Only short pieces of helices were visible from the initial solvent flattened electron density map and they were built into the density with program 0 (Jones et al., Acta Crystallogr. A 47, 110–119 (1991)). Repeated cycles of model building and solvent flattening combined with partial structures were performed until most of all four molecules in the asymmetric unit were built. Subsequent refinements were carried out against the lower energy (wavelength of 1.01 Å) diffraction data with Crystallography and NMR System (CNS) (Brunger et al., Acta. Crystallogr. D 54, 905–921 (1998)). Refinement progress was monitored with the R_(free) value using a 10% randomly selected test data set, and residue positions adjusted against 2Fo-Fc electron density maps.

The structure was determined by using anomalous scattering differences of samarium ions in the crystal at two wavelengths and refined to 2.3 Å (Table 4). There are four molecules in each asymmetric unit and the initial experimental electron density clearly showed the four-helix bundle and two beta strands in the molecules. The connecting loops, as well as the N-terminal and C-terminal regions, were built from 2Fo-Fc maps. Table 4 gives the statistics of the final model, which contains 120 solvent molecules, four samarium ions, two calcium ions and one Tris molecule. The structure of the human stem cell factor homodimer has been described in Zhang et al., Proc. Nat. Acad. Sci. 97(14), 7732–7737 (2000) and the coordinates for the human SCF dimer are available on the internet through the Protein Data Bank (Protein Data Bank ID code IEXZ), the disclosures of which are herein incorporated by reference.

General Features of the Structure

Although there are four SCF protomers in the crystallographic asymmetric unit, the biological dimer is unmistakably recognizable. The four protomers are superimposable except for the N-terminal and C-terminal loop regions. These loops are flexible and adopt multiple conformations in the four molecules in the asymmetric unit. The protomers in the biological dimer are packed head-to-head in a manner of almost perfect C2 symmetry (see FIG. 19). The dimer bends approximately 30° toward the side of the beta strands, resulting in an elongated shape with approximate dimensions of 87 Å×32 Å×25 Å.

SCF is a non-covalent homodimer composed of two slightly wedged protomers. The overall topology of a SCF protomer displays an antiparallel four-helix bundle fold (see FIG. 19), in a manner similar to other short-chain helix cytokines (Roswarski et al., Structure 2, 159–173 (1994)). The helices run up-up-down-down, with two crossing beta strands wrapped on one side. The structure of the dimer interface shows that dimerization is mediated by extensive polar and non-polar interactions between the two protomers with a large buried surface area The structure includes a hydrophobic crevice and a charged region at the tail of each protomer that functions as a potential receptor binding site. The X-ray structure of SCF shows that there are extensive interactions between the two SCF protomers, with approximately 1700 Å² surface area buried upon dimerization (calculated with a probe of radius 1.4 Å). This buried surface area accounts for about 20% of the total surface of each individual protomer, and is twice that reported for the 850 Å² buried surface area of the disulfide linked M-CSF dimer.

The side chains of the hydrophobic residues of the four helices pack the core of each monomer. Cys4 and Cys89 as well as Cys43 and Cys138 form two intramolecular disulfide pairs. Both disulfide bonds are located at one end (tail) of each protomer away from the dimer interface. The Cys4–Cys89 disulfide bond is more exposed than Cys43–Cys138, a disulfide bond wrapped by the side chains of Val39, Leu98, Pro40 and His42. This probably explains why the Cys4–Cys89 bond is more susceptible to chemical reduction than the Cys43–Cys138 disulfide bond (Lu et al., J. Biol. Chem. 271, 11309–1131 (1996)).

The SCF dimer interface is composed of loops between alphaA and beta1, alphaB and alphaC, and can also be divided into three layers (see FIG. 21). The bottom layer at the side of the beta strands is composed of hydrophobic interactions. Side chains from Tyr26, Pro23, Phe63 and Leu22 from one protomer pack against corresponding side chains from the other protomer, with Tyr26-Asp25′ and Tyr26′-Asp25 forming a hydrogen bond circle as the carpet (see FIG. 2B). These intermolecular hydrogen bond pair replace the intermolecular disulfide bond between the two M-CSF protomers (Bazan, Cell 65, 9–10 (1991); Broudy, Blood 90, 1345–1364 (1997)). Sequence alignment shows that this Tyr-Asp pair is preserved in flt3 ligand, the third member of this family of cytokines that also forms dimers by non-covalent interactions (Hannum et al., Nature 368, 643–648 (1994)). At the core of the interface, the side chains of four asparagine residues (Asn72 and Asn21 from both protomers) form hydrogen bonds among themselves as well as via a water molecule (see FIG. 21). This well coordinated water molecule forms hydrogen bonds with an average bond length of 2.7 Å with the two carbonyl oxygen atoms of the two symmetry related Asn21 residues. The top layer involves interactions between loop alphaB-alphaC of one protomer against that of the other protomer. In addition to a dozen hydrogen bonds formed between the two protomers, there are four possible salt bridges between Lys17-Glu68′, Lys24-Asp61′, and their symmetry related counterparts.

Example 5 Structure Determination Ternary FGF2-FGFR1-Heparin complex

The expression, purification and crystallization of FGF2-FGFR1 complexes were carried out as described previously (Plotnikov et al., Cell 98, 641–650 (1999)). Crystals of the native FGF2-FGFR1 complex were incubated in 10 μl of stabilizing solution (40% PEG 8000, 0.25M ammonium sulfate, 0.1M Tris-HCl (pH 8.5)) containing 1 mM decasaccharide for one week at 20° C. Data were collected on a flash-frozen crystal (in a dry nitrogen stream using mother liquor containing 10% glycerol as cryo-protectant) on a CCD detector at beamline X4A at the National Synchrotron Light Source, Brookhaven National Laboratory. Data were processed using DENZO and SCALEPACK (Otwinowski, “Oscillation data reduction program,” in Proceedings of the CCP4 Study Weekend, Sawyer et al., (eds). (SERC Daresbury Laboratory, Daresbury, United Kingdom) (1993)). Difference Fourier electron density maps were computated using the FGF2-FGFR1 structure (Plotnikov et al., 1999). Initial model for the oligosaccharide was taken from the crystal structure of FGF2 in complex with hexasaccharide (1BFC) (Faham et al., Science 271, 1116–1120 (1996)). The parameters for the oligosaccharide were generated using the HIC-Up server (Kleywegt et al., Acta Crystallogr. D54, 1119–1131 (1998)). Simulated annealing and positional/B-factor refinement were performed using CNS (Bruenger et al., Acta. Crystallogr. D 54, 905–921 (1998)). Model building into 2F_(o)-F_(c) and F_(o)-F_(c) electron density maps was performed with the program O (Jones et al., Acta Crystallogr. A 47, 110–119 (1991)). The average B-factor is 36.9 Å² for all atoms, 35.0 Å² for FGF2, 35.3 Å² for FGFR1, and 72.4 Å² for decasaccharide molecules.

Structure Determination

Since a heparin binding canyon is present in the FGF2-FGFR1 crystals, incubation of these crystals with decasaccharide facilitated obtaining a ternary FGF-FGFR-heparin complex. The crystal structure of the ternary FGF2-FGFR1-heparin complex was solved using the phases obtained from the FGF2-FGFR1 structure. Data collection and refinement statistics are given in Table 5. It was anticipated to find a single decasaccharide molecule (heparin) traversing the canyon and bridging the ligands. However, the difference Fourier electron density map clearly shows two decasaccharide molecules in the canyon (see FIGS. 27 and 28). Only the first 6 sugar rings (A to F) are observed to interact with protein. Consequently, the electron density is well defined for these rings. In addition, due to favorable lattice contacts, two additional sugars (rings G and H) could be modeled for one of the decasaccharides.

Atomic Structural Coordinates

Table 6 provides the atomic structural coordinates of the the ternary FGF2-FGFR1-heparin complex.

Heparin Structure

The heparin can be approximated as a helix generated by repeating disaccharide units of D-glucosamine (GlcN) and L-iduronic acid (IdoA) joined by α-1–4 linkages. Each disaccharide unit is sulfated at three positions; one at the 2-hydroxyl group of IdoA and two at the 2-amino and 6-hydroxyl groups of GlcN. Sulfate and carboxylate groups form the negatively-charged edges of the heparin helix and appear on a given side of the helix every 17–19 Å on average. These helical parameters are in agreement with the X-ray fiber diffraction values of 8.7 Å and 180° for a heparin polymer (Nieduszynski et al., Am. Chem. Soc. Symp. Ser. 48, 73 (1977)). Heparin polysaccharides are polar entities with a non-reducing end (O4) and a reducing end (O1). In the crystal structure, the decasaccharides bind with their non-reducing ends in the center of canyon and run out onto the high-affinity heparin binding sites of the ligands. Consequently, the symmetry of the dimeric assembly is maintained. Traversing of the canyon by one polar heparin molecule disrupts the two-fold symmetry of the system.

Several intramolecular hydrogen bonds stabilize the helical conformation of the decasaccharide (data not shown). The GlcN rings are all found in a chair conformation. The IdoA rings are in either a chair or a skewed boat conformation as previously observed in the solution structure of a dodecasaccharide (Mulloy et al., Biochem. J. 293, 849–858 (1993)), suggesting that IdoA can adopt multiple conformations depending on the contacts it makes with FGF or FGFR. It is likely that the conformational flexibility of IdoA plays a role in specific recognition of various FGFs or FGFRs.

Heparin-FGF and Heparin-FGFR Interactions

Each decasaccharide makes a total of 30 hydrogen bonds with FGF and both FGFRs (see FIGS. 29 and 30). Within one 1:1 FGF:FGFR complex, 25 hydrogen bonds are made with heparin. The remaining 5 hydrogen bonds with heparin originate from the FGFR of the adjoining 1:1 FGF:FGFR complex. Lysines 160,163, 172,175 and 177, located on the heparin-binding surface of D2, form 7 hydrogen bonds between FGFR and heparin in the context of a 1:1 FGF:FGFR complex. With the exception of a single hydrogen bond between Lys-175 and heparin, which is mediated by a ring oxygen of heparin (ring A), the remainder of these hydrogen bonds are sulfate-mediated. All three types of heparin sulfate groups (N-sulfate, 2-O-sulfate and 6-O-sulfate) are employed in these interactions (FIGS. 29 and 30).

At the FGF-heparin interface, a total of 18 hydrogen bonds are made, of which half are sulfate-mediated (FIGS. 29 and 30). The other half is mediated by carboxylate, linker or ring oxygens of heparin. Surface residues Asn-27 (located in the β1-β2 loop), Arg-120, and Thr-121 (located in the β9-β10 loop), Lys-125, Lys-129, Gln-134, Lys-135, and Ala-136 (located in β11-β12 loop) form the heparin-binding site on FGF. These residues are the same ones that interact with heparin in the FGF2-hexasaccharide structure (Faham et al., Science 271, 1116–1120 (1996)). However, since the orientation of the heparin helix with respect to FGF is flipped between these two structures, the hydrogen binding pairs are not identical.

Aside from a single hydrogen bond between Lys-135 of FGF2 and a 6-O-sulfate (ring B) of heparin, the remainder of the sulfate-mediated interactions involve N-sulfate and 2-O-sulfate groups. This provides an explanation for why FGF2 has been reported to retain binding ability to 6-O-desulfated heparin. Nevertheless, 6-O-desulfated heparin oligosaccharides are still ineffective in promoting FGF2-FGFR interaction. In the present crystal structure, the 6-O-sulfate of ring B (FIGS. 29 and 30) makes hydrogen bonds with heparin-binding residues of both FGF and FGFR. Concurrent binding of both FGF and FGFR to the same sulfate group of heparin clearly serves to increase the apparent affinity of FGF for FGFR. Hence, the present structure also provides a molecular basis for the well-documented heparin-dependent 1:1 FGF:FGFR interaction.

In addition to promoting FGF-FGFR interaction within the 1:1 FGF:FGFR complex, heparin also interacts with the adjoining receptor across the two-fold dimer. A total of 5 hydrogen bonds are made at this interface between FGFR residues Lys-207 and Arg-209 and sugar rings A–D of heparin (FIGS. 29 and 30). Hydrophobic contacts between Ile-216 and the non-reduced ring A of heparin further fortify this interface. The hydrogen bonds between Lys-207 and heparin are mediated via carboxylate, linker and ring oxygens of heparin. In contrast, Arg-209 makes hydrogen bonds with the 6-O-sulfate group of ring D, thereby emphasizing the critical dual role of 6-O-sulfate in promoting 1:1 FGF2:FGFR interaction and inducing 2:2 FGF:FGFR dimer formation. The crystal structure provides a plausible explanation for the well-documented inability of 6-O-desulfated heparin oligosaccharides to promote mitogenic activities by failing to induce receptor dimerization.

TABLE 5 Summary of Crystallographic Analysis Data Collection Statistics Reflections Completeness R_(sym) ^(a) Signal (<l/ Resolution (Å) (total/unique) (%) (%) δl>) 30.0–3.0 97669/19774 97.2 (92.6)^(b) 7.0 (30.3)^(b) 12.3 Refinement Statistics^(c) Root-mean-square Deviations Resolu- R_(cryst)/ Bonds Angles B-factors^(e) tion (Å) Reflections R_(free) ^(d) (%) Bonds (Å) (°) (Å²) 25.0–3.0 18305 23.1/28.9 0.011 1.6 1.28 ^(a)R_(sym) = 100 × Σ_(hkl)Σ_(i)|l_(i)(hkl) − <l(hkl)>|/Σ_(hkl)Σ_(i)l_(i)(hkl). ^(b)Value in parentheses is for the highest resolution shell: 3.11–3.00 Å. ^(c)Atomic model: 5245 protein atoms and 245 decasaccharide atoms. ^(d)R_(cryst/free) = 100 × Σ_(hkl)||F_(o)(hkl)| − |F_(c)(hkl)||/Σ_(hkl)|F_(o)(hkl)|, where F_(o) (>2δ) and F_(c) are the observed and calculated structure factors, respectively. 5% of the reflections were used for calculation of R_(free). ^(e)For bonded atoms.

The invention illustratively described herein may be practiced in the absence of any element or elements, limitation or limitations which is not specifically disclosed herein. The terms and expressions which have been employed are used as terms of description and not of limitation, and there is no intention that in the use of such terms and expressions of excluding any equivalents of the features shown and described or portions thereof, but it is recognized that various modifications are possible within the scope of the invention claimed. Thus, it should be understood that although the present invention has been specifically disclosed by preferred embodiments and optional features, modification and variation of the concepts herein disclosed may be resorted to by those skilled in the art, and that such modifications and variations are considered to be within the scope of this invention as defined by the appended claims.

The contents of the articles, patents, and patent applications, and all other documents and electronically available information mentioned or cited herein, are hereby incorporated by reference in their entirety to the same extent as if each individual publication was specifically and individually indicated to be incorporated by reference. Applicants reserve the right to physically incorporate into this application any and all materials and information from any such articles, patents, patent applications, or other documents.

The terms and expressions employed herein have been used as terms of description and not of limitation, and there is no intention in the use of such terms and expressions of excluding any equivalents of the features shown and described or portions thereof, but it is recognized that various modifications are possible within the scope of the invention claimed. Thus, it should be understood that although the present invention has been specifically disclosed by preferred embodiments and optional features, modification and variation of the inventions embodied therein herein disclosed may be resorted to by those skilled in the art, and that such modifications and variations are considered to be within the scope of this invention.

The structure of the FGFR1(D2-D3)/FGF2 complex has been described in Plotnikov et al., Cell 98, 641–650 (1999). The structures of the FGFR1(D2-D3)/FGF1 complex and the FGFR2/FGF2 complex are described in Plotnikov et al., Cell 101, 413424 (2000). The structure of the human stem cell factor homodimer is described in Zhang et al., Proc. Nat. Acad. Sci. 97(14), 7732–7737 (2000). The disclosures of these three references are herein incorporated by reference.

The following bibliography includes general references relating to RPTKs as well as citations relating more specifically to the structure of the FGF-FGFR-heparin ternary complexes described herein.

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Structural requirements in heparin for binding     and activation of FGF-1 and FGF4 are different from that for FGF-2.     Glycobiology 4, 817–824. -   Jaye, M., (1992). Fibroblast growth factor receptor tyrosine     kinases: molecular analysis and signal transduction. Biochim.     Biophys. Acta 1135, 185–199. -   Johnson, D. E., and Williams, L. T. (1993). Structural and     functional diversity in the FGF receptor multigene family. Adv.     Cancer Res. 60, 1–41. -   Jones, T. A. (1991). Improved methods for binding protein models in     electron density maps and the location of errors in these models.     Acta Crystallogr,. A 47, 110–119. -   Kleywegt, (1998). Databases in protein crystallography. Acta     Crystallogr. D54, 1119–1131. -   Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed     and schematic plots of protein structures. J. Appl. Crystallogr. 24,     946–950. -   Merrit, E. A. and Bacon, D. J. (1997). Raster3D: photorealistic     molecular graphics. Meth. Enzymol. 277, 505–524. -   Mulloy, B, Forster, M. J., Jones, C., and Davies, D. B. (1993).     N.M.R. and molecular-modelling studies of the solution conformation     of heparin. Biochem. J. 293, 849–858. -   Naski, M. C. (1998). FGF signaling in skeletal development. Front     Biosci. 3, D781–794. -   Nicholls, A., Sharp, K. A., and Honig, B. (1991). Protein folding     and association: insights from interfacial and thermodynamic     properties of hydrocarbons. Proteins 11, 281–296. -   Nieduszynski, (1977). Am. Chem. Soc. Symp. Ser. 48,73. -   Nishimura, T., Nakatake, Y., Konishi, M., and Itoh, N. (2000).     Identification of a novel FGF, FGF-21, preferentially expressed in     the liver. Biochim. Biophys. Acta, 1492, 203–206. -   Ornitz, D. M., Xu, J., Colvin, J. S., McEwen, D. G., MacArthur, C.     A., Coulier, F., Gao, G., and Goldfarb, M. (1996). Receptor     specificity of the fibroblast growth factor family. J. Biol. Chem.     271, 15292–15297. -   Ornitz, D. M., Yayon, A., Flanagan, J. G., Svahn, C. M., Levi, E.,     and Leder, P. (1992). Heparin is required for cell-free binding of     bFGF to a soluble receptor and for mitogenesis in whole cells. Mol.     Cell. Biol. 12,240–247. -   Ornitz, D. M., Herr, A. B., Nilsson, M., Westman, J., Svahn, C. M.,     and Waksman, G. (1995). FGF binding and FGF receptor activation by     synthetic heparan-derived di- and trisaccharides. Science 268,     432–436 -   Otwinowski, Z. (1993). Oscillation data reduction program. In     Proceedings of the CCP4 Study Weekend. (SERC Daresbury Laboratory,     Daresbury, United Kingdom). -   Plotnikov, A. N., Schlessinger, J., Hubbard, S. R., and     Mohammadi, M. (1999). Structural basis for FGF receptor dimerization     and activation. Cell 98, 641–650. -   Plotnikov, A. N., Hubbard, S. R., Schlessinger, J., and     Mohammadi, M. (2000). Structural basis for FGF receptor dimerization     and activation. Cell 101, 413–424. -   Pye, D. A., Vives, R. R., Turnbull, J. E., Hyde, P., and     Gallagher, J. T. (1998). Heparan sulfate oligosaccharides require     6-O-sulfation for promotion of basic fibroblast growth factor     mitogenic activity. J. Biol. Chem. 273, 22936–22942. -   Rapraeger, A. C., Krufka, A., and Olwin, B. B. (1991). Requirement     of heparan sulfate for bFGF-mediated fibroblast growth and myoblast     differentiation. Science 252, 1708–1708. -   Rusnati, M., Coltrini, D., Caccia, P., Dell'Era, P., Zoppetti, G.,     Oreste, P., Valsasina, B., and -   Presta, M. (1994). Distinct role of 2-O—, N—, and 6-O-sulfate groups     of heparin in the formation of the ternary complex with basic     fibroblast growth factor and soluble FGF receptor-1. Biochem.     Biophys. Res. Commun. 203,450–458. -   Stauber, et al. (2000). Proc. Natl. Acad. Sci. USA 97, 49–54. -   Venkataraman, G (1999). Proc. Natl. Acad. Sci. USA 96, 3658–3663. -   Yayon,. (1991). Cell 64, 841–848. -   Spivak-Kroizman. (1994). Heparin-induced oligomerization of FGF     molecules is responsible for FGF receptor dimerization, activation,     and cell proliferation. Cell 79, 1015–1024. -   Zhou, F. Y. et al. Eur. J. Cell Biol. 73, 71–80.

TABLE 1 FGFR1 D2–D3 Complexed with FGF2 ATOM 1 CB HIS A 16 69.016 29.963 137.171 1.00 41.99 ATOM 2 CG HIS A 16 67.950 29.424 138.074 1.00 44.70 ATOM 3 CD2 HIS A 16 67.435 29.899 139.233 1.00 44.60 ATOM 4 ND1 HIS A 16 67.286 28.242 137.817 1.00 45.58 ATOM 5 CE1 HIS A 16 66.412 28.011 138.781 1.00 45.34 ATOM 6 NE2 HIS A 16 66.481 29.002 139.652 1.00 45.97 ATOM 7 C HIS A 16 68.950 28.141 135.513 1.00 42.15 ATOM 8 O HIS A 16 68.419 28.749 134.583 1.00 44.62 ATOM 9 N HIS A 16 71.039 29.455 135.830 1.00 40.32 ATOM 10 CA HIS A 16 69.840 28.875 136.502 1.00 41.81 ATOM 11 N PHE A 17 68.761 26.844 135.742 1.00 41.35 ATOM 12 CA PHE A 17 67.965 25.985 134.864 1.00 40.26 ATOM 13 CB PHE A 17 68.024 24.543 135.383 1.00 37.06 ATOM 14 CG PHE A 17 67.253 24.321 136.661 1.00 36.58 ATOM 15 CD1 PHE A 17 65.951 23.823 136.632 1.00 35.88 ATOM 16 CD2 PHE A 17 67.796 24.674 137.891 1.00 35.10 ATOM 17 CE1 PHE A 17 65.210 23.686 137.809 1.00 32.72 ATOM 18 CE2 PHE A 17 67.052 24.539 139.064 1.00 31.85 ATOM 19 CZ PHE A 17 65.761 24.047 139.018 1.00 30.46 ATOM 20 C PHE A 17 66.501 26.413 134.643 1.00 41.70 ATOM 21 O PHE A 17 65.914 26.068 133.623 1.00 42.96 ATOM 22 N LYS A 18 65.942 27.163 135.587 1.00 42.87 ATOM 23 CA LYS A 18 64.556 27.622 135.488 1.00 42.89 ATOM 24 CB LYS A 18 64.083 28.161 136.843 1.00 40.05 ATOM 25 C LYS A 18 64.348 28.702 134.420 1.00 43.25 ATOM 26 O LYS A 18 63.273 28.783 133.818 1.00 43.36 ATOM 27 N ASP A 19 65.377 29.522 134.190 1.00 42.81 ATOM 28 CA ASP A 19 65.312 30.618 133.216 1.00 40.93 ATOM 29 CB ASP A 19 66.335 31.686 133.579 1.00 41.73 ATOM 30 CG ASP A 19 66.025 32.348 134.896 1.00 43.73 ATOM 31 OD1 ASP A 19 65.882 31.624 135.903 1.00 46.50 ATOM 32 OD2 ASP A 19 65.919 33.591 134.931 1.00 43.92 ATOM 33 C ASP A 19 65.520 30.193 131.765 1.00 38.86 ATOM 34 O ASP A 19 66.038 29.108 131.492 1.00 38.38 ATOM 35 N PRO A 20 65.097 31.044 130.809 1.00 36.59 ATOM 36 CD PRO A 20 64.245 32.233 130.938 1.00 36.39 ATOM 37 CA PRO A 20 65.263 30.712 129.396 1.00 34.39 ATOM 38 CB PRO A 20 64.474 31.799 128.673 1.00 31.04 ATOM 39 CG PRO A 20 63.467 32.189 129.638 1.00 33.58 ATOM 40 C PRO A 20 66.726 30.773 129.038 1.00 34.58 ATOM 41 O PRO A 20 67.507 31.506 129.657 1.00 35.62 ATOM 42 N LYS A 21 67.089 30.000 128.027 1.00 32.92 ATOM 43 CA LYS A 21 68.449 29.959 127.556 1.00 32.11 ATOM 44 CB LYS A 21 69.042 28.572 127.773 1.00 31.65 ATOM 45 CG LYS A 21 69.408 28.268 129.214 1.00 33.27 ATOM 46 CD LYS A 21 70.054 26.901 129.323 1.00 32.63 ATOM 47 CE LYS A 21 70.056 26.396 130.757 1.00 34.58 ATOM 48 NZ LYS A 21 70.472 24.961 130.814 1.00 35.96 ATOM 49 C LYS A 21 68.481 30.296 126.078 1.00 32.97 ATOM 50 O LYS A 21 67.484 30.154 125.377 1.00 32.04 ATOM 51 N ARG A 22 69.626 30.779 125.613 1.00 33.48 ATOM 52 CA ARG A 22 69.784 31.097 124.209 1.00 32.66 ATOM 53 CB ARG A 22 70.360 32.501 124.032 1.00 32.91 ATOM 54 CG ARG A 22 69.297 33.575 123.837 1.00 34.86 ATOM 55 CD ARG A 22 69.895 34.819 123.216 1.00 36.56 ATOM 56 NE ARG A 22 70.410 35.730 124.227 1.00 41.57 ATOM 57 CZ ARG A 22 69.640 36.525 124.961 1.00 44.42 ATOM 58 NH1 ARG A 22 68.326 36.510 124.781 1.00 47.29 ATOM 59 NH2 ARG A 22 70.174 37.330 125.873 1.00 46.76 ATOM 60 C ARG A 22 70.743 30.050 123.680 1.00 31.65 ATOM 61 O ARG A 22 71.782 29.812 124.285 1.00 32.89 ATOM 62 N LEU A 23 70.392 29.389 122.585 1.00 29.77 ATOM 63 CA LEU A 23 71.296 28.386 122.050 1.00 28.94 ATOM 64 CB LEU A 23 70.528 27.131 121.626 1.00 26.35 ATOM 65 CG LEU A 23 69.825 26.375 122.758 1.00 24.87 ATOM 66 CD1 LEU A 23 69.641 24.951 122.332 1.00 21.75 ATOM 67 CD2 LEU A 23 70.656 26.393 124.034 1.00 26.45 ATOM 68 C LEU A 23 72.160 28.911 120.897 1.00 30.13 ATOM 69 O LEU A 23 71.690 29.114 119.774 1.00 29.81 ATOM 70 N TYR A 24 73.436 29.136 121.199 1.00 29.52 ATOM 71 CA TYR A 24 74.399 29.633 120.224 1.00 27.79 ATOM 72 CB TYR A 24 75.404 30.516 120.962 1.00 25.04 ATOM 73 CG TYR A 24 76.606 30.962 120.168 1.00 27.06 ATOM 74 CD1 TYR A 24 77.653 30.079 119.899 1.00 26.87 ATOM 75 CE1 TYR A 24 78.785 30.489 119.219 1.00 24.47 ATOM 76 CD2 TYR A 24 76.727 32.283 119.722 1.00 26.32 ATOM 77 CE2 TYR A 24 77.865 32.705 119.039 1.00 24.37 ATOM 78 CZ TYR A 24 78.888 31.796 118.795 1.00 23.72 ATOM 79 OH TYR A 24 80.023 32.183 118.134 1.00 22.17 ATOM 80 C TYR A 24 75.077 28.448 119.509 1.00 28.20 ATOM 81 O TYR A 24 75.748 27.635 120.132 1.00 27.40 ATOM 82 N CYS A 25 74.887 28.342 118.199 1.00 29.93 ATOM 83 CA CYS A 25 75.471 27.239 117.437 1.00 30.80 ATOM 84 CB CYS A 25 74.690 27.015 116.141 1.00 29.39 ATOM 85 SG CYS A 25 75.266 25.611 115.174 1.00 27.95 ATOM 86 C CYS A 25 76.926 27.506 117.111 1.00 32.90 ATOM 87 O CYS A 25 77.279 28.585 116.633 1.00 35.05 ATOM 88 N LYS A 26 77.774 26.519 117.370 1.00 34.20 ATOM 89 CA LYS A 26 79.205 26.646 117.103 1.00 33.90 ATOM 90 CB LYS A 26 79.917 25.362 117.540 1.00 33.25 ATOM 91 CG LYS A 26 81.420 25.379 117.382 1.00 33.15 ATOM 92 CD LYS A 26 82.028 24.156 118.038 1.00 33.12 ATOM 93 CE LYS A 26 83.540 24.186 117.966 1.00 33.97 ATOM 94 NZ LYS A 26 84.056 23.910 116.590 1.00 38.44 ATOM 95 C LYS A 26 79.466 26.903 115.621 1.00 34.79 ATOM 96 O LYS A 26 80.472 27.520 115.253 1.00 35.31 ATOM 97 N ASN A 27 78.548 26.439 114.775 1.00 34.52 ATOM 98 CA ASN A 27 78.696 26.588 113.340 1.00 33.29 ATOM 99 CB ASN A 27 78.043 25.408 112.637 1.00 35.53 ATOM 100 CG ASN A 27 78.423 25.320 111.176 1.00 37.03 ATOM 101 OD1 ASN A 27 79.601 25.349 110.829 1.00 39.05 ATOM 102 ND2 ASN A 27 77.427 25.200 110.311 1.00 38.14 ATOM 103 C ASN A 27 78.129 27.886 112.794 1.00 33.64 ATOM 104 O ASN A 27 77.013 27.917 112.271 1.00 32.60 ATOM 105 N GLY A 28 78.909 28.958 112.922 1.00 33.42 ATOM 106 CA GLY A 28 78.489 30.247 112.408 1.00 32.48 ATOM 107 C GLY A 28 78.101 31.273 113.447 1.00 31.65 ATOM 108 O GLY A 28 77.968 32.458 113.146 1.00 30.93 ATOM 109 N GLY A 29 77.904 30.821 114.673 1.00 30.89 ATOM 110 CA GLY A 29 77.527 31.745 115.716 1.00 32.62 ATOM 111 C GLY A 29 76.065 32.109 115.616 1.00 33.06 ATOM 112 O GLY A 29 75.639 33.179 116.061 1.00 33.90 ATOM 113 N PHE A 30 75.293 31.214 115.013 1.00 33.36 ATOM 114 CA PHE A 30 73.863 31.425 114.869 1.00 33.15 ATOM 115 CB PHE A 30 73.339 30.732 113.604 1.00 32.93 ATOM 116 CG PHE A 30 73.802 31.366 112.320 1.00 34.10 ATOM 117 CD1 PHE A 30 74.945 30.912 111.674 1.00 33.99 ATOM 118 CD2 PHE A 30 73.101 32.438 111.763 1.00 33.52 ATOM 119 CE1 PHE A 30 75.381 31.511 110.494 1.00 32.91 ATOM 120 CE2 PHE A 30 73.533 33.042 110.585 1.00 31.25 ATOM 121 CZ PHE A 30 74.674 32.578 109.951 1.00 31.88 ATOM 122 C PHE A 30 73.091 30.900 116.083 1.00 32.68 ATOM 123 O PHE A 30 73.306 29.778 116.531 1.00 31.40 ATOM 124 N PHE A 31 72.206 31.737 116.611 1.00 33.00 ATOM 125 CA PHE A 31 71.341 31.386 117.732 1.00 34.02 ATOM 126 CB PHE A 31 70.856 32.643 118.445 1.00 34.25 ATOM 127 CG PHE A 31 71.883 33.283 119.306 1.00 35.90 ATOM 128 CD1 PHE A 31 72.290 32.670 120.488 1.00 36.24 ATOM 129 CD2 PHE A 31 72.438 34.503 118.952 1.00 34.85 ATOM 13O CE1 PHE A 31 73.237 33.266 121.306 1.00 35.63 ATOM 131 CE2 PHE A 31 73.385 35.105 119.763 1.00 35.21 ATOM 132 CZ PHE A 31 73.786 34.484 120.946 1.00 35.42 ATOM 133 C PHE A 31 70.110 30.681 117.163 1.00 33.76 ATOM 134 O PHE A 31 69.507 31.172 116.216 1.00 34.00 ATOM 135 N LEU A 32 69.727 29.544 117.735 1.00 33.72 ATOM 136 CA LEU A 32 68.546 28.843 117.246 1.00 32.35 ATOM 137 CB LEU A 32 68.324 27.520 117.978 1.00 33.20 ATOM 138 CG LEU A 32 67.212 26.674 117.337 1.00 35.02 ATOM 139 CD1 LEU A 32 67.743 26.012 116.074 1.00 34.56 ATOM 140 CD2 LEU A 32 66.724 25.611 118.301 1.00 34.97 ATOM 141 C LEU A 32 67.333 29.739 117.448 1.00 30.84 ATOM 142 O LEU A 32 67.113 30.288 118.533 1.00 31.20 ATOM 143 N ARG A 33 66.550 29.887 116.390 1.00 29.27 ATOM 144 CA ARG A 33 65.374 30.734 116.445 1.00 30.54 ATOM 145 CB ARG A 33 65.548 31.920 115.508 1.00 28.32 ATOM 146 CG ARG A 33 64.365 32.834 115.547 1.00 26.41 ATOM 147 CD ARG A 33 64.640 34.102 114.822 1.00 23.29 ATOM 148 NE ARG A 33 65.039 33.869 113.445 1.00 18.71 ATOM 149 CZ ARG A 33 65.222 34.854 112.574 1.00 18.55 ATOM 150 NH1 ARG A 33 65.037 36.113 112.957 1.00 13.11 ATOM 151 NH2 ARG A 33 65.602 34.585 111.334 1.00 18.20 ATOM 152 C ARG A 33 64.062 30.030 116.100 1.00 32.27 ATOM 153 O ARG A 33 63.993 29.229 115.149 1.00 33.66 ATOM 154 N ILE A 34 63.022 30.330 116.876 1.00 30.42 ATOM 155 CA ILE A 34 61.718 29.750 116.625 1.00 29.36 ATOM 156 CB ILE A 34 61.230 28.904 117.788 1.00 27.41 ATOM 157 CG2 ILE A 34 59.744 28.626 117.631 1.00 25.89 ATOM 158 CG1 ILE A 34 62.001 27.587 117.822 1.00 26.27 ATOM 159 CD1 ILE A 34 61.727 26.757 119.052 1.00 25.37 ATOM 160 C ILE A 34 60.710 30.847 116.370 1.00 30.63 ATOM 161 O ILE A 34 60.280 31.534 117.293 1.00 30.14 ATOM 162 N HIS A 35 60.350 31.001 115.099 1.00 31.46 ATOM 163 CA HIS A 35 59.383 32.002 114.665 1.00 33.03 ATOM 164 CB HIS A 35 59.334 32.064 113.136 1.00 32.91 ATOM 165 CG HIS A 35 60.620 32.472 112.498 1.00 32.44 ATOM 166 CD2 HIS A 35 61.634 31.734 111.985 1.00 33.64 ATOM 167 ND1 HIS A 35 60.975 33.790 112.321 1.00 32.36 ATOM 168 CE1 HIS A 35 62.151 33.849 111.722 1.00 33.74 ATOM 169 NE2 HIS A 35 62.573 32.615 111.506 1.00 33.60 ATOM 170 C HIS A 35 57.981 31.667 115.155 1.00 32.67 ATOM 171 O HIS A 35 57.588 30.500 115.213 1.00 32.12 ATOM 172 N PRO A 36 57.205 32.691 115.508 1.00 33.10 ATOM 173 CD PRO A 36 57.659 34.079 115.691 1.00 32.12 ATOM 174 CA PRO A 36 55.829 32.511 115.988 1.00 34.09 ATOM 175 CB PRO A 36 55.339 33.942 116.136 1.00 32.69 ATOM 176 CG PRO A 36 56.588 34.657 116.587 1.00 33.71 ATOM 177 C PRO A 36 54.968 31.705 115.009 1.00 34.10 ATOM 178 O PRO A 36 53.993 31.080 115.393 1.00 34.65 ATOM 179 N ASP A 37 55.347 31.720 113.742 1.00 34.54 ATOM 180 CA ASP A 37 54.610 31.009 112.719 1.00 34.85 ATOM 181 CB ASP A 37 54.831 31.717 111.378 1.00 35.76 ATOM 182 CG ASP A 37 56.219 31.444 110.778 1.00 39.05 ATOM 183 OD1 ASP A 37 57.142 30.974 111.495 1.00 37.89 ATOM 184 OD2 ASP A 37 56.387 31.709 109.566 1.00 41.38 ATOM 185 C ASP A 37 55.021 29.532 112.623 1.00 35.51 ATOM 186 O ASP A 37 54.530 28.801 111.755 1.00 35.50 ATOM 187 N GLY A 38 55.927 29.098 113.500 1.00 34.87 ATOM 188 CA GLY A 38 56.371 27.715 113.471 1.00 32.57 ATOM 189 C GLY A 38 57.635 27.428 112.676 1.00 32.56 ATOM 190 O GLY A 38 58.130 26.300 112.696 1.00 31.39 ATOM 191 N ARG A 39 58.170 28.421 111.974 1.00 32.64 ATOM 192 CA ARG A 39 59.387 28.197 111.200 1.00 34.59 ATOM 193 CB ARG A 39 59.576 29.307 110.170 1.00 35.46 ATOM 194 CG ARG A 39 58.676 29.184 108.946 1.00 37.20 ATOM 195 CD ARG A 39 58.918 30.321 107.970 1.00 37.24 ATOM 196 NE ARG A 39 58.727 31.623 108.606 1.00 36.10 ATOM 197 CZ ARG A 39 59.006 32.785 108.025 1.00 36.28 ATOM 198 NH1 ARG A 39 58.800 33.917 108.681 1.00 38.00 ATOM 199 NH2 ARG A 39 59.493 32.816 106.791 1.00 35.62 ATOM 200 C ARG A 39 60.585 28.157 112.135 1.00 35.64 ATOM 201 O ARG A 39 60.576 28.812 113.177 1.00 37.00 ATOM 202 N VAL A 40 61.610 27.390 111.763 1.00 35.00 ATOM 203 CA VAL A 40 62.829 27.257 112.565 1.00 33.88 ATOM 204 CB VAL A 40 62.989 25.787 113.115 1.00 33.74 ATOM 205 CG1 VAL A 40 64.364 25.590 113.742 1.00 31.93 ATOM 206 CG2 VAL A 40 61.918 25.487 114.146 1.00 30.42 ATOM 207 C VAL A 40 64.070 27.611 111.735 1.00 34.33 ATOM 208 O VAL A 40 64.236 27.126 110.617 1.00 33.67 ATOM 209 N ASP A 41 64.939 28.457 112.285 1.00 34.88 ATOM 210 CA ASP A 41 66.172 28.851 111.603 1.00 33.77 ATOM 211 CE ASP A 41 65.871 29.850 110.483 1.00 33.17 ATOM 212 CG ASP A 41 65.184 31.111 110.984 1.00 34.75 ATOM 213 OD1 ASP A 41 65.026 32.052 110.177 1.00 34.83 ATOM 214 OD2 ASP A 41 64.794 31.167 112.173 1.00 36.12 ATOM 215 C ASP A 41 67.148 29.462 112.600 1.00 33.16 ATOM 216 O ASP A 41 66.972 29.327 113.809 1.00 32.95 ATOM 217 N GLY A 42 68.170 30.144 112.093 1.00 32.65 ATOM 218 CA GLY A 42 69.154 30.761 112.966 1.00 32.74 ATOM 219 C GLY A 42 69.387 32.246 112.721 1.00 33.27 ATOM 220 O GLY A 42 69.042 32.781 111.663 1.00 34.04 ATOM 221 N VAL A 43 69.979 32.913 113.707 1.00 31.48 ATOM 222 CA VAL A 43 70.277 34.334 113.626 1.00 31.31 ATOM 223 CB VAL A 43 69.081 35.211 114.037 1.00 31.65 ATOM 224 CG1 VAL A 43 68.090 35.255 112.932 1.00 32.00 ATOM 225 CG2 VAL A 43 68.446 34.680 115.327 1.00 29.54 ATOM 226 C VAL A 43 71.391 34.689 114.578 1.00 31.62 ATOM 227 O VAL A 43 71.384 34.269 115.725 1.00 32.45 ATOM 228 N ARG A 44 72.330 35.501 114.120 1.00 32.59 ATOM 229 CA ARG A 44 73.430 35.900 114.978 1.00 32.23 ATOM 230 CB ARG A 44 74.634 36.305 114.133 1.00 30.10 ATOM 231 CG ARG A 44 75.173 35.165 113.321 1.00 28.38 ATOM 232 CD ARG A 44 76.442 35.549 112.600 1.00 29.66 ATOM 233 NE ARG A 44 76.916 34.448 111.762 1.00 32.18 ATOM 234 CZ ARG A 44 77.421 34.607 110.543 1.00 30.72 ATOM 235 NH1 ARG A 44 77.521 35.821 110.020 1.00 31.62 ATOM 236 NH2 ARG A 44 77.809 33.556 109.842 1.00 29.64 ATOM 237 C ARG A 44 73.047 37.025 115.928 1.00 32.13 ATOM 238 O ARG A 44 73.689 37.207 116.960 1.00 31.61 ATOM 239 N GLU A 45 71.990 37.762 115.598 1.00 32.69 ATOM 240 CA GLU A 45 71.573 38.873 116.445 1.00 34.53 ATOM 241 CB GLU A 45 70.578 39.769 115.694 1.00 36.59 ATOM 242 CG GLU A 45 70.223 41.025 116.479 1.00 41.80 ATOM 243 CD GLU A 45 71.440 41.594 117.213 1.00 44.59 ATOM 244 OE1 GLU A 45 72.466 41.834 116.522 1.00 46.33 ATOM 245 OE2 GLU A 45 71.371 41.786 118.460 1.00 41.23 ATOM 246 CG GLU A 45 71.00 338.474 117.814 1.00 32.72 ATOM 247 O GLU A 45 69.852 38.092 117.935 1.00 33.26 ATOM 248 N LYS A 46 71.829 38.604 118.842 1.00 31.74 ATOM 249 CA LYS A 46 71.461 38.254 120.193 1.00 31.44 ATOM 250 CB LYS A 46 72.650 38.548 121.111 1.00 33.55 ATOM 251 CG LYS A 46 72.550 37.959 122.516 1.00 37.58 ATOM 252 CD LYS A 46 73.931 37.596 123.067 1.00 37.72 ATOM 253 CE LYS A 46 73.862 37.059 124.488 1.00 36.84 ATOM 254 NZ LYS A 46 73.418 38.106 125.450 1.00 39.04 ATOM 255 C LYS A 46 70.200 38.959 120.691 1.00 32.17 ATOM 256 O LYS A 46 69.531 38.468 121.609 1.00 33.32 ATOM 257 N SER A 47 69.848 40.096 120.095 1.00 31.91 ATOM 258 CA SER A 47 68.649 40.804 120.550 1.00 30.89 ATOM 259 CB SER A 47 68.814 42.333 120.404 1.00 29.98 ATOM 260 OG SER A 47 68.697 42.795 119.066 1.00 28.59 ATOM 261 C SER A 47 67.374 40.335 119.853 1.00 29.76 ATOM 262 O SER A 47 66.293 40.863 120.108 1.00 28.86 ATOM 263 N ASP A 48 67.504 39.338 118.978 1.00 29.77 ATOM 264 CA ASP A 48 66.350 38.781 118.262 1.00 30.47 ATOM 265 CB ASP A 48 66.751 37.543 117.459 1.00 28.93 ATOM 266 CG ASP A 48 65.691 37.127 116.459 1.00 30.60 ATOM 267 OD1 ASP A 48 65.627 37.727 115.366 1.00 32.23 ATOM 268 OD2 ASP A 48 64.913 36.202 116.759 1.00 30.50 ATOM 269 C ASP A 48 65.287 38.383 119.277 1.00 31.67 ATOM 270 O ASP A 48 65.582 37.714 120.279 1.00 33.65 ATOM 271 N PRO A 49 64.032 38.779 119.028 1.00 30.74 ATOM 272 CD PRO A 49 63.576 39.618 117.907 1.00 28.94 ATOM 273 CA PRO A 49 62.923 38.467 119.933 1.00 30.97 ATOM 274 CB PRO A 49 61.787 39.340 119.387 1.00 28.99 ATOM 275 CG PRO A 49 62.086 39.416 117.952 1.00 28.31 ATOM 276 C PRO A 49 62.530 36.990 120.069 1.00 30.63 ATOM 277 O PRO A 49 62.015 36.565 121.106 1.00 30.71 ATOM 278 N HIS A 50 62.815 36.208 119.043 1.00 30.61 ATOM 279 CA HIS A 50 62.433 34.811 119.044 1.00 31.64 ATOM 280 CB HIS A 50 61.790 34.502 117.704 1.00 32.65 ATOM 281 CG HIS A 50 60.935 35.616 117.201 1.00 35.28 ATOM 282 CD2 HIS A 50 61.070 36.428 116.126 1.00 34.75 ATOM 283 ND1 HIS A 50 59.822 36.060 117.883 1.00 36.16 ATOM 284 CE1 HIS A 50 59.311 37.101 117.251 1.00 36.04 ATOM 285 NE2 HIS A 50 60.050 37.345 116.182 1.00 35.40 ATOM 286 C HIS A 50 63.527 33.800 119.330 1.00 32.15 ATOM 287 O HIS A 50 63.411 32.636 118.922 1.00 33.26 ATOM 288 N ILE A 51 64.593 34.209 120.008 1.00 30.57 ATOM 289 CA ILE A 51 65.611 33.217 120.283 1.00 30.02 ATOM 290 CB ILE A 51 66.984 33.631 119.775 1.00 26.66 ATOM 291 CG2 ILE A 51 67.006 33.469 118.276 1.00 22.82 ATOM 292 CG1 ILE A 51 67.340 35.032 120.263 1.00 26.24 ATOM 293 CD1 ILE A 51 68.817 35.345 120.095 1.00 24.74 ATOM 294 C ILE A 51 65.698 32.758 121.729 1.00 31.15 ATOM 295 O ILE A 51 66.518 31.894 122.050 1.00 33.30 ATOM 296 N LYS A 52 64.846 33.303 122.594 1.00 29.85 ATOM 297 CA LYS A 52 64.839 32.860 123.979 1.00 30.59 ATOM 298 CB LYS A 52 64.263 33.937 124.893 1.00 30.72 ATOM 299 CG LYS A 52 65.254 35.054 125.151 1.00 30.18 ATOM 300 CD LYS A 52 64.722 36.068 126.127 1.00 31.56 ATOM 301 CE LYS A 52 65.679 37.234 126.251 1.00 32.74 ATOM 302 NZ LYS A 52 65.133 38.319 127.108 1.00 35.64 ATOM 303 C LYS A 52 64.040 31.558 124.074 1.00 30.27 ATOM 304 O LYS A 52 62.833 31.522 123.817 1.00 30.12 ATOM 305 N LEU A 53 64.748 30.490 124.433 1.00 29.82 ATOM 306 CA LEU A 53 64.178 29.153 124.547 1.00 28.57 ATOM 307 CB LEU A 53 65.069 28.163 123.810 1.00 26.87 ATOM 308 CG LEU A 53 65.440 28.616 122.403 1.00 25.04 ATOM 309 CD1 LEU A 53 66.496 27.717 121.801 1.00 26.29 ATOM 310 CD2 LEU A 53 64.198 28.609 121.561 1.00 28.71 ATOM 311 C LEU A 53 64.026 28.696 125.987 1.00 28.76 ATOM 312 O LEU A 53 64.776 29.105 126.870 1.00 29.48 ATOM 313 N GLN A 54 63.028 27.856 126.221 1.00 30.22 ATOM 314 CA GLN A 54 62.786 27.314 127.558 1.00 29.52 ATOM 315 CB GLN A 54 61.370 27.617 128.041 1.00 28.20 ATOM 316 CG GLN A 54 61.152 27.291 129.505 1.00 30.47 ATOM 317 CD GLN A 54 61.887 28.243 130.440 1.00 30.27 ATOM 318 OE1 GLN A 54 61.775 29.461 130.312 1.00 31.93 ATOM 319 NE2 GLN A 54 62.627 27.690 131.392 1.00 29.64 ATOM 320 C GLN A 54 62.974 25.814 127.444 1.00 28.34 ATOM 321 O GLN A 54 62.132 25.106 126.884 1.00 28.87 ATOM 322 N LEU A 55 64.111 25.352 127.940 1.00 26.92 ATOM 323 CA LEU A 55 64.449 23.948 127.910 1.00 26.23 ATOM 324 CB LEU A 55 65.972 23.784 127.983 1.00 24.83 ATOM 325 CG LEU A 55 66.905 24.355 126.903 1.00 24.23 ATOM 326 CD1 LEU A 55 66.962 23.433 125.713 1.00 24.55 ATOM 327 CD2 LEU A 55 66.438 25.731 126.480 1.00 26.63 ATOM 328 C LEU A 55 63.796 23.322 129.136 1.00 27.06 ATOM 329 O LEU A 55 64.004 23.768 130.272 1.00 26.61 ATOM 330 N GLN A 56 62.984 22.304 128.898 1.00 27.30 ATOM 331 CA GLN A 56 62.312 21.606 129.981 1.00 28.34 ATOM 332 CB GLN A 56 60.798 21.788 129.867 1.00 26.66 ATOM 333 CG GLN A 56 60.030 21.033 130.907 1.00 23.34 ATOM 334 CD GLN A 56 60.538 21.321 132.299 1.00 28.68 ATOM 335 OE1 GLN A 56 60.418 22.451 132.802 1.00 29.89 ATOM 336 NE2 GLN A 56 61.115 20.302 132.941 1.00 26.31 ATOM 337 CG LN A 56 62.678 20.126 129.906 1.00 28.99 ATOM 338 O GLN A 56 62.699 19.535 128.825 1.00 29.17 ATOM 339 N ALA A 57 62.994 19.533 131.050 1.00 30.52 ATOM 340 CA ALA A 57 63.354 18.118 131.072 1.00 31.59 ATOM 341 CB ALA A 57 64.322 17.828 132.237 1.00 31.98 ATOM 342 C ALA A 57 62.085 17.299 131.228 1.00 30.88 ATOM 343 O ALA A 57 61.226 17.638 132.045 1.00 30.25 ATOM 344 N GLU A 58 61.956 16.241 130.436 1.00 31.07 ATOM 345 CA GLU A 58 60.786 15.385 130.543 1.00 34.30 ATOM 346 CB GLU A 58 60.338 14.907 129.160 1.00 35.65 ATOM 347 CG GLU A 58 58.793 14.838 128.986 1.00 36.64 ATOM 348 CD GLU A 58 58.041 16.071 129.527 1.00 36.53 ATOM 349 OE1 GLU A 58 58.538 17.214 129.363 1.00 38.32 ATOM 350 OE2 GLU A 58 56.941 15.894 130.104 1.00 33.99 ATOM 351 C GLU A 58 61.201 14.213 131.425 1.00 35.52 ATOM 352 O GLU A 58 60.381 13.576 132.082 1.00 35.87 ATOM 353 N GLU A 59 62.506 13.977 131.456 1.00 36.68 ATOM 354 CA GLU A 59 63.106 12.922 132.246 1.00 36.67 ATOM 355 CB GLU A 59 62.691 11.558 131.694 1.00 38.47 ATOM 356 CG GLU A 59 63.287 11.241 130.343 1.00 42.93 ATOM 357 CD GLU A 59 63.214 9.760 130.001 1.00 46.79 ATOM 358 OE1 GLU A 59 62.144 9.292 129.544 1.00 47.48 ATOM 359 OE2 GLU A 59 64.239 9.063 130.198 1.00 47.84 ATOM 360 C GLU A 59 64.619 13.108 132.116 1.00 35.99 ATOM 361 O GLU A 59 65.068 13.938 131.332 1.00 35.86 ATOM 362 N ARG A 60 65.402 12.338 132.866 1.00 35.25 ATOM 363 CA ARG A 60 66.855 12.454 132.801 1.00 34.39 ATOM 364 CB ARG A 60 67.536 11.325 133.589 1.00 35.43 ATOM 365 CG ARG A 60 67.711 11.638 135.064 1.00 38.14 ATOM 366 CD ARG A 60 68.487 10.568 135.787 1.00 40.57 ATOM 367 NE ARG A 60 69.811 10.376 135.207 1.00 44.90 ATOM 368 CZ ARG A 60 70.789 9.688 135.790 1.00 45.49 ATOM 369 NH1 ARG A 60 70.583 9.129 136.973 1.00 46.54 ATOM 370 NH2 ARG A 60 71.971 9.562 135.195 1.00 46.25 ATOM 371 C ARG A 60 67.392 12.459 131.380 1.00 32.51 ATOM 372 O ARG A 60 67.131 11.541 130.600 1.00 29.35 ATOM 373 N GLY A 61 68.132 13.516 131.058 1.00 30.50 ATOM 374 CA GLY A 61 68.734 13.635 129.744 1.00 30.56 ATOM 375 C GLY A 61 67.821 13.868 128.554 1.00 30.06 ATOM 376 O GLY A 61 68.264 13.731 127.406 1.00 30.72 ATOM 377 N VAL A 62 66.564 14.223 128.810 1.00 28.30 ATOM 378 CA VAL A 62 65.613 14.470 127.734 1.00 27.79 ATOM 379 CB VAL A 62 64.547 13.347 127.641 1.00 28.76 ATOM 380 CG1 VAL A 62 63.525 13.703 126.571 1.00 28.93 ATOM 381 CG2 VAL A 62 65.208 12.008 127.327 1.00 25.92 ATOM 382 C VAL A 62 64.897 15.799 127.937 1.00 28.19 ATOM 383 O VAL A 62 64.305 16.045 128.995 1.00 27.55 ATOM 384 N VAL A 63 64.941 16.651 126.915 1.00 27.67 ATOM 385 CA VAL A 63 64.292 17.952 127.006 1.00 27.32 ATOM 386 CB VAL A 63 65.318 19.109 127.120 1.00 26.53 ATOM 387 CG1 VAL A 63 66.211 18.918 128.330 1.00 25.20 ATOM 388 CG2 VAL A 63 66.127 19.201 125.840 1.00 23.28 ATOM 389 C VAL A 63 63.417 18.284 125.803 1.00 29.19 ATOM 390 O VAL A 63 63.595 17.740 124.698 1.00 30.04 ATOM 391 N SER A 64 62.469 19.184 126.043 1.00 27.23 ATOM 392 CA SER A 64 61.593 19.690 125.008 1.00 28.22 ATOM 393 CB SER A 64 60.119 19.691 125.449 1.00 30.07 ATOM 394 OG SER A 64 59.827 20.752 126.355 1.00 32.47 ATOM 395 C SER A 64 62.116 21.116 124.934 1.00 28.93 ATOM 396 O SER A 64 62.448 21.714 125.968 1.00 29.38 ATOM 397 N ILE A 65 62.221 21.650 123.722 1.00 28.04 ATOM 398 CA ILE A 65 62.718 22.999 123.529 1.00 27.05 ATOM 399 CB ILE A 65 63.789 23.005 122.422 1.00 26.59 ATOM 400 CG2 ILE A 65 64.172 24.434 122.035 1.00 24.34 ATOM 401 CG1 ILE A 65 64.998 22.213 122.910 1.00 24.17 ATOM 402 CD1 ILE A 65 65.874 21.698 121.799 1.00 26.19 ATOM 403 C ILE A 65 61.540 23.872 123.144 1.00 27.68 ATOM 404 O ILE A 65 60.977 23.715 122.066 1.00 28.09 ATOM 405 N LYS A 66 61.153 24.778 124.032 1.00 27.82 ATOM 406 CA LYS A 66 60.020 25.648 123.742 1.00 27.41 ATOM 407 CB LYS A 66 59.025 25.629 124.905 1.00 29.28 ATOM 408 CG LYS A 66 57.662 26.227 124.565 1.00 30.44 ATOM 409 CD LYS A 66 56.898 26.687 125.814 1.00 30.89 ATOM 410 CE LYS A 66 55.535 27.276 125.439 1.00 33.17 ATOM 411 NZ LYS A 66 54.860 28.001 126.561 1.00 34.75 ATOM 412 C LYS A 66 60.415 27.086 123.450 1.00 26.21 ATOM 413 O LYS A 66 61.122 27.723 124.234 1.00 25.68 ATOM 414 N GLY A 67 59.962 27.591 122.309 1.00 27.07 ATOM 415 CA GLY A 67 60.246 28.970 121.953 1.00 27.99 ATOM 416 C GLY A 67 59.338 29.858 122.792 1.00 26.28 ATOM 417 O GLY A 67 58.128 29.844 122.622 1.00 24.02 ATOM 418 N VAL A 68 59.918 30.622 123.706 1.00 26.60 ATOM 419 CA VAL A 68 59.129 31.475 124.574 1.00 27.61 ATOM 420 CB VAL A 68 60.010 32.232 125.527 1.00 25.66 ATOM 421 CG1 VAL A 68 59.169 33.214 126.326 1.00 22.69 ATOM 422 CG2 VAL A 68 60.733 31.253 126.420 1.00 24.49 ATOM 423 C VAL A 68 58.259 32.491 123.856 1.00 31.12 ATOM 424 O VAL A 68 57.100 32.682 124.210 1.00 32.65 ATOM 425 N SER A 69 58.821 33.164 122.861 1.00 34.30 ATOM 426 CA SER A 69 58.068 34.159 122.111 1.00 34.47 ATOM 427 CB SER A 69 59.011 34.932 121.190 1.00 33.89 ATOM 428 OG SER A 69 58.374 36.059 120.617 1.00 31.52 ATOM 429 C SER A 69 56.989 33.475 121.282 1.00 34.11 ATOM 430 O SER A 69 55.817 33.794 121.388 1.00 34.65 ATOM 431 N ALA A 70 57.397 32.520 120.463 1.00 34.71 ATOM 432 CA ALA A 70 56.459 31.809 119.603 1.00 38.14 ATOM 433 CB ALA A 70 57.228 31.060 118.527 1.00 37.34 ATOM 434 C ALA A 70 55.508 30.844 120.322 1.00 39.12 ATOM 435 O ALA A 70 54.511 30.405 119.747 1.00 39.71 ATOM 436 N ASN A 71 55.811 30.520 121.573 1.00 39.27 ATOM 437 CA ASN A 71 54.986 29.584 122.320 1.00 39.70 ATOM 438 CB ASN A 71 53.626 30.212 122.640 1.00 40.65 ATOM 439 CG ASN A 71 52.815 29.386 123.638 1.00 41.06 ATOM 440 OD1 ASN A 71 52.788 29.684 124.835 1.00 41.08 ATOM 441 ND2 ASN A 71 52.158 28.334 123.145 1.00 41.61 ATOM 442 C ASN A 71 54.786 28.295 121.497 1.00 39.74 ATOM 443 O ASN A 71 53.667 27.806 121.356 1.00 40.01 ATOM 444 N ARG A 72 55.874 27.766 120.940 1.00 38.92 ATOM 445 CA ARG A 72 55.837 26.534 120.155 1.00 37.82 ATOM 446 CB ARG A 72 55.961 26.813 118.652 1.00 38.60 ATOM 447 CG ARG A 72 54.771 27.458 117.997 1.00 40.39 ATOM 448 CD ARG A 72 55.025 27.683 116.503 1.00 41.15 ATOW 449 NE ARG A 72 53.873 28.320 115.866 1.00 43.72 ATOM 450 CZ ARG A 72 52.870 27.668 115.279 1.00 43.26 ATOM 451 NH1 ARG A 72 52.865 26.342 115.221 1.00 43.91 ATOM 452 NH2 ARG A 72 51.844 28.349 114.782 1.00 42.43 ATOM 453 C ARG A 72 57.008 25.655 120.576 1.00 36.80 ATOM 454 O ARG A 72 58.002 26.149 121.096 1.00 35.83 ATOM 455 N TYR A 73 56.888 24.358 120.310 1.00 36.24 ATOM 456 CA TYR A 73 57.904 23.383 120.666 1.00 34.68 ATOM 457 CB TYR A 73 57.241 22.193 121.365 1.00 34.67 ATOM 458 CG TYR A 73 56.510 22.600 122.634 1.00 37.17 ATOM 459 CD1 TYR A 73 55.248 23.208 122.586 1.00 35.65 ATOM 46O CE1 TYR A 73 54.625 23.675 123.752 1.00 33.81 ATOM 461 CD2 TYR A 73 57.123 22.463 123.888 1.00 37.73 ATOM 462 CE2 TYR A 73 56.505 22.928 125.054 1.00 34.97 ATOM 463 CZ TYR A 73 55.264 23.530 124.974 1.00 33.93 ATOM 464 OH TYR A 73 54.684 23.988 126.125 1.00 31.81 ATOM 465 C TYR A 73 58.680 22.904 119.460 1.00 35.98 ATOM 466 O TYR A 73 58.093 22.516 118.453 1.00 36.90 ATOM 467 N LEU A 74 60.006 22.941 119.558 1.00 36.36 ATOM 468 CA LEU A 74 60.869 22.495 118.471 1.00 36.15 ATOM 469 CB LEU A 74 62.340 22.635 118.868 1.00 35.84 ATOM 470 CG LEU A 74 63.337 21.933 117.941 1.00 35.61 ATOM 471 CD1 LEU A 74 63.478 22.738 116.675 1.00 37.88 ATOM 472 CD2 LEU A 74 64.689 21.791 118.601 1.00 35.93 ATOM 473 C LEU A 74 60.571 21.029 118.192 1.00 37.21 ATOM 474 O LEU A 74 60.536 20.219 119.119 1.00 38.28 ATOM 475 N ALA A 75 60.361 20.685 116.926 1.00 37.24 ATOM 476 CA ALA A 75 60.076 19.310 116.572 1.00 36.32 ATOM 477 CB ALA A 75 58.599 19.140 116.354 1.00 34.38 ATOM 478 C ALA A 75 60.849 18.841 115.347 1.00 38.35 ATOM 479 O ALA A 75 61.073 19.591 114.398 1.00 39.59 ATOM 480 N MET A 76 61.262 17.583 115.398 1.00 41.23 ATOM 481 CA MET A 76 62.005 16.928 114.337 1.00 43.91 ATOM 482 CB MET A 76 63.081 16.043 114.955 1.00 43.17 ATOM 483 CG MET A 76 63.893 15.252 113.964 1.00 42.26 ATOM 484 SD MET A 76 65.172 16.245 113.248 1.00 44.57 ATOM 485 CE MET A 76 66.636 15.543 113.985 1.00 40.99 ATOM 486 C MET A 76 60.983 16.058 113.614 1.00 47.78 ATOM 487 O MET A 76 60.247 15.306 114.256 1.00 47.85 ATOM 488 N LYS A 77 60.941 16.151 112.289 1.00 51.17 ATOM 489 CA LYS A 77 59.989 15.376 111.506 1.00 53.40 ATOM 490 CB LYS A 77 59.462 16.230 110.359 1.00 55.29 ATOM 491 CG LYS A 77 59.035 17.633 110.791 1.00 57.32 ATOM 492 CD LYS A 77 57.874 17.601 111.772 1.00 59.11 ATOM 493 CE LYS A 77 56.622 17.010 111.129 1.00 60.34 ATOM 494 NZ LYS A 77 55.421 17.122 112.010 1.00 60.76 ATOM 495 C LYS A 77 60.644 14.114 110.975 1.00 54.55 ATOM 496 O LYS A 77 61.869 14.008 110.949 1.00 54.47 ATOM 497 N GLU A 78 59.818 13.165 110.548 1.00 56.34 ATOM 498 CA GLU A 78 60.299 11.888 110.038 1.00 58.33 ATOM 499 CB GLU A 78 59.135 11.094 109.470 1.00 60.98 ATOM 500 CG GLU A 78 58.563 11.682 108.209 1.00 65.49 ATOM 501 CD GLU A 78 57.240 11.052 107.846 1.00 69.33 ATOM 502 OE1 GLU A 78 57.134 9.804 107.922 1.00 70.62 ATOM 503 OE2 GLU A 78 56.308 11.805 107.484 1.00 71.91 ATOM 504 C GLU A 78 61.397 12.002 108.987 1.00 57.93 ATOM 505 O GLU A 78 62.294 11.163 108.933 1.00 57.53 ATOM 506 N ASP A 79 61.328 13.036 108.154 1.00 57.03 ATOM 507 CA ASP A 79 62.324 13.234 107.102 1.00 56.19 ATOM 508 CB ASP A 79 61.695 13.958 105.914 1.00 54.79 ATOM 509 CG ASP A 79 61.251 15.353 106.264 1.00 54.84 ATOM 510 OD1 ASP A 79 60.626 16.013 105.406 1.00 55.03 ATOM 511 OD2 ASP A 79 61.531 15.788 107.400 1.00 54.33 ATOM 512 C ASP A 79 63.527 14.032 107.599 1.00 55.83 ATOM 513 O ASP A 79 64.516 14.210 106.876 1.00 56.39 ATOM 514 N GLY A 80 63.430 14.528 108.827 1.00 53.82 ATOM 515 CA GLY A 80 64.532 15.283 109.388 1.00 51.60 ATOM 516 C GLY A 80 64.448 16.794 109.282 1.00 49.35 ATOM 517 O GLY A 80 65.457 17.483 109.428 1.00 48.60 ATOM 518 N ARG A 81 63.263 17.328 109.023 1.00 47.11 ATOM 519 CA ARG A 81 63.142 18.772 108.942 1.00 45.50 ATOM 520 CB ARG A 81 62.191 19.185 107.814 1.00 46.15 ATOM 521 CG ARG A 81 60.754 18.770 108.012 1.00 47.86 ATOM 522 CD ARG A 81 59.879 19.203 106.845 1.00 48.98 ATOM 523 NE ARG A 81 58.461 18.940 107.100 1.00 50.64 ATOM 524 CZ ARG A 81 57.931 17.726 107.253 1.00 51.67 ATOM 525 NH1 ARG A 81 58.696 16.635 107.176 1.00 50.89 ATOM 526 NH2 ARG A 81 56.631 17.597 107.492 1.00 51.50 ATOM 527 C ARG A 81 62.649 19.296 110.283 1.00 44.44 ATOM 528 O ARG A 81 61.926 18.614 111.001 1.00 43.89 ATOM 529 N LEU A 82 63.052 20.510 110.629 1.00 43.77 ATOM 530 CA LEU A 82 62.641 21.096 111.897 1.00 42.44 ATOM 531 CB LEU A 82 63.772 21.908 112.533 1.00 43.49 ATOM 532 CG LEU A 82 65.163 21.304 112.660 1.00 44.62 ATOM 533 CD1 LEU A 82 66.064 22.291 113.388 1.00 44.86 ATOM 534 CD2 LEU A 82 65.080 19.985 113.408 1.00 46.49 ATOM 535 C LEU A 82 61.466 22.025 111.717 1.00 41.65 ATOM 536 O LEU A 82 61.255 22.585 110.643 1.00 42.91 ATOM 537 N LEU A 83 60.709 22.189 112.791 1.00 40.18 ATOM 538 CA LEU A 83 59.565 23.083 112.812 1.00 39.02 ATOM 539 CB LEU A 83 58.405 22.518 111.987 1.00 36.36 ATOM 540 CG LEU A 83 57.635 21.274 112.448 1.00 34.63 ATOM 541 CD1 LEU A 83 56.792 21.559 113.671 1.00 31.47 ATOM 542 CD2 LEU A 83 56.746 20.832 111.313 1.00 34.37 ATOM 543 C LEU A 83 59.177 23.194 114.273 1.00 40.14 ATOM 544 O LEU A 83 59.630 22.403 115.095 1.00 38.27 ATOM 545 N ALA A 84 58.351 24.176 114.604 1.00 41.60 ATOM 546 CA ALA A 64 57.934 24.344 115.986 1.00 43.32 ATOM 547 CB ALA A 84 58.311 25.730 116.490 1.00 41.67 ATOM 548 C ALA A 84 56.438 24.112 116.114 1.00 45.19 ATOM 549 O ALA A 84 55.623 24.927 115.677 1.00 46.57 ATOM 550 N SER A 85 56.096 22.981 116.721 1.00 46.92 ATOM 551 CA SER A 85 54.714 22.561 116.938 1.00 47.45 ATOM 552 CB SER A 85 54.703 21.115 117.450 1.00 47.39 ATOM 553 OG SER A 85 53.386 20.674 117.709 1.00 49.88 ATOM 554 C SER A 85 53.983 23.465 117.928 1.00 48.14 ATOM 555 O SER A 85 54.601 24.078 118.799 1.00 49.09 ATOM 556 N LYS A 86 52.664 23.547 117.793 1.00 47.71 ATOM 557 CA LYS A 86 51.878 24.385 118.684 1.00 47.45 ATOM 558 CB LYS A 86 50.490 24.614 118.095 1.00 49.56 ATOM 559 CG LYS A 86 49.813 25.891 118.567 1.00 51.27 ATOM 560 CD LYS A 86 50.287 27.073 117.740 1.00 53.09 ATOM 561 CE LYS A 86 49.472 28.321 118.005 1.00 53.92 ATOM 562 NZ LYS A 86 49.716 29.341 116.934 1.00 57.90 ATOM 563 C LYS A 86 51.752 23.692 120.033 1.00 46.65 ATOM 564 O LYS A 86 51.873 24.319 121.086 1.00 46.47 ATOM 565 N SER A 87 51.496 22.389 119.986 1.00 45.59 ATOM 566 CA SER A 87 51.351 21.587 121.194 1.00 44.66 ATOM 567 CB SER A 87 49.939 20.992 121.282 1.00 43.08 ATOM 568 OG SER A 87 49.701 20.091 120.221 1.00 40.33 ATOM 569 C SER A 87 52.391 20.474 121.144 1.00 44.59 ATOM 570 O SER A 87 52.881 20.111 120.074 1.00 43.61 ATOM 571 N VAL A 88 52.718 19.926 122.306 1.00 44.63 ATOM 572 CA VAL A 88 53.729 18.883 122.374 1.00 43.82 ATOM 573 CB VAL A 88 54.187 18.656 123.824 1.00 43.24 ATOM 574 CG1 VAL A 88 55.408 17.749 123.837 1.00 42.87 ATOM 575 CG2 VAL A 88 54.495 19.995 124.490 1.00 41.50 ATOM 576 C VAL A 88 53.314 17.542 121.782 1.00 43.66 ATOM 577 O VAL A 88 52.230 17.028 122.066 1.00 44.12 ATOM 578 N THR A 89 54.182 16.991 120.938 1.00 43.04 ATOM 579 CA THR A 89 53.950 15.683 120.337 1.00 42.15 ATOM 580 CB THR A 89 53.761 15.750 118.798 1.00 43.10 ATOM 581 OG1 THR A 89 55.033 15.794 118.144 1.00 46.42 ATOM 582 CG2 THR A 89 52.976 16.988 118.422 1.00 43.70 ATOM 583 C THR A 89 55.183 14.862 120.706 1.00 41.22 ATOM 584 O THR A 89 56.020 15.320 121.480 1.00 40.52 ATOM 585 N ASP A 90 55.311 13.657 120.172 1.00 41.76 ATOM 586 CA ASP A 90 56.447 12.821 120.545 1.00 42.49 ATOM 587 CB ASP A 90 56.095 11.340 120.379 1.00 43.14 ATOM 588 CG ASP A 90 56.112 10.893 118.925 1.00 45.82 ATOM 589 OD1 ASP A 90 55.470 11.559 118.084 1.00 45.52 ATOM 590 OD2 ASP A 90 56.769 9.869 118.625 1.00 47.64 ATOM 591 C ASP A 90 57.727 13.143 119.785 1.00 42.84 ATOM 592 O ASP A 90 58.759 12.495 119.989 1.00 43.34 ATOM 593 N GLU A 91 57.664 14.148 118.915 1.00 42.08 ATOM 594 CA GLU A 91 58.825 14.557 118.127 1.00 39.76 ATOM 595 CB GLU A 91 58.409 14.855 116.681 1.00 39.16 ATOM 596 CG GLU A 91 58.045 13.608 115.869 1.00 39.61 ATOM 597 CD GLU A 91 57.290 13.940 114.595 1.00 39.92 ATOM 598 OE1 GLU A 91 56.277 14.666 114.694 1.00 40.67 ATOM 599 OE2 GLU A 91 57.696 13.475 113.505 1.00 37.43 ATOM 600 C GLU A 91 59.435 15.794 118.756 1.00 37.44 ATOM 601 O GLU A 91 60.395 16.354 118.241 1.00 35.98 ATOM 602 N CYS A 92 58.878 16.201 119.887 1.00 35.82 ATOM 603 CA CYS A 92 59.355 17.386 120.581 1.00 36.58 ATOM 604 CB CYS A 92 58.161 18.157 121.138 1.00 38.16 ATOM 605 SG CYS A 92 57.052 18.772 119.863 1.00 43.78 ATOM 606 C CYS A 92 60.363 17.110 121.703 1.00 35.32 ATOM 607 O CYS A 92 60.642 17.990 122.530 1.00 33.99 ATOM 608 N PHE A 93 60.926 15.902 121.716 1.00 33.77 ATOM 609 CA PHE A 93 61.886 15.526 122.750 1.00 31.34 ATOM 610 CB PHE A 93 61.323 14.349 123.541 1.00 27.27 ATOM 611 CG PHE A 93 60.019 14.670 124.211 1.00 24.63 ATOM 612 CD1 PHE A 93 59.981 15.537 125.297 1.00 23.64 ATOM 613 CD2 PHE A 93 58.819 14.185 123.703 1.00 24.13 ATOM 614 CE1 PHE A 93 58.766 15.924 125.864 1.00 22.52 ATOM 615 CE2 PHE A 93 57.598 14.571 124.268 1.00 23.86 ATOM 616 CZ PHE A 93 57.576 15.442 125.351 1.00 21.53 ATOM 617 C PHE A 93 63.261 15.218 122.184 1.00 31.25 ATOM 618 O PHE A 93 63.389 14.592 121.132 1.00 31.43 ATOM 619 N PHE A 94 64.290 15.679 122.889 1.00 31.24 ATOM 620 CA PHE A 94 65.663 15.489 122.445 1.00 30.43 ATOM 621 CB PHE A 94 66.181 16.789 121.821 1.00 30.29 ATOM 622 CG PHE A 94 65.320 17.309 120.701 1.00 29.49 ATOM 623 CD1 PHE A 94 65.534 16.892 119.386 1.00 28.03 ATOM 624 CD2 PHE A 94 64.265 18.182 120.967 1.00 27.75 ATOM 625 CE1 PHE A 94 64.707 17.333 118.363 1.00 26.35 ATOM 626 CE2 PHE A 94 63.434 18.625 119.947 1.00 25.73 ATOM 627 CZ PHE A 94 63.653 18.204 118.649 1.00 25.48 ATOM 628 C PHE A 94 66.584 15.089 123.582 1.00 30.16 ATOM 629 O PHE A 94 66.328 15.407 124.748 1.00 30.02 ATOM 630 N PHE A 95 67.657 14.393 123.225 1.00 29.48 ATOM 631 CA PHE A 95 68.658 13.968 124.186 1.00 29.03 ATOM 632 CB PHE A 95 69.362 12.721 123.668 1.00 31.70 ATOM 633 CG PHE A 95 68.469 11.523 123.582 1.00 34.61 ATOM 634 CD1 PHE A 95 68.600 10.618 122.533 1.00 36.23 ATOM 635 CD2 PHE A 95 67.497 11.291 124.553 1.00 36.09 ATOM 636 CE1 PHE A 95 67.776 9.492 122.447 1.00 35.87 ATOM 637 CE2 PHE A 95 66.665 10.170 124.480 1.00 36.33 ATOM 638 CZ PHE A 95 66.807 9.269 123.421 1.00 36.80 ATOM 639 C PHE A 95 69.659 15.099 124.365 1.00 28.52 ATOM 640 O PHE A 95 70.512 15.339 123.502 1.00 27.18 ATOM 641 N GLU A 96 69.533 15.819 125.474 1.00 28.65 ATOM 642 CA GLU A 96 70.448 16.910 125.744 1.00 29.50 ATOM 643 CB GLU A 96 69.858 17.889 126.756 1.00 27.99 ATOM 644 CG GLU A 96 70.801 19.042 127.058 1.00 29.21 ATOM 645 CD GLU A 96 70.265 20.005 128.098 1.00 31.55 ATOM 646 OE1 GLU A 96 70.020 19.575 129.250 1.00 31.32 ATOM 647 OE2 GLU A 96 70.097 21.198 127.767 1.00 33.49 ATOM 648 C GLU A 96 71.707 16.280 126.311 1.00 31.72 ATOM 649 O GLU A 96 71.683 15.666 127.384 1.00 34.11 ATOM 650 N ARG A 97 72.803 16.404 125.578 1.00 31.74 ATOM 651 CA ARG A 97 74.056 15.835 126.034 1.00 31.84 ATOM 652 CB ARG A 97 74.425 14.637 125.176 1.00 34.27 ATOM 653 CG ARG A 97 75.761 14.043 125.540 1.00 38.54 ATOM 654 CD ARG A 97 76.319 13.201 124.417 1.00 42.56 ATOM 655 NE ARG A 97 77.711 12.881 124.699 1.00 49.50 ATOM 656 CZ ARG A 97 78.102 11.907 125.513 1.00 52.72 ATOM 657 NH1 ARG A 97 77.191 11.143 126.114 1.00 52.62 ATOM 658 NH2 ARG A 97 79.400 11.722 125.756 1.00 51.89 ATOM 659 C ARG A 97 75.198 16.838 125.995 1.00 30.59 ATOM 660 O ARG A 97 75.453 17.463 124.969 1.00 32.34 ATOM 661 N LEU A 98 75.872 16.999 127.126 1.00 28.50 ATOM 662 C ALEU A 98 77.019 17.884 127.221 1.00 27.17 ATOM 663 CB LEU A 98 77.184 18.371 128.661 1.00 21.92 ATOM 664 CG LEU A 98 78.523 18.977 129.071 1.00 20.39 ATOM 665 CD1 LEU A 98 78.988 19.998 128.063 1.00 21.52 ATOM 666 CD2 LEU A 98 78.376 19.607 130.430 1.00 21.24 ATOM 667 C LEU A 98 78.242 17.063 126.777 1.00 28.93 ATOM 668 O LEU A 98 78.787 16.276 127.546 1.00 31.40 ATOM 669 N GLU A 99 78.652 17.240 125.524 1.00 30.17 ATOM 670 CA GLU A 99 79.785 16.515 124.951 1.00 31.19 ATOM 671 CB GLU A 99 79.948 16.876 123.476 1.00 29.56 ATOM 672 CG GLU A 99 78.693 16.717 122.678 1.00 31.83 ATOM 673 CD GLU A 99 78.207 15.291 122.655 1.00 33.86 ATOM 674 OE1 GLU A 99 77.101 15.036 122.129 1.00 32.15 ATOM 675 OE2 GLU A 99 78.943 14.422 123.161 1.00 37.73 ATOM 676 C GLU A 99 81.098 16.808 125.661 1.00 33.20 ATOM 677 O GLU A 99 81.194 17.747 126.467 1.00 32.11 ATOM 678 N SER A 100 82.119 16.020 125.323 1.00 34.00 ATOM 679 CA SER A 100 83.432 16.186 125.930 1.00 36.02 ATOM 680 CB SER A 100 84.331 14.982 125.628 1.00 37.15 ATOM 681 OG SER A 100 84.846 15.048 124.312 1.00 42.19 ATOM 682 C SER A 100 84.142 17.468 125.502 1.00 35.51 ATOM 683 O SER A 100 85.099 17.882 126.151 1.00 36.82 ATOM 684 N ASN A 101 83.690 18.104 124.425 1.00 35.15 ATOM 685 CA ASN A 101 84.338 19.343 123.984 1.00 33.34 ATOM 686 CB ASN A 101 84.212 19.521 122.475 1.00 35.00 ATOM 687 CG ASN A 101 82.782 19.684 122.040 1.00 37.73 ATOM 688 OD1 ASN A 101 81.895 19.882 122.873 1.00 39.82 ATOM 689 ND2 ASN A 101 82.541 19.609 120.736 1.00 39.52 ATOM 690 C ASN A 101 83.721 20.546 124.677 1.00 30.87 ATOM 691 O ASN A 101 84.142 21.669 124.448 1.00 29.80 ATOM 692 N ASN A 102 82.722 20.287 125.521 1.00 30.67 ATOM 693 CA ASN A 102 81.991 21.309 126.286 1.00 29.39 ATOM 694 CB ASN A 102 82.929 22.348 126.914 1.00 31.37 ATOM 695 CG ASN A 102 83.496 21.900 128.257 1.00 33.09 ATOM 696 OD1 ASN A 102 83.095 20.871 128.810 1.00 33.67 ATOM 697 ND2 ASN A 102 84.429 22.683 128.789 1.00 32.79 ATOM 698 C ASN A 102 80.911 22.031 125.508 1.00 27.39 ATOM 699 O ASN A 102 80.558 23.164 125.818 1.00 26.13 ATOM 700 N TYR A 103 80.389 21.354 124.500 1.00 26.24 ATOM 701 CA TYR A 103 79.314 21.879 123.697 1.00 26.55 ATOM 702 CB TYR A 103 79.766 21.964 122.244 1.00 29.17 ATOM 703 CG TYR A 103 80.580 23.210 121.940 1.00 30.57 ATOM 704 CD1 TYR A 103 79.959 24.456 121.824 1.00 30.73 ATOM 705 CE1 TYR A 103 80.692 25.600 121.576 1.00 30.98 ATOM 706 CD2 TYR A 103 81.968 23.151 121.797 1.00 29.10 ATOM 707 CE2 TYR A 103 82.713 24.300 121.551 1.00 28.71 ATOM 708 CZ TYR A 103 82.068 25.518 121.441 1.00 31.03 ATOM 709 OH TYR A 103 82.785 26.665 121.192 1.00 33.17 ATOM 710 C TYR A 103 78.150 20.904 123.883 1.00 26.39 ATOM 711 O TYR A 103 78.359 19.738 124.203 1.00 25.31 ATOM 712 N ASN A 104 76.926 21.394 123.729 1.00 26.69 ATOM 713 CA ASN A 104 75.738 20.565 123.893 1.00 25.29 ATOM 714 CB ASN A 104 74.596 21.367 124.536 1.00 25.30 ATOM 715 CG ASN A 104 74.775 21.582 126.038 1.00 25.81 ATOM 716 OD1 ASN A 104 75.896 21.637 126.545 1.00 26.52 ATOM 717 ND2 ASN A 104 73.658 21.728 126.750 1.00 24.06 ATOM 718 C ASN A 104 75.267 20.094 122.534 1.00 25.53 ATOM 719 O ASN A 104 75.528 20.734 121.521 1.00 24.70 ATOM 720 N THR A 105 74.580 18.960 122.523 1.00 26.46 ATOM 721 CA THR A 105 74.005 18.429 121.299 1.00 27.72 ATOM 722 CB THR A 105 74.758 17.240 120.765 1.00 28.31 ATOM 723 OG1 THR A 105 74.707 16.185 121.730 1.00 30.41 ATOM 724 CG2 THR A 105 76.187 17.630 120.464 1.00 29.27 ATOM 725 C THR A 105 72.597 17.975 121.621 1.00 27.86 ATOM 726 O THR A 105 72.337 17.441 122.703 1.00 26.82 ATOM 727 N TYR A 106 71.691 18.189 120.675 1.00 27.97 ATOM 728 CA TYR A 106 70.309 17.808 120.869 1.00 28.05 ATOM 729 CB TYR A 106 69.443 19.054 120.819 1.00 25.08 ATOM 730 CG TYR A 106 69.764 19.973 121.966 1.00 23.18 ATOM 731 CD1 TYR A 106 68.973 19.987 123.118 1.00 21.13 ATOM 732 CE1 TYR A 106 69.297 20.791 124.205 1.00 20.58 ATOM 733 CD2 TYR A 106 70.894 20.790 121.928 1.00 20.43 ATOM 734 CE2 TYR A 106 71.229 21.591 123.004 1.00 21.60 ATOM 735 CZ TYR A 106 70.431 21.591 124.147 1.00 21.86 ATOM 736 OH TYR A 106 70.798 22.368 125.234 1.00 22.45 ATOM 737 C TYR A 106 69.893 16.784 119.838 1.00 30.08 ATOM 738 O TYR A 106 69.630 17.105 118.676 1.00 30.82 ATOM 739 N ARG A 107 69.841 15.538 120.292 1.00 31.66 ATOM 740 CA ARG A 107 69.503 14.405 119.447 1.00 32.61 ATOM 741 CB ARG A 107 70.392 13.220 119.842 1.00 32.36 ATOM 742 CG ARG A 107 70.434 12.064 118.872 1.00 32.70 ATOM 743 CD ARG A 107 71.697 11.253 119.117 1.00 34.85 ATOM 744 NE ARG A 107 71.800 10.744 120.491 1.00 36.65 ATOM 745 CZ ARG A 107 71.106 9.708 120.963 1.00 35.72 ATOM 746 NH1 ARG A 107 70.258 9.071 120.169 1.00 36.28 ATOM 747 NH2 ARG A 107 71.259 9.301 122.218 1.00 32.47 ATOM 748 C ARG A 107 68.039 14.040 119.589 1.00 33.19 ATOM 749 O ARG A 107 67.524 13.930 120.700 1.00 34.18 ATOM 750 N SER A 108 67.375 13.858 118.453 1.00 34.58 ATOM 751 CA SER A 108 65.966 13.477 118.416 1.00 36.35 ATOM 752 CB SER A 108 65.511 13.306 116.960 1.00 37.24 ATOM 753 OG SER A 108 64.124 13.019 116.878 1.00 39.38 ATOM 754 C SER A 108 65.735 12.162 119.160 1.00 37.63 ATOM 755 O SER A 108 66.339 11.134 118.837 1.00 35.70 ATOM 756 N ARG A 109 64.851 12.189 120.148 1.00 40.12 ATOM 757 CA ARG A 109 64.557 10.984 120.905 1.00 42.97 ATOM 758 CB ARG A 109 63.705 11.321 122.139 1.00 46.15 ATOM 759 CG ARG A 109 63.406 10.117 123.032 1.00 49.94 ATOM 760 CD ARG A 109 62.781 10.490 124.386 1.00 53.41 ATOM 761 NE ARG A 109 61.383 10.928 124.305 1.00 56.68 ATOM 762 CZ ARG A 109 60.598 11.121 125.367 1.00 57.49 ATOM 763 NH1 ARG A 109 61.066 10.914 126.594 1.00 58.10 ATOM 764 NH2 ARG A 109 59.345 11.526 125.210 1.00 57.66 ATOM 765 C ARG A 109 63.810 10.009 120.006 1.00 43.50 ATOM 766 O ARG A 109 63.879 8.800 120.204 1.00 43.69 ATOM 767 N LYS A 110 63.112 10.541 119.007 1.00 44.03 ATOM 768 CA LYS A 110 62.349 9.706 118.097 1.00 44.44 ATOM 769 CB LYS A 110 61.105 10.457 117.627 1.00 45.66 ATOM 770 CG LYS A 110 60.215 9.607 116.755 1.00 47.20 ATOM 771 CD LYS A 110 58.823 10.168 116.618 1.00 49.29 ATOM 772 CE LYS A 110 57.912 9.130 115.962 1.00 50.25 ATOM 773 NZ LYS A 110 56.508 9.603 115.819 1.00 51.01 ATOM 774 C LYS A 110 63.150 9.222 116.893 1.00 46.02 ATOM 775 O LYS A 110 63.013 8.068 116.477 1.00 47.58 ATOM 776 N TYR A 111 63.974 10.099 116.324 1.00 46.38 ATOM 777 CA TYR A 111 64.807 9.743 115.172 1.00 46.60 ATOM 778 CB TYR A 111 64.630 10.778 114.061 1.00 46.06 ATOM 779 CG TYR A 111 63.177 11.000 113.702 1.00 45.65 ATOM 780 CD1 TYR A 111 62.432 9.998 113.081 1.00 46.57 ATOM 781 CE1 TYR A 111 61.069 10.160 112.823 1.00 44.89 ATOM 782 CD2 TYR A 111 62.523 12.183 114.052 1.00 45.29 ATOM 783 CE2 TYR A 111 61.164 12.357 113.801 1.00 45.59 ATOM 784 CZ TYR A 111 60.444 11.338 113.188 1.00 45.93 ATOM 785 OH TYR A 111 59.100 11.493 112.952 1.00 45.61 ATOM 786 C TYR A 111 66.248 9.721 115.666 1.00 47.88 ATOM 787 O TYR A 111 67.111 10.437 115.162 1.00 49.06 ATOM 788 N THR A 112 66.462 8.879 116.674 1.00 48.36 ATOM 789 CA THR A 112 67.730 8.672 117.373 1.00 48.90 ATOM 790 CB THR A 112 67.812 7.236 117.871 1.00 49.47 ATOM 791 OG1 THR A 112 67.705 6.338 116.757 1.00 51.22 ATOM 792 CG2 THR A 112 66.698 6.968 118.851 1.00 49.93 ATOM 793 C THR A 112 69.081 8.987 116.732 1.00 48.64 ATOM 794 O THR A 112 70.041 9.265 117.452 1.00 48.37 ATOM 795 N SER A 113 69.183 8.932 115.408 1.00 47.78 ATOM 796 CA SER A 113 70.465 9.207 114.759 1.00 47.11 ATOM 797 CB SER A 113 70.764 8.116 113.710 1.00 48.27 ATOM 798 OG SER A 113 69.752 8.012 112.716 1.00 49.10 ATOM 799 C SER A 113 70.606 10.606 114.122 1.00 46.61 ATOM 800 O SER A 113 71.570 10.866 113.388 1.00 46.29 ATOM 801 N TRP A 114 69.666 11.505 114.418 1.00 44.06 ATOM 802 CA TRP A 114 69.687 12.849 113.856 1.00 41.41 ATOM 803 CB TRP A 114 68.442 13.091 113.015 1.00 41.01 ATOM 804 CG TRP A 114 68.258 12.140 111.889 1.00 40.42 ATOM 805 CD2 TRP A 114 67.052 11.918 111.155 1.00 38.46 ATOM 806 CE2 TRP A 114 67.359 11.016 110.108 1.00 38.51 ATOM 807 CE3 TRP A 114 65.744 12.398 111.276 1.00 37.09 ATOM 808 CD1 TRP A 114 69.221 11.380 111.284 1.00 41.23 ATOM 809 NE1 TRP A 114 68.689 10.704 110.212 1.00 40.74 ATOM 810 CZ2 TRP A 114 66.405 10.586 109.184 1.00 35.23 ATOM 811 CZ3 TRP A 114 64.793 11.972 110.357 1.00 37.18 ATOM 812 CH2 TRP A 114 65.133 11.074 109.322 1.00 37.14 ATOM 813 C TRP A 114 69.732 13.918 114.923 1.00 41.41 ATOM 814 O TRP A 114 69.090 13.778 115.963 1.00 41.05 ATOM 815 N TYR A 115 70.462 14.999 114.635 1.00 41.08 ATOM 816 CA TYR A 115 70.618 16.136 115.548 1.00 39.88 ATOM 817 CB TYR A 115 72.096 16.472 115.766 1.00 41.04 ATOM 818 CG TYR A 115 72.945 15.383 116.345 1.00 43.89 ATOM 819 CD1 TYR A 115 73.605 14.478 115.523 1.00 43.91 ATOM 820 CE1 TYR A 115 74.394 13.474 116.058 1.00 45.80 ATOM 821 CD2 TYR A 115 73.092 15.258 117.726 1.00 45.48 ATOM 822 CE2 TYR A 115 73.870 14.258 118.273 1.00 45.73 ATOM 823 CZ TYR A 115 74.519 13.367 117.438 1.00 46.36 ATOM 824 OH TYR A 115 75.277 12.356 117.992 1.00 47.60 ATOM 825 C TYR A 115 69.989 17.445 115.073 1.00 38.37 ATOM 826 O TYR A 115 69.880 17.706 113.876 1.00 37.51 ATOM 827 N VAL A 116 69.598 18.276 116.031 1.00 36.40 ATOM 828 CA VAL A 116 69.099 19.603 115.730 1.00 35.41 ATOM 829 CB VAL A 116 68.590 20.297 117.010 1.00 32.19 ATOM 830 CG1 VAL A 116 68.369 21.759 116.754 1.00 32.30 ATOM 831 CG2 VAL A 116 67.313 19.662 117.480 1.00 32.27 ATOM 832 C VAL A 116 70.416 20.279 115.297 1.00 37.32 ATOM 833 O VAL A 116 71.411 20.209 116.024 1.00 39.26 ATOM 834 N ALA A 117 70.453 20.912 114.129 1.00 37.44 ATOM 835 CA ALA A 117 71.697 21.547 113.677 1.00 37.22 ATOM 836 CB ALA A 117 72.604 20.510 113.015 1.00 34.89 ATOM 837 C ALA A 117 71.454 22.702 112.717 1.00 37.59 ATOM 838 O ALA A 117 70.430 22.747 112.042 1.00 41.05 ATOM 839 N LEU A 118 72.398 23.636 112.652 1.00 35.93 ATOM 840 CA LEU A 118 72.264 24.780 111.760 1.00 33.55 ATOM 841 CB LEU A 118 72.152 26.065 112.587 1.00 29.51 ATOM 842 CG LEU A 118 70.944 26.105 113.531 1.00 27.36 ATOM 843 CD1 LEU A 118 70.899 27.395 114.344 1.00 25.77 ATOM 844 CD2 LEU A 118 69.692 25.969 112.710 1.00 25.54 ATOM 845 C LEU A 118 73.436 24.869 110.772 1.00 35.22 ATOM 846 O LEU A 118 74.592 24.611 111.125 1.00 33.57 ATOM 847 N LYS A 119 73.130 25.217 109.523 1.00 37.24 ATOM 848 CA LYS A 119 74.162 25.347 108.493 1.00 36.59 ATOM 849 CB LYS A 119 73.560 25.312 107.092 1.00 33.96 ATOM 850 CG LYS A 119 72.815 24.064 106.692 1.00 29.96 ATOM 851 CD LYS A 119 71.942 24.425 105.511 1.00 29.66 ATOM 852 CE LYS A 119 71.331 23.224 104.833 1.00 33.54 ATOM 853 NZ LYS A 119 71.921 22.954 103.486 1.00 35.42 ATOM 854 C LYS A 119 74.902 26.677 108.653 1.00 39.10 ATOM 855 O LYS A 119 74.431 27.604 109.332 1.00 36.63 ATOM 856 N ARG A 120 76.061 26.758 108.001 1.00 42.69 ATOM 857 CA ARG A 120 76.912 27.947 108.038 1.00 44.11 ATOM 858 CB ARG A 120 78.206 27.696 107.225 1.00 47.39 ATOM 859 CG ARG A 120 78.957 26.401 107.626 1.00 53.28 ATOM 860 CD ARG A 120 80.288 26.112 106.862 1.00 56.82 ATOM 861 NE ARG A 120 81.424 26.933 107.312 1.00 60.63 ATOM 862 CZ ARG A 120 82.712 26.621 107.140 1.00 60.35 ATOM 863 NH1 ARG A 120 83.051 25.494 106.528 1.00 60.36 ATOM 864 NH2 ARG A 120 83.668 27.439 107.578 1.00 60.20 ATOM 865 C ARG A 120 76.141 29.148 107.471 1.00 43.14 ATOM 866 O ARG A 120 76.507 30.300 107.708 1.00 41.07 ATOM 867 N THR A 121 75.059 28.858 106.746 1.00 42.80 ATOM 868 CA THR A 121 74.216 29.876 106.117 1.00 41.17 ATOM 869 CB THR A 121 73.562 29.337 104.811 1.00 40.10 ATOM 870 OG1 THR A 121 72.603 28.317 105.123 1.00 38.39 ATOM 871 CG2 THR A 121 74.617 28.758 103.894 1.00 38.65 ATOM 872 C THR A 121 73.100 30.417 107.012 1.00 41.97 ATOM 873 O THR A 121 72.415 31.370 106.648 1.00 42.59 ATOM 874 N GLY A 122 72.906 29.809 108.175 1.00 42.85 ATOM 875 CA GLY A 122 71.861 30.279 109.063 1.00 43.14 ATOM 876 C GLY A 122 70.534 29.559 108.903 1.00 42.89 ATOM 877 O GLY A 122 69.504 30.038 109.370 1.00 42.66 ATOM 878 N GLN A 123 70.541 28.411 108.240 1.00 43.13 ATOM 879 CA GLN A 123 69.310 27.651 108.068 1.00 44.40 ATOM 880 CB GLN A 123 68.999 27.460 106.593 1.00 43.97 ATOM 881 CG GLN A 123 68.606 28.738 105.924 1.00 45.73 ATOM 882 CD GLN A 123 68.358 28.550 104.461 1.00 47.36 ATOM 883 OE1 GLN A 123 69.230 28.059 103.730 1.00 49.61 ATOM 884 NE2 GLN A 123 67.171 28.939 104.008 1.00 45.86 ATOM 885 C GLN A 123 69.459 26.304 108.736 1.00 43.81 ATOM 886 O GLN A 123 70.562 25.758 108.791 1.00 43.65 ATOM 887 N TYR A 124 68.360 25.759 109.249 1.00 42.36 ATOM 888 CA TYR A 124 68.477 24.473 109.905 1.00 42.34 ATOM 889 CB TYR A 124 67.150 24.034 110.549 1.00 42.89 ATOM 890 CG TYR A 124 66.061 23.552 109.619 1.00 43.69 ATOM 891 CD TYR A 124 66.216 22.388 108.869 1.00 45.57 ATOM 892 CE1 TYR A 124 65.180 21.905 108.060 1.00 46.18 ATOM 893 CD2 TYR A 124 64.845 24.230 109.538 1.00 44.59 ATOM 894 CE2 TYR A 124 63.805 23.759 108.741 1.00 45.52 ATOM 895 CZ TYR A 124 63.977 22.596 108.005 1.00 46.26 ATOM 896 OH TYR A 124 62.943 22.123 107.231 1.00 46.93 ATOM 897 C TYR A 124 68.973 23.433 108.917 1.00 41.35 ATOM 898 O TYR A 124 68.729 23.530 107.718 1.00 41.57 ATOM 899 N LYS A 125 69.701 22.455 109.436 1.00 40.46 ATOM 900 CA LYS A 125 70.243 21.372 108.637 1.00 39.14 ATOM 901 CB LYS A 125 71.682 21.087 109.051 1.00 39.11 ATOM 902 CG LYS A 125 72.407 20.091 108.190 1.00 37.48 ATOM 903 CD LYS A 125 73.887 20.151 108.518 1.00 37.19 ATOM 904 CE LYS A 125 74.688 19.209 107.642 1.00 38.30 ATOM 905 NZ LYS A 125 76.163 19.376 107.821 1.00 40.09 ATOM 906 C LYS A 125 69.377 20.149 108.884 1.00 38.94 ATOM 907 O LYS A 125 69.009 19.841 110.028 1.00 37.71 ATOM 908 N LEU A 126 69.046 19.463 107.799 1.00 38.64 ATOM 909 CA LEU A 126 68.210 18.281 107.871 1.00 38.50 ATOM 910 CE LEU A 126 67.949 17.740 106.470 1.00 38.60 ATOM 911 CG LEU A 126 66.789 18.378 105.716 1.00 38.62 ATOM 912 CD1 LEU A 126 66.711 17.759 104.329 1.00 38.87 ATOM 913 CD2 LEU A 126 65.484 18.156 106.484 1.00 37.99 ATOM 914 C LEU A 126 68.817 17.191 108.723 1.00 38.32 ATOM 915 O LEU A 126 70.006 16.895 108.603 1.00 37.82 ATOM 916 N GLY A 127 67.989 16.599 109.581 1.00 38.45 ATOM 917 CA GLY A 127 68.449 15.530 110.445 1.00 39.64 ATOM 918 C GLY A 127 69.158 14.482 109.616 1.00 40.85 ATOM 919 O GLY A 127 70.275 14.067 109.930 1.00 42.00 ATOM 920 N SER A 128 68.513 14.063 108.535 1.00 41.54 ATOM 921 CA SER A 128 69.084 13.064 107.641 1.00 42.63 ATOM 922 CB SER A 128 68.188 12.916 106.404 1.00 43.01 ATOM 923 OG SER A 128 67.359 14.059 106.223 1.00 43.58 ATOM 924 C SER A 128 70.524 13.379 107.203 1.00 44.28 ATOM 925 O SER A 128 71.232 12.515 106.685 1.00 44.87 ATOM 926 N LYS A 129 70.966 14.612 107.423 1.00 45.93 ATOM 927 CA LYS A 129 72.307 15.013 107.017 1.00 45.44 ATOM 928 CB LYS A 129 72.228 16.234 106.083 1.00 46.85 ATOM 929 CG LYS A 129 71.242 16.098 104.909 1.00 51.95 ATOM 930 CD LYS A 129 71.502 17.129 103.783 1.00 55.26 ATOM 931 CE LYS A 129 71.325 18.594 104.254 1.00 60.79 ATOM 932 NZ LYS A 129 71.878 19.660 103.325 1.00 61.01 ATOM 933 C LYS A 129 73.250 15.336 108.175 1.00 44.17 ATOM 934 O LYS A 129 74.367 15.774 107.945 1.00 43.85 ATOM 935 N THR A 130 72.828 15.123 109.414 1.00 42.92 ATOM 936 CA THR A 130 73.709 15.457 110.525 1.00 42.43 ATOM 937 CB THR A 130 72.934 16.133 111.682 1.00 41.22 ATOM 938 OG1 THR A 130 71.931 15.243 112.194 1.00 39.15 ATOM 939 CG2 THR A 130 72.282 17.408 111.197 1.00 38.70 ATOM 940 C THR A 130 74.506 14.280 111.073 1.00 44.22 ATOM 941 O THR A 130 74.024 13.147 111.127 1.00 44.98 ATOM 942 N GLY A 131 75.739 14.567 111.474 1.00 44.70 ATOM 943 CA GLY A 131 76.608 13.541 112.018 1.00 45.33 ATOM 944 C GLY A 131 77.376 14.055 113.222 1.00 46.80 ATOM 945 O GLY A 131 77.409 15.265 113.471 1.00 47.55 ATOM 946 N PRO A 132 78.016 13.159 113.985 1.00 46.38 ATOM 947 CD PRO A 132 78.213 11.755 113.589 1.00 47.25 ATOM 948 CA PRO A 132 78.808 13.457 115.182 1.00 45.69 ATOM 949 CB PRO A 132 79.259 12.079 115.622 1.00 47.47 ATOM 950 CG PRO A 132 79.497 11.407 114.305 1.00 46.80 ATOM 951 C PRO A 132 80.013 14.370 114.926 1.00 44.62 ATOM 952 O PRO A 132 80.330 15.253 115.731 1.00 45.57 ATOM 953 N GLY A 133 80.698 14.140 113.815 1.00 42.56 ATOM 954 CA GLY A 133 81.850 14.960 113.508 1.00 41.60 ATOM 955 C GLY A 133 81.486 16.319 112.938 1.00 41.19 ATOM 956 O GLY A 133 82.339 17.023 112.411 1.00 40.45 ATOM 957 N GLN A 134 80.223 16.707 113.053 1.00 41.05 ATOM 958 CA GLN A 134 79.784 17.986 112.507 1.00 41.03 ATOM 959 CB GLN A 134 78.422 17.820 111.858 1.00 42.60 ATOM 960 CG GLN A 134 78.439 17.045 110.575 1.00 42.17 ATOM 961 CD GLN A 134 77.077 17.019 109.953 1.00 41.64 ATOM 962 OE1 GLN A 134 76.335 18.001 110.035 1.00 42.15 ATOM 963 NE2 GLN A 134 76.733 15.905 109.319 1.00 41.49 ATOM 964 C GLN A 134 79.726 19.180 113.460 1.00 40.14 ATOM 965 O GLN A 134 79.214 19.090 114.577 1.00 39.81 ATOM 966 N LYS A 135 80.233 20.308 112.972 1.00 38.91 ATOM 967 CA LYS A 135 80.278 21.562 113.715 1.00 36.79 ATOM 968 CB LYS A 135 81.217 22.521 112.985 1.00 36.65 ATOM 969 CG LYS A 135 81.505 23.848 113.651 1.00 38.80 ATOM 970 CD LYS A 135 82.711 24.479 112.939 1.00 41.93 ATOM 971 CE LYS A 135 82.735 26.008 113.003 1.00 44.55 ATOM 972 NZ LYS A 135 83.581 26.607 111.908 1.00 44.29 ATOM 973 C LYS A 135 78.876 22.155 113.831 1.00 35.29 ATOM 974 O LYS A 135 78.604 22.978 114.705 1.00 34.18 ATOM 975 N ALA A 136 77.981 21.705 112.958 1.00 34.66 ATOM 976 CA ALA A 136 76.610 22.191 112.942 1.00 33.50 ATOM 977 CB ALA A 136 75.951 21.816 111.623 1.00 32.41 ATOM 978 C ALA A 136 75.763 21.687 114.109 1.00 33.64 ATOM 979 O ALA A 136 74.823 22.366 114.533 1.00 33.54 ATOM 980 N ILE A 137 76.091 20.510 114.637 1.00 32.69 ATOM 981 CA ILE A 137 75.317 19.942 115.739 1.00 32.18 ATOM 982 CB ILE A 137 75.445 18.405 115.815 1.00 32.98 ATOM 983 CG2 ILE A 137 74.871 17.773 114.554 1.00 33.96 ATOM 984 CG1 ILE A 137 76.908 18.011 116.079 1.00 32.14 ATOM 985 CD1 ILE A 137 77.141 16.506 116.268 1.00 29.78 ATOM 986 C ILE A 137 75.693 20.448 117.111 1.00 32.80 ATOM 987 O ILE A 137 75.029 20.112 118.098 1.00 34.26 ATOM 988 N LEU A 138 76.753 21.244 117.186 1.00 32.26 ATOM 989 CA LEU A 138 77.213 21.743 118.476 1.00 31.34 ATOM 990 CB LEU A 138 78.746 21.780 118.491 1.00 30.49 ATOM 991 CG LEU A 138 79.371 20.440 118.088 1.00 30.42 ATOM 992 CD1 LEU A 138 80.876 20.550 118.071 1.00 31.69 ATOM 993 CD2 LEU A 138 78.944 19.352 119.061 1.00 32.51 ATOM 994 C LEU A 138 76.640 23.104 118.862 1.00 30.99 ATOM 995 O LEU A 138 76.717 24.068 118.099 1.00 30.94 ATOM 996 N PHE A 139 76.061 23.166 120.058 1.00 30.10 ATOM 997 CA PHE A 139 75.479 24.397 120.573 1.00 29.61 ATOM 998 CB PHE A 139 73.959 24.294 120.685 1.00 29.86 ATOM 999 CG PHE A 139 73.291 23.992 119.402 1.00 30.42 ATOM 1000 CD1 PHE A 139 73.283 22.695 118.905 1.00 31.20 ATOM 1001 CD2 PHE A 139 72.712 25.009 118.659 1.00 31.75 ATOM 1002 CE1 PHE A 139 72.709 22.407 117.681 1.00 32.46 ATOM 1003 CE2 PHE A 139 72.133 24.739 117.427 1.00 33.50 ATOM 1004 CZ PHE A 139 72.132 23.430 116.934 1.00 33.41 ATOM 1005 C PHE A 139 76.021 24.709 121.946 1.00 29.99 ATOM 1006 O PHE A 139 76.456 23.822 122.678 1.00 29.92 ATOM 1007 N LEU A 140 75.978 25.987 122.293 1.00 29.55 ATOM 1008 CA LEU A 140 76.443 26.436 123.580 1.00 28.07 ATOM 1009 CB LEU A 140 77.649 27.357 123.415 1.00 25.38 ATOM 1010 CG LEU A 140 78.343 27.762 124.719 1.00 26.90 ATOM 1011 CD1 LEU A 140 79.389 26.707 125.117 1.00 23.01 ATOM 1012 CD2 LEU A 140 78.991 29.120 124.523 1.00 26.49 ATOM 1013 C LEU A 140 75.280 27.175 124.244 1.00 30.30 ATOM 1014 O LEU A 140 74.763 28.169 123.714 1.00 30.33 ATOM 1015 N PRO A 141 74.830 26.678 125.407 1.00 30.93 ATOM 1016 CD PRO A 141 75.130 25.361 125.992 1.00 29.93 ATOM 1017 CA PRO A 141 73.720 27.320 126.116 1.00 30.37 ATOM 1018 CB PRO A 141 73.354 26.292 127.188 1.00 29.43 ATOM 1019 CG PRO A 141 73.803 24.997 126.597 1.00 30.39 ATOM 1020 C PRO A 141 74.160 28.644 126.720 1.00 29.99 ATOM 1021 O PRO A 141 75.263 28.755 127.230 1.00 29.80 ATOM 1022 N MET A 142 73.296 29.645 126.654 1.00 31.55 ATOM 1023 CA MET A 142 73.605 30.949 127.215 1.00 33.42 ATOM 1024 CB MET A 142 74.054 31.913 126.121 1.00 34.28 ATOM 1025 CG MET A 142 75.418 31.603 125.534 1.00 35.59 ATOM 1026 SD MET A 142 75.795 32.644 124.108 1.00 36.91 ATOM 1027 CE MET A 142 76.070 34.233 124.865 1.00 37.00 ATOM 1028 C MET A 142 72.380 31.496 127.933 1.00 35.30 ATOM 1029 O MET A 142 71.343 31.769 127.325 1.00 33.50 ATOM 1030 N SER A 143 72.518 31.639 129.244 1.00 38.45 ATOM 1031 CA SER A 143 71.449 32.134 130.092 1.00 41.94 ATOM 1032 CB SER A 143 71.935 32.262 131.545 1.00 43.82 ATOM 1033 OG SER A 143 73.020 33.175 131.668 1.00 46.24 ATOM 1034 C SER A 143 70.892 33.462 129.605 1.00 43.77 ATOM 1035 O SER A 143 71.627 34.330 129.133 1.00 44.56 ATOM 1036 N ALA A 144 69.578 33.601 129.731 1.00 45.87 ATOM 1037 CA ALA A 144 68.872 34.797 129.304 1.00 47.92 ATOM 1038 CB ALA A 144 68.241 34.556 127.941 1.00 46.91 ATOM 1039 C ALA A 144 67.796 35.151 130.327 1.00 49.42 ATOM 1040 O ALA A 144 67.606 36.366 130.560 1.00 50.94 ATOM 1041 CB HIS B 16 101.445 8.523 141.693 1.00 53.58 ATOM 1042 CG HIS B 16 101.728 8.165 143.119 1.00 58.45 ATOM 1043 CD2 HIS B 16 101.794 6.964 143.742 1.00 60.61 ATOM 1044 ND1 HIS B 16 101.993 9.112 144.087 1.00 60.79 ATOM 1045 CE1 HIS B 16 102.207 8.509 145.243 1.00 61.84 ATOM 1046 NE2 HIS B 16 102.093 7.205 145.061 1.00 62.31 ATOM 1047 C HIS B 16 102.083 10.901 141.902 1.00 48.11 ATOM 1048 O HIS B 16 103.177 10.845 141.327 1.00 47.34 ATOM 1049 N HIS B 16 100.509 10.188 140.098 1.00 46.31 ATOM 1050 CA HIS B 16 100.953 9.958 141.508 1.00 49.06 ATOM 1051 N PHE B 17 101.816 11.731 142.910 1.00 47.00 ATOM 1052 CA PHE B 17 102.763 12.726 143.423 1.00 45.92 ATOM 1053 CB PHE B 17 102.107 13.493 144.587 1.00 45.44 ATOM 1054 CG PHE B 17 101.954 12.679 145.857 1.00 44.25 ATOM 1055 CD1 PHE B 17 102.968 12.657 146.815 1.00 43.19 ATOM 1056 CD2 PHE B 17 100.799 11.928 146.093 1.00 42.90 ATOM 1057 CE1 PHE B 17 102.833 11.898 147.985 1.00 41.41 ATOM 1058 CE2 PHE B 17 100.657 11.164 147.263 1.00 40.06 ATOM 1059 CZ PHE B 17 101.670 11.150 148.204 1.00 40.32 ATOM 1060 C PHE B 17 104.133 12.181 143.869 1.00 45.68 ATOM 1061 O PHE B 17 105.147 12.890 143.818 1.00 43.64 ATOM 1062 N LYS B 18 104.166 10.927 144.307 1.00 46.37 ATOM 1063 CA LYS B 18 105.415 10.325 144.772 1.00 47.59 ATOM 1064 CB LYS B 18 105.142 9.028 145.550 1.00 46.13 ATOM 1065 C LYS B 18 106.421 10.030 143.658 1.00 47.69 ATOM 1066 O LYS B 18 107.636 10.060 143.895 1.00 47.25 ATOM 1067 N ASP B 19 105.918 9.752 142.453 1.00 47.51 ATOM 1068 CA ASP B 19 106.774 9.416 141.311 1.00 46.25 ATOM 1069 CB ASP B 19 105.996 8.597 140.278 1.00 48.23 ATOM 1070 CG ASP B 19 105.414 7.315 140.862 1.00 51.06 ATOM 1071 OD1 ASP B 19 106.151 6.591 141.580 1.00 49.53 ATOM 1072 OD2 ASP B 19 104.220 7.034 140.592 1.00 50.69 ATOM 1073 C ASP B 19 107.375 10.622 140.624 1.00 44.83 ATOM 1074 O ASP B 19 106.895 11.745 140.781 1.00 47.81 ATOM 1075 N PRO B 20 108.439 10.407 139.838 1.00 42.28 ATOM 1076 CD PRO B 20 109.144 9.140 139.612 1.00 41.29 ATOM 1077 CA PRO B 20 109.106 11.496 139.124 1.00 39.23 ATOM 1078 CB PRO B 20 110.348 10.825 138.540 1.00 40.15 ATOM 1079 CG PRO B 20 110.550 9.624 139.424 1.00 41.97 ATOM 1080 C PRO B 20 108.204 12.019 138.037 1.00 35.93 ATOM 1081 O PRO B 20 107.371 11.291 137.511 1.00 35.62 ATOM 1082 N LYS B 21 108.381 13.281 137.695 1.00 34.38 ATOM 1083 C ALYS B 21 107.581 13.877 136.656 1.00 33.82 ATOM 1084 CB LYS B 21 106.633 14.890 137.290 1.00 32.42 ATOM 1085 CG LYS B 21 105.802 14.240 138.382 1.00 35.36 ATOM 1086 CD LYS B 21 104.698 15.135 138.905 1.00 38.67 ATOM 1087 CE LYS B 21 103.854 14.410 139.947 1.00 39.11 ATOM 1088 NZ LYS B 21 102.725 15.254 140.441 1.00 39.48 ATOM 1089 C LYS B 21 108.494 14.501 135.607 1.00 33.46 ATOM 1090 O LYS B 21 109.656 14.795 135.879 1.00 33.20 ATOM 1091 N ARG B 22 107.983 14.645 134.392 1.00 32.18 ATOM 1092 CA ARG B 22 108.751 15.249 133.318 1.00 32.62 ATOM 1093 CB ARG B 22 108.623 14.423 132.021 1.00 35.35 ATOM 1094 CG ARG B 22 109.685 13.336 131.798 1.00 39.07 ATOM 1095 CD ARG B 22 109.521 12.639 130.429 1.00 43.42 ATOM 1096 NE ARG B 22 108.763 11.383 130.484 1.00 48.74 ATOM 1097 CZ ARG B 22 109.266 10.207 130.871 1.00 51.40 ATOM 1098 NH1 ARG B 22 110.541 10.111 131.240 1.00 53.26 ATOM 1099 NH2 ARG B 22 108.494 9.121 130.895 1.00 51.66 ATOM 1100 C ARG B 22 108.111 16.606 133.117 1.00 31.88 ATOM 1101 O ARG B 22 106.899 16.699 133.019 1.00 32.34 ATOM 1102 N LEU B 23 108.901 17.666 133.068 1.00 31.50 ATOM 1103 CA LEU B 23 108.316 18.984 132.849 1.00 30.85 ATOM 1104 CB LEU B 23 108.953 19.997 133.809 1.00 29.80 ATOM 1105 CG LEU B 23 108.568 19.805 135.282 1.00 30.02 ATOM 1106 CD1 LEU B 23 109.288 20.822 136.157 1.00 29.71 ATOM 1107 CD2 LEU B 23 107.062 19.962 135.441 1.00 29.76 ATOM 1108 C LEU B 23 108.437 19.441 131.377 1.00 31.55 ATOM 1109 O LEU B 23 109.509 19.818 130.898 1.00 31.98 ATOM 1110 N TYR B 24 107.318 19.391 130.665 1.00 31.38 ATOM 1111 CA TYR B 24 107.257 19.768 129.258 1.00 30.32 ATOM 1112 CB TYR B 24 106.202 18.885 128.593 1.00 31.90 ATOM 1113 CG TYR B 24 105.930 19.160 127.140 1.00 34.51 ATOM 1114 CD1 TYR B 24 105.203 20.282 126.741 1.00 33.58 ATOM 1115 CE1 TYR B 24 104.898 20.489 125.402 1.00 33.99 ATOM 1116 CD2 TYR B 24 106.351 18.264 126.161 1.00 33.10 ATOM 1117 CE2 TYR B 24 106.054 18.469 124.828 1.00 31.74 ATOM 1118 CZ TYR B 24 105.327 19.572 124.454 1.00 32.06 ATOM 1119 OH TYR B 24 105.001 19.738 123.131 1.00 33.37 ATOM 1120 C TYR B 24 106.908 21.257 129.135 1.00 29.21 ATOM 1121 O TYR B 24 105.830 21.674 129.545 1.00 28.83 ATOM 1122 N CYS B 25 107.822 22.053 128.578 1.00 28.00 ATOM 1123 CA CYS B 25 107.592 23.492 128.430 1.00 28.66 ATOM 1124 CB CYS B 25 108.920 24.246 128.273 1.00 28.41 ATOM 1125 SG CYS B 25 108.778 26.080 128.299 1.00 24.31 ATOM 1126 C CYS B 25 106.703 23.807 127.238 1.00 30.84 ATOM 1127 O CYS B 25 106.941 23.303 126.136 1.00 33.28 ATOM 1128 N LYS B 26 105.685 24.644 127.449 1.00 30.59 ATOM 1129 CA LYS B 26 104.772 24.993 126.363 1.00 30.75 ATOM 1130 CB LYS B 26 103.642 25.911 126.833 1.00 30.15 ATOM 1131 CG LYS B 26 102.644 26.241 125.718 1.00 26.13 ATOM 1132 CD LYS B 26 101.597 27.212 126.165 1.00 23.86 ATOM 1133 CE LYS B 26 100.711 27.617 125.007 1.00 25.53 ATOM 1134 NZ LYS B 26 99.854 28.790 125.357 1.00 23.37 ATOM 1135 C LYS B 26 105.504 25.696 125.249 1.00 31.19 ATOM 1136 O LYS B 26 105.090 25.658 124.099 1.00 32.72 ATOM 1137 N ASN B 27 106.605 26.336 125.595 1.00 33.18 ATOM 1138 CA ASN B 27 107.368 27.073 124.618 1.00 34.32 ATOM 1139 CB ASN B 27 108.038 28.254 125.289 1.00 35.05 ATOM 1140 CG ASN B 27 108.694 29.154 124.301 1.00 37.69 ATOM 1141 OD1 ASN B 27 108.213 29.294 123.179 1.00 40.64 ATOM 1142 ND2 ASN B 27 109.791 29.789 124.702 1.00 39.91 ATOM 1143 C ASN B 27 108.413 26.258 123.871 1.00 36.01 ATOM 1144 O ASN B 27 109.604 26.318 124.188 1.00 36.60 ATOM 1145 N GLY B 28 107.960 25.497 122.876 1.00 36.54 ATOM 1146 CA GLY B 28 108.868 24.701 122.072 1.00 34.89 ATOM 1147 C GLY B 28 108.758 23.214 122.278 1.00 35.90 ATOM 1148 O GLY B 28 109.283 22.439 121.482 1.00 35.86 ATOM 1149 N GLY B 29 108.082 22.809 123.348 1.00 37.35 ATOM 1150 CA GLY B 29 107.933 21.392 123.627 1.00 37.23 ATOM 1151 C GLY B 29 109.202 20.823 124.223 1.00 37.28 ATOM 1152 O GLY B 29 109.479 19.625 124.094 1.00 38.96 ATOM 1153 N PHE B 30 109.982 21.694 124.860 1.00 36.18 ATOM 1154 CA PHE B 30 111.228 21.291 125.499 1.00 36.03 ATOM 1155 CB PHE B 30 112.224 22.458 125.569 1.00 35.91 ATOM 1156 CG PHE B 30 112.801 22.859 124.243 1.00 36.45 ATOM 1157 CD1 PHE B 30 112.337 23.996 123.583 1.00 34.88 ATOM 1158 CD2 PHE B 30 113.799 22.090 123.647 1.00 36.18 ATOM 1159 CE1 PHE B 30 112.846 24.363 122.353 1.00 34.85 ATOM 1160 CE2 PHE B 30 114.316 22.447 122.416 1.00 35.27 ATOM 1161 CZ PHE B 30 113.837 23.590 121.764 1.00 36.19 ATOM 1162 C PHE B 30 110.983 20.811 126.925 1.00 36.21 ATOM 1163 O PHE B 30 110.292 21.473 127.707 1.00 36.14 ATOM 1164 N PHE B 31 111.555 19.659 127.249 1.00 35.85 ATOM 1165 CA PHE B 31 111.469 19.097 128.589 1.00 37.40 ATOM 1166 CB PHE B 31 111.618 17.580 128.526 1.00 37.92 ATOM 1167 CG PHE B 31 110.402 16.878 128.027 1.00 40.04 ATOM 1168 CD1 PHE B 31 109.385 16.526 128.901 1.00 41.04 ATOM 1169 CD2 PHE B 31 110.281 16.543 126.684 1.00 41.32 ATOM 117O CE1 PHE B 31 108.260 15.838 128.446 1.00 42.85 ATOM 1171 CE2 PHE B 31 109.162 15.855 126.212 1.00 42.54 ATOM 1172 CZ PHE B 31 108.148 15.500 127.097 1.00 43.55 ATOM 1173 C PHE B 31 112.622 19.682 129.420 1.00 37.60 ATOM 1174 O PHE B 31 113.771 19.700 128.963 1.00 38.92 ATOM 1175 N LEU B 32 112.323 20.163 130.625 1.00 35.55 ATOM 1176 CA LEU B 32 113.355 20.716 131.488 1.00 34.17 ATOM 1177 CB LEU B 32 112.728 21.197 132.795 1.00 35.16 ATOM 1178 CG LEU B 32 113.638 21.861 133.832 1.00 36.30 ATOM 1179 CD1 LEU B 32 114.192 23.176 133.306 1.00 33.58 ATOM 1180 CD2 LEU B 32 112.832 22.093 135.097 1.00 36.73 ATOM 1181 C LEU B 32 114.384 19.619 131.774 1.00 33.55 ATOM 1182 O LEU B 32 114.026 18.501 132.172 1.00 30.47 ATOM 1183 N ARG B 33 115.658 19.936 131.556 1.00 32.82 ATOM 1184 CA ARG B 33 116.722 18.975 131.792 1.00 32.99 ATOM 1185 CB ARG B 33 117.387 18.584 130.483 1.00 32.91 ATOM 1186 CG ARG B 33 118.606 17.695 130.699 1.00 34.53 ATOM 1187 CD ARG B 33 119.161 17.186 129.381 1.00 34.21 ATOM 1188 NE ARG B 33 119.641 18.270 128.530 1.00 32.09 ATOM 1189 CZ ARG B 33 120.035 18.101 127.275 1.00 29.40 ATOM 1190 NH1 ARG B 33 120.002 16.894 126.734 1.00 26.60 ATOM 1191 NH2 ARG B 33 120.456 19.135 126.563 1.00 26.93 ATOM 1192 C ARG B 33 117.802 19.445 132.760 1.00 33.81 ATOM 1193 O ARG B 33 118.268 20.589 132.702 1.00 34.83 ATOM 1194 N ILE B 34 118.207 18.541 133.645 1.00 33.61 ATOM 1195 CA ILE B 34 119.243 18.835 134.624 1.00 34.06 ATOM 1196 CB ILE B 34 118.743 18.638 136.050 1.00 31.91 ATOM 1197 CG2 ILE B 34 119.898 18.733 137.023 1.00 31.52 ATOM 1198 CG1 ILE B 34 117.676 19.672 136.371 1.00 28.95 ATOM 1199 CD1 ILE B 34 117.027 19.425 137.693 1.00 28.65 ATOM 1200 C ILE B 34 120.408 17.884 134.412 1.00 36.60 ATOM 1201 O ILE B 34 120.322 16.702 134.770 1.00 36.08 ATOM 1202 N HIS B 35 121.485 18.413 133.828 1.00 38.97 ATOM 1203 CA HIS B 35 122.704 17.653 133.548 1.00 40.24 ATOM 1204 CB HIS B 35 123.634 18.480 132.656 1.00 42.94 ATOM 1205 CG HIS B 35 123.049 18.814 131.322 1.00 47.19 ATOM 1206 CD2 HIS B 35 122.371 19.906 130.892 1.00 48.47 ATOM 1207 ND1 HIS B 35 123.109 17.951 130.247 1.00 49.89 ATOM 1208 CE1 HIS B 35 122.495 18.499 129.212 1.00 50.03 ATOM 1209 NE2 HIS B 35 122.037 19.684 129.576 1.00 48.17 ATOM 1210 C HIS B 35 123.436 17.302 134.848 1.00 39.62 ATOM 1211 O HIS B 35 123.449 18.093 135.796 1.00 38.77 ATOM 1212 N PRO B 36 124.045 16.104 134.912 1.00 39.09 ATOM 1213 CD PRO B 36 123.867 14.947 134.014 1.00 39.98 ATOM 1214 CA PRO B 36 124.769 15.698 136.117 1.00 38.70 ATOM 1215 CB PRO B 36 125.303 14.324 135.746 1.00 37.90 ATOM 1216 CG PRO B 36 124.187 13.773 134.938 1.00 38.98 ATOM 1217 C PRO B 36 125.870 16.673 136.521 1.00 38.41 ATOM 1218 O PRO B 36 126.284 16.687 137.678 1.00 37.55 ATOM 1219 N ASP B 37 126.327 17.494 135.575 1.00 38.67 ATOM 1220 CA ASP B 37 127.367 18.476 135.866 1.00 39.47 ATOM 1221 CB ASP B 37 128.194 18.804 134.620 1.00 41.64 ATOM 1222 CG ASP B 37 127.404 19.576 133.574 1.00 44.39 ATOM 1223 OD1 ASP B 37 126.465 20.313 133.950 1.00 44.40 ATOM 1224 OD2 ASP B 37 127.734 19.458 132.370 1.00 45.65 ATOM 1225 C ASP B 37 126.796 19.783 136.409 1.00 40.37 ATOM 1226 O ASP B 37 127.542 20.745 136.601 1.00 41.14 ATOM 1227 N GLY B 38 125.482 19.836 136.629 1.00 40.30 ATOM 1228 CA GLY B 38 124.875 21.055 137.152 1.00 38.99 ATOM 1229 C GLY B 38 124.299 22.029 136.125 1.00 38.03 ATOM 1230 O GLY B 38 123.657 23.009 136.501 1.00 36.64 ATOM 1231 N ARG B 39 124.525 21.787 134.837 1.00 37.93 ATOM 1232 CA ARG B 39 123.969 22.666 133.809 1.00 39.37 ATOM 1233 CB ARG B 39 124.578 22.392 132.436 1.00 42.00 ATOM 1234 CG ARG B 39 126.018 22.802 132.223 1.00 46.71 ATOM 1235 CD ARG B 39 126.459 22.370 130.817 1.00 51.06 ATOM 1236 NE ARG B 39 126.320 20.921 130.634 1.00 54.86 ATOM 1237 CZ ARG B 39 125.992 20.323 129.487 1.00 56.96 ATOM 1238 NH1 ARG B 39 125.893 18.996 129.436 1.00 57.35 ATOM 1239 NH2 ARG B 39 125.751 21.044 128.395 1.00 56.77 ATOM 1240 C ARG B 39 122.470 22.413 133.680 1.00 39.42 ATOM 1241 O ARG B 39 121.997 21.295 133.899 1.00 38.02 ATOM 1242 N VAL B 40 121.733 23.452 133.298 1.00 40.07 ATOM 1243 CA VAL B 40 120.284 23.353 133.107 1.00 40.65 ATOM 1244 CB VAL B 40 119.526 24.162 134.182 1.00 41.39 ATOM 1245 CG1 VAL B 40 118.045 24.203 133.862 1.00 41.97 ATOM 1246 CG2 VAL B 40 119.738 23.525 135.545 1.00 42.94 ATOM 1247 C VAL B 40 119.876 23.848 131.713 1.00 40.44 ATOM 1248 O VAL B 40 120.300 24.921 131.274 1.00 41.16 ATOM 1249 N ASP B 41 119.056 23.064 131.018 1.00 39.94 ATOM 1250 CA ASP B 41 118.607 23.430 129.669 1.00 39.12 ATOM 1251 CB ASP B 41 119.706 23.118 128.659 1.00 39.83 ATOM 1252 CG ASP B 41 119.986 21.622 128.554 1.00 43.38 ATOM 1253 OD1 ASP B 41 120.942 21.243 127.844 1.00 45.53 ATOM 1254 OD2 ASP B 41 119.251 20.820 129.180 1.00 42.00 ATOM 1255 C ASP B 41 117.365 22.622 129.312 1.00 37.83 ATOM 1256 O ASP B 41 116.745 22.011 130.184 1.00 38.38 ATOM 1257 N GLY B 42 117.021 22.603 128.028 1.00 35.97 ATOM 1258 CA GLY B 42 115.860 21.849 127.590 1.00 35.38 ATOM 1259 C GLY B 42 116.124 20.881 126.446 1.00 35.25 ATOM 1260 O GLY B 42 117.119 21.001 125.742 1.00 37.44 ATOM 1261 N VAL B 43 115.233 19.912 126.268 1.00 33.57 ATOM 1262 CA VAL B 43 115.352 18.928 125.203 1.00 32.47 ATOM 1263 CB VAL B 43 116.279 17.752 125.573 1.00 30.78 ATOM 1264 CG1 VAL B 43 117.687 18.146 125.372 1.00 30.16 ATOM 1265 CG2 VAL B 43 116.049 17.324 127.008 1.00 30.59 ATOM 1266 C VAL B 43 113.997 18.340 124.899 1.00 33.51 ATOM 1267 O VAL B 43 113.227 18.032 125.810 1.00 34.09 ATOM 1268 N ARG B 44 113.720 18.162 123.615 1.00 33.46 ATOM 1269 CA ARG B 44 112.456 17.600 123.178 1.00 33.32 ATOM 1270 CB ARG B 44 112.217 17.925 121.711 1.00 32.91 ATOM 1271 CG ARG B 44 112.222 19.390 121.366 1.00 33.07 ATOM 1272 CD ARG B 44 111.099 19.639 120.384 1.00 34.99 ATOM 1273 NE ARG B 44 111.156 20.953 119.760 1.00 35.14 ATOM 1274 CZ ARG B 44 112.144 21.349 118.969 1.00 36.05 ATOM 1275 NH1 ARG B 44 113.166 20.523 118.714 1.00 36.18 ATOM 1276 NH2 ARG B 44 112.097 22.556 118.420 1.00 33.20 ATOM 1277 C ARG B 44 112.416 16.087 123.338 1.00 33.08 ATOM 1278 O ARG B 44 111.340 15.502 123.471 1.00 32.18 ATOM 1279 N GLU B 45 113.579 15.450 123.322 1.00 33.83 ATOM 1280 CA GLU B 45 113.611 13.994 123.424 1.00 36.58 ATOM 1281 CB GLU B 45 114.997 13.433 123.108 1.00 38.67 ATOM 1282 CG GLU B 45 115.037 11.900 123.234 1.00 41.88 ATOM 1283 CD GLU B 45 113.997 11.189 122.343 1.00 44.31 ATOM 1284 OE1 GLU B 45 114.080 11.341 121.102 1.00 42.64 ATOM 1285 OE2 GLU B 45 113.104 10.476 122.878 1.00 43.97 ATOM 1286 C GLU B 45 113.161 13.415 124.748 1.00 36.47 ATOM 1287 O GLU B 45 113.914 13.398 125.724 1.00 37.20 ATOM 1288 N LYS B 46 111.939 12.899 124.752 1.00 36.81 ATOM 1289 CA LYS B 46 111.332 12.304 125.935 1.00 37.99 ATOM 1290 CB LYS B 46 109.933 11.794 125.581 1.00 39.90 ATOM 1291 CG LYS B 46 109.087 11.317 126.752 1.00 43.95 ATOM 1292 CD LYS B 46 107.666 10.993 126.262 1.00 47.36 ATOM 1293 CE LYS B 46 106.787 10.333 127.338 1.00 48.53 ATOM 1294 NZ LYS B 46 106.393 8.920 126.999 1.00 47.10 ATOM 1295 C LYS B 46 112.159 11.175 126.553 1.00 37.61 ATOM 1296 O LYS B 46 112.018 10.874 127.736 1.00 38.77 ATOM 1297 N SER B 47 113.032 10.554 125.773 1.00 37.27 ATOM 1298 CA SER B 47 113.843 9.464 126.314 1.00 37.83 ATOM 1299 CB SER B 47 114.182 8.465 125.209 1.00 40.05 ATOM 1300 OG SER B 47 114.903 9.101 124.168 1.00 41.43 ATOM 1301 C SER B 47 115.137 9.953 126.971 1.00 37.29 ATOM 1302 O SER B 47 115.942 9.151 127.461 1.00 36.39 ATOM 1303 N ASP B 48 115.337 11.267 126.984 1.00 35.33 ATOM 1304 CA ASP B 48 116.536 11.807 127.588 1.00 34.88 ATOM 1305 CB ASP B 48 116.502 13.319 127.628 1.00 35.85 ATOM 1306 CG ASP B 48 117.822 13.882 128.042 1.00 37.14 ATOM 1307 OD1 ASP B 48 118.492 14.504 127.195 1.00 38.97 ATOM 1308 OD2 ASP B 48 118.203 13.669 129.212 1.00 38.89 ATOM 1309 C ASP B 48 116.675 11.275 129.005 1.00 34.83 ATOM 1310 O ASP B 48 115.711 11.244 129.771 1.00 34.62 ATOM 1311 N PRO B 49 117.890 10.875 129.388 1.00 34.68 ATOM 1312 CD PRO B 49 119.175 11.093 128.695 1.00 35.21 ATOM 1313 CA PRO B 49 118.114 10.336 130.730 1.00 34.34 ATOM 1314 CB PRO B 49 119.507 9.758 130.624 1.00 34.29 ATOM 1315 CG PRO B 49 120.194 10.836 129.798 1.00 35.75 ATOM 1316 C PRO B 49 118.026 11.340 131.869 1.00 34.60 ATOM 1317 O PRO B 49 117.728 10.969 133.004 1.00 34.68 ATOM 1318 N HIS B 50 118.274 12.611 131.569 1.00 34.99 ATOM 1319 CA HIS B 50 118.281 13.640 132.605 1.00 35.11 ATOM 1320 CB HIS B 50 119.514 14.516 132.433 1.00 38.33 ATOM 1321 CG HIS B 50 120.771 13.732 132.248 1.00 39.99 ATOM 1322 CD2 HIS B 50 121.628 13.656 131.205 1.00 40.25 ATOM 1323 ND1 HIS B 50 121.224 12.830 133.186 1.00 40.36 ATOM 1324 CE1 HIS B 50 122.304 12.228 132.725 1.00 41.16 ATOM 1325 NE2 HIS B 50 122.569 12.711 131.525 1.00 41.80 ATOM 1326 C HIS B 50 117.064 14.529 132.695 1.00 33.22 ATOM 1327 O HIS B 50 117.154 15.649 133.191 1.00 32.87 ATOM 1328 N ILE B 51 115.921 14.046 132.237 1.00 31.67 ATOM 1329 CA ILE B 51 114.726 14.867 132.302 1.00 29.82 ATOM 1330 CB ILE B 51 113.988 14.899 130.938 1.00 27.56 ATOM 1331 CG2 ILE B 51 114.947 15.389 129.861 1.00 27.80 ATOM 1332 CG1 ILE B 51 113.427 13.520 130.591 1.00 23.56 ATOM 1333 CD1 ILE B 51 112.630 13.498 129.324 1.00 19.14 ATOM 1334 C ILE B 51 113.744 14.454 133.387 1.00 29.57 ATOM 1335 O ILE B 51 112.771 15.156 133.625 1.00 29.45 ATOM 1336 N LYS B 52 113.998 13.324 134.043 1.00 30.99 ATOM 1337 CA LYS B 52 113.119 12.857 135.114 1.00 32.77 ATOM 1338 CB LYS B 52 113.319 11.364 135.377 1.00 35.63 ATOM 1339 CG LYS B 52 112.769 10.497 134.265 1.00 40.57 ATOM 1340 CD LYS B 52 112.534 9.059 134.718 1.00 43.44 ATOM 1341 CE LYS B 52 111.798 8.274 133.625 1.00 44.57 ATOM 1342 NZ LYS B 52 111.173 7.015 134.138 1.00 46.19 ATOM 1343 C LYS B 52 113.387 13.651 136.386 1.00 31.74 ATOM 1344 O LYS B 52 114.458 13.540 136.990 1.00 30.75 ATOM 1345 N LEU B 53 112.389 14.443 136.776 1.00 30.81 ATOM 1346 CA LEU B 53 112.450 15.321 137.941 1.00 28.75 ATOM 1347 CB LEU B 53 111.893 16.689 137.561 1.00 26.09 ATOM 1348 CG LEU B 53 112.283 17.154 136.159 1.00 23.54 ATOM 1349 CD1 LEU B 53 111.568 18.436 135.788 1.00 21.62 ATOM 135O CD2 LEU B 53 113.780 17.343 136.124 1.00 22.95 ATOM 1351 C LEU B 53 111.656 14.791 139.123 1.00 28.90 ATOM 1352 O LEU B 53 110.652 14.108 138.960 1.00 29.34 ATOM 1353 N GLN B 54 112.116 15.114 140.323 1.00 29.74 ATOM 1354 CA GLN B 54 111.426 14.695 141.530 1.00 28.75 ATOM 1355 CB GLN B 54 112.362 13.864 142.403 1.00 26.78 ATOM 1356 CG GLN B 54 111.667 13.080 143.490 1.00 28.67 ATOM 1357 CD GLN B 54 110.638 12.088 142.956 1.00 30.79 ATOM 1358 OE1 GLN B 54 110.960 11.197 142.163 1.00 33.61 ATOM 1359 NE2 GLN B 54 109.396 12.235 143.398 1.00 30.23 ATOM 1360 C GLN B 54 111.025 15.986 142.234 1.00 28.64 ATOM 1361 O GLN B 54 111.854 16.671 142.816 1.00 29.72 ATOM 1362 N LEU B 55 109.752 16.340 142.132 1.00 28.94 ATOM 1363 CA LEU B 55 109.270 17.554 142.759 1.00 27.80 ATOM 1364 CB LEU B 55 108.072 18.148 142.006 1.00 27.78 ATOM 1365 CG LEU B 55 108.160 18.507 140.514 1.00 26.52 ATOM 1366 CD1 LEU B 55 109.194 19.576 140.274 1.00 27.66 ATOM 1367 CD2 LEU B 55 108.480 17.267 139.724 1.00 27.39 ATOM 1368 C LEU B 55 108.863 17.173 144.167 1.00 27.87 ATOM 1369 O LEU B 55 108.118 16.210 144.389 1.00 27.58 ATOM 1370 N GLN B 56 109.394 17.925 145.119 1.00 27.07 ATOM 1371 CA GLN B 56 109.115 17.699 146.519 1.00 26.11 ATOM 1372 CB GLN B 56 110.390 17.269 147.244 1.00 25.15 ATOM 1373 CG GLN B 56 110.220 17.014 148.719 1.00 20.80 ATOM 1374 CD GLN B 56 109.326 15.828 149.010 1.00 23.03 ATOM 1375 OE1 GLN B 56 109.585 14.707 148.564 1.00 21.86 ATOM 1376 NE2 GLN B 56 108.265 16.067 149.771 1.00 24.69 ATOM 1377 C GLN B 56 108.601 18.997 147.114 1.00 27.37 ATOM 1378 O GLN B 56 109.140 20.076 146.863 1.00 26.42 ATOM 1379 N ALA B 57 107.545 18.891 147.902 1.00 27.79 ATOM 1380 CA ALA B 57 106.985 20.068 148.521 1.00 27.74 ATOM 1381 CB ALA B 57 105.495 19.869 148.763 1.00 27.74 ATOM 1382 C ALA B 57 107.705 20.310 149.833 1.00 28.44 ATOM 1383 O ALA B 57 107.961 19.372 150.593 1.00 26.26 ATOM 1384 N GLU B 58 108.042 21.572 150.087 1.00 30.24 ATOM 1385 CA GLU B 58 108.710 21.951 151.328 1.00 31.94 ATOM 1386 CB GLU B 58 109.725 23.073 151.089 1.00 32.06 ATOM 1387 CG GLU B 58 110.875 23.099 152.094 1.00 32.70 ATOM 1388 CD GLU B 58 111.582 21.747 152.219 1.00 35.13 ATOM 1389 OE1 GLU B 58 111.629 20.999 151.210 1.00 37.39 ATOM 1390 OE2 GLU B 58 112.104 21.436 153.319 1.00 34.15 ATOM 1391 C GLU B 58 107.614 22.433 152.255 1.00 32.23 ATOM 1392 O GLU B 58 107.745 22.371 153.471 1.00 33.09 ATOM 1393 N GLU B 59 106.531 22.903 151.643 1.00 32.83 ATOM 1394 CA GLU B 59 105.347 23.391 152.336 1.00 32.73 ATOM 1395 CB GLU B 59 105.676 24.642 153.137 1.00 34.19 ATOM 1396 CG GLU B 59 106.362 25.734 152.354 1.00 37.42 ATOM 1397 CD GLU B 59 106.419 27.017 153.160 1.00 41.98 ATOM 1398 OE1 GLU B 59 106.713 26.920 154.376 1.00 43.49 ATOM 1399 OE2 GLU B 59 106.175 28.109 152.594 1.00 42.36 ATOM 1400 C GLU B 59 104.294 23.697 151.275 1.00 31.75 ATOM 1401 O GLU B 59 104.594 23.657 150.086 1.00 30.10 ATOM 1402 N ARG B 60 103.070 24.007 151.689 1.00 31.28 ATOM 1403 CA ARG B 60 102.009 24.291 150.722 1.00 32.14 ATOM 1404 CB ARG B 60 100.765 24.866 151.402 1.00 31.64 ATOM 1405 CG ARG B 60 99.878 23.830 152.044 1.00 36.28 ATOM 1406 CD ARG B 60 98.689 24.483 152.722 1.00 39.82 ATOM 1407 NE ARG B 60 97.848 25.183 151.756 1.00 44.52 ATOM 1408 CZ ARG B 60 96.775 25.901 152.076 1.00 44.93 ATOM 1409 NH1 ARG B 60 96.409 26.017 153.349 1.00 44.87 ATOM 1410 NH2 ARG B 60 96.066 26.499 151.121 1.00 44.99 ATOM 1411 C ARG B 60 102.426 25.228 149.604 1.00 30.88 ATOM 1412 O ARG B 60 102.863 26.347 149.856 1.00 30.20 ATOM 1413 N GLY B 61 102.279 24.754 148.368 1.00 29.53 ATOM 1414 CA GLY B 61 102.623 25.558 147.209 1.00 28.37 ATOM 1415 C GLY B 61 104.097 25.855 146.951 1.00 26.54 ATOM 1416 O GLY B 61 104.413 26.716 146.125 1.00 25.85 ATOM 1417 N VAL B 62 104.994 25.154 147.642 1.00 23.72 ATOM 1418 CA VAL B 62 106.428 25.364 147.463 1.00 21.76 ATOM 1419 CB VAL B 62 107.067 26.030 148.710 1.00 18.92 ATOM 1420 CG1 VAL B 62 108.589 25.949 148.630 1.00 18.20 ATOM 1421 CG2 VAL B 62 106.637 27.468 148.811 1.00 14.47 ATOM 1422 C VAL B 62 107.132 24.036 147.206 1.00 22.30 ATOM 1423 O VAL B 62 106.994 23.093 147.982 1.00 22.35 ATOM 1424 N VAL B 63 107.899 23.972 146.125 1.00 21.78 ATOM 1425 CA VAL B 63 108.599 22.750 145.787 1.00 23.21 ATOM 1426 CB VAL B 63 107.937 22.058 144.578 1.00 21.42 ATOM 1427 CG1 VAL B 63 106.487 21.831 144.850 1.00 20.97 ATOM 1428 CG2 VAL B 63 108.106 22.900 143.338 1.00 19.19 ATOM 1429 C VAL B 63 110.067 22.963 145.440 1.00 25.78 ATOM 1430 O VAL B 63 110.484 24.060 145.071 1.00 28.04 ATOM 1431 N SER B 64 110.842 21.894 145.577 1.00 26.96 ATOM 1432 CA SER B 64 112.253 21.905 145.214 1.00 27.58 ATOM 1433 CB SER B 64 113.153 21.333 146.323 1.00 26.89 ATOM 1434 OG SER B 64 113.006 19.927 146.434 1.00 27.20 ATOM 1435 C SER B 64 112.197 20.941 144.048 1.00 27.27 ATOM 1436 O SER B 64 111.467 19.956 144.090 1.00 27.77 ATOM 1437 N ILE B 65 112.943 21.239 143.000 1.00 27.86 ATOM 1438 CA ILE B 65 112.954 20.399 141.820 1.00 26.92 ATOM 1439 CB ILE B 65 112.755 21.274 140.552 1.00 26.65 ATOM 1440 CG2 ILE B 65 112.860 20.409 139.280 1.00 26.91 ATOM 1441 CG1 ILE B 65 111.390 21.982 140.646 1.00 24.20 ATOM 1442 CD1 ILE B 65 111.158 23.103 139.653 1.00 21.27 ATOM 1443 C ILE B 65 114.284 19.663 141.781 1.00 27.92 ATOM 1444 O ILE B 65 115.338 20.279 141.604 1.00 29.68 ATOM 1445 N LYS B 66 114.235 18.349 141.975 1.00 27.70 ATOM 1446 CA LYS B 66 115.443 17.536 141.974 1.00 27.93 ATOM 1447 CB LYS B 66 115.433 16.571 143.141 1.00 28.47 ATOM 1448 CG LYS B 66 116.602 15.613 143.107 1.00 28.99 ATOM 1449 CD LYS B 66 116.637 14.760 144.353 1.00 31.91 ATOM 1450 CE LYS B 66 118.065 14.652 144.880 1.00 34.91 ATOM 1451 NZ LYS B 66 118.119 13.913 146.175 1.00 37.70 ATOM 1452 C LYS B 66 115.621 16.709 140.717 1.00 29.46 ATOM 1453 O LYS B 66 114.724 15.950 140.354 1.00 29.47 ATOM 1454 N GLY B 67 116.777 16.847 140.064 1.00 29.55 ATOM 1455 CA GLY B 67 117.058 16.059 138.877 1.00 29.40 ATOM 1456 C GLY B 67 117.436 14.674 139.374 1.00 30.54 ATOM 1457 O GLY B 67 118.471 14.506 140.019 1.00 31.69 ATOM 1458 N VAL B 68 116.600 13.680 139.097 1.00 30.20 ATOM 1459 CA VAL B 68 116.861 12.328 139.577 1.00 31.28 ATOM 146O CB VAL B 68 115.708 11.363 139.188 1.00 29.45 ATOM 1461 CG1 VAL B 68 116.075 9.937 139.551 1.00 24.11 ATOM 1462 CG2 VAL B 68 114.424 11.768 139.911 1.00 26.34 ATOM 1463 C VAL B 68 118.184 11.744 139.110 1.00 33.38 ATOM 1464 O VAL B 68 118.915 11.157 139.899 1.00 33.82 ATOM 1465 N SER B 69 118.494 11.893 137.830 1.00 36.86 ATOM 1466 CA SER B 69 119.744 11.352 137.317 1.00 38.82 ATOM 1467 CB SER B 69 119.751 11.387 135.792 1.00 40.75 ATOM 1468 OG SER B 69 120.967 10.861 135.293 1.00 42.57 ATOM 1469 C SER B 69 120.941 12.137 137.867 1.00 39.71 ATOM 1470 O SER B 69 121.865 11.550 138.434 1.00 40.03 ATOM 1471 N ALA B 70 120.911 13.459 137.717 1.00 39.07 ATOM 1472 CA ALA B 70 121.998 14.316 138.187 1.00 38.97 ATOM 1473 CB ALA B 70 121.841 15.714 137.608 1.00 37.82 ATOM 1474 C ALA B 70 122.102 14.422 139.702 1.00 39.68 ATOM 1475 O ALA B 70 123.134 14.840 140.231 1.00 40.63 ATOM 1476 N ASN B 71 121.041 14.044 140.401 1.00 40.19 ATOM 1477 CA ASN B 71 121.007 14.161 141.854 1.00 40.46 ATOM 1478 CB ASN B 71 121.953 13.170 142.516 1.00 40.79 ATOM 1479 CG ASN B 71 121.742 13.090 144.016 1.00 40.60 ATOM 1480 OD1 ASN B 71 120.735 12.562 144.486 1.00 41.57 ATOM 1481 ND2 ASN B 71 122.683 13.630 144.775 1.00 41.54 ATOM 1482 C ASN B 71 121.398 15.584 142.270 1.00 40.88 ATOM 1483 O ASN B 71 122.240 15.780 143.154 1.00 41.28 ATOM 1484 N ARG B 72 120.788 16.567 141.611 1.00 40.64 ATOM 1485 CA ARG B 72 121.036 17.980 141.891 1.00 40.55 ATOM 1486 CB ARG B 72 121.898 18.600 140.793 1.00 41.41 ATOM 1487 CG ARG B 72 123.366 18.189 140.786 1.00 42.06 ATOM 1488 CD ARG B 72 124.021 18.715 139.515 1.00 43.85 ATOM 1489 NE ARG B 72 125.474 18.584 139.511 1.00 44.83 ATOM 1490 CZ ARG B 72 126.299 19.341 140.226 1.00 42.83 ATOM 1491 NH1 ARG B 72 125.819 20.294 141.013 1.00 42.08 ATOM 1492 NH2 ARG B 72 127.606 19.137 140.154 1.00 41.81 ATOM 1493 C ARG B 72 119.704 18.716 141.946 1.00 40.00 ATOM 1494 O ARG B 72 118.725 18.279 141.350 1.00 40.69 ATOM 1495 N TYR B 73 119.678 19.841 142.650 1.00 39.69 ATOM 1496 CA TYR B 73 118.462 20.629 142.784 1.00 38.01 ATOM 1497 CB TYR B 73 118.266 21.040 144.239 1.00 37.74 ATOM 1498 CG TYR B 73 118.162 19.861 145.156 1.00 38.72 ATOM 1499 CD1 TYR B 73 119.296 19.134 145.518 1.00 38.86 ATOM 150O CE1 TYR B 73 119.198 18.006 146.319 1.00 39.71 ATOM 1501 CD2 TYR B 73 116.923 19.433 145.624 1.00 39.11 ATOM 1502 CE2 TYR B 73 116.810 18.306 146.430 1.00 39.71 ATOM 1503 CZ TYR B 73 117.948 17.596 146.771 1.00 40.56 ATOM 1504 OH TYR B 73 117.831 16.467 147.548 1.00 42.94 ATOM 1505 C TYR B 73 118.489 21.872 141.920 1.00 37.16 ATOM 1506 O TYR B 73 119.464 22.620 141.928 1.00 36.61 ATOM 1507 N LEU B 74 117.411 22.098 141.177 1.00 35.71 ATOM 1508 CA LEU B 74 117.324 23.283 140.332 1.00 35.01 ATOM 1509 CB LEU B 74 116.031 23.268 139.519 1.00 35.05 ATOM 1510 CG LEU B 74 115.822 24.514 138.649 1.00 37.90 ATOM 1511 CD1 LEU B 74 116.901 24.617 137.565 1.00 37.05 ATOM 1512 CD2 LEU B 74 114.441 24.456 138.020 1.00 37.87 ATOM 1513 C LEU B 74 117.368 24.537 141.203 1.00 34.61 ATOM 1514 O LEU B 74 116.637 24.650 142.188 1.00 33.92 ATOM 1515 N ALA B 75 118.240 25.472 140.847 1.00 34.97 ATOM 1516 CA ALA B 75 118.367 26.704 141.610 1.00 36.06 ATOM 1517 CB ALA B 75 119.599 26.647 142.493 1.00 33.12 ATOM 1518 C ALA B 75 118.410 27.955 140.741 1.00 36.98 ATOM 1519 O ALA B 75 118.963 27.959 139.643 1.00 36.77 ATOM 1520 N MET B 76 117.800 29.014 141.252 1.00 39.19 ATOM 1521 CA MET B 76 117.756 30.296 140.576 1.00 42.08 ATOM 1522 CB MET B 76 116.372 30.928 140.715 1.00 42.36 ATOM 1523 CG MET B 76 116.301 32.378 140.264 1.00 41.46 ATOM 1524 SD MET B 76 115.478 32.588 138.680 1.00 43.04 ATOM 1525 CE MET B 76 113.881 33.019 139.188 1.00 40.48 ATOM 1526 C MET B 76 118.771 31.160 141.291 1.00 45.25 ATOM 1527 O MET B 76 118.787 31.217 142.523 1.00 44.89 ATOM 1528 N LYS B 77 119.619 31.831 140.521 1.00 48.52 ATOM 1529 CA LYS B 77 120.639 32.695 141.097 1.00 52.31 ATOM 153O CB LYS B 77 121.934 32.641 140.280 1.00 53.30 ATOM 1531 CG LYS B 77 122.496 31.239 140.049 1.00 56.11 ATOM 1532 CD LYS B 77 122.588 30.435 141.334 1.00 58.28 ATOM 1533 CE LYS B 77 123.405 31.153 142.391 1.00 59.93 ATOM 1534 NZ LYS B 77 123.562 30.287 143.589 1.00 62.93 ATOM 1535 C LYS B 77 120.158 34.135 141.161 1.00 54.00 ATOM 1536 O LYS B 77 119.186 34.510 140.505 1.00 53.67 ATOM 1537 N GLU B 78 120.865 34.937 141.950 1.00 56.33 ATOM 1538 CA GLU B 78 120.542 36.344 142.137 1.00 58.25 ATOM 1539 CB GLU B 78 121.662 37.045 142.912 1.00 61.62 ATOM 1540 CG GLU B 78 122.843 37.464 142.034 1.00 67.26 ATOM 1541 CD GLU B 78 123.925 38.221 142.798 1.00 70.03 ATOM 1542 OE1 GLU B 78 123.568 39.077 143.639 1.00 69.74 ATOM 1543 OE2 GLU B 78 125.132 37.969 142.546 1.00 71.37 ATOM 1544 C GLU B 78 120.319 37.093 140.827 1.00 57.71 ATOM 1545 O GLU B 78 119.465 37.974 140.757 1.00 58.26 ATOM 1546 N ASP B 79 121.092 36.757 139.797 1.00 56.53 ATOM 1547 CA ASP B 79 120.966 37.431 138.510 1.00 54.63 ATOM 1548 CB ASP B 79 122.319 37.464 137.798 1.00 52.84 ATOM 1549 CG ASP B 79 122.815 36.092 137.430 1.00 51.45 ATOM 1550 OD1 ASP B 79 123.915 35.997 136.854 1.00 51.83 ATOM 1551 OD2 ASP B 79 122.107 35.105 137.714 1.00 51.29 ATOM 1552 C ASP B 79 119.916 36.780 137.611 1.00 54.78 ATOM 1553 O ASP B 79 119.636 37.264 136.506 1.00 55.45 ATOM 1554 N GLY B 80 119.344 35.677 138.084 1.00 53.84 ATOM 1555 CA GLY B 80 118.320 34.996 137.315 1.00 51.77 ATOM 1556 C GLY B 80 118.778 33.857 136.426 1.00 50.03 ATOM 1557 O GLY B 80 118.055 33.464 135.515 1.00 49.68 ATOM 1558 N ARG B 81 119.966 33.320 136.669 1.00 48.16 ATOM 1559 CA ARG B 81 120.433 32.214 135.850 1.00 48.37 ATOM 1560 CB ARG B 81 121.935 32.331 135.589 1.00 51.00 ATOM 1561 CG ARG B 81 122.780 32.353 136.833 1.00 56.56 ATOM 1562 CD ARG B 81 124.245 32.646 136.531 1.00 60.32 ATOM 1563 NE ARG B 81 125.073 32.401 137.714 1.00 66.82 ATOM 1564 CZ ARG B 81 125.085 33.162 138.811 1.00 68.79 ATOM 1565 NH1 ARG B 81 124.320 34.243 138.895 1.00 69.57 ATOM 1566 NH2 ARG B 81 125.848 32.822 139.846 1.00 69.73 ATOM 1567 C ARG B 81 120.113 30.917 136.563 1.00 46.60 ATOM 1568 O ARG B 81 120.075 30.867 137.786 1.00 47.16 ATOM 1569 N LEU B 82 119.866 29.870 135.793 1.00 45.60 ATOM 1570 CA LEU B 82 119.536 28.572 136.361 1.00 45.32 ATOM 1571 CB LEU B 82 118.471 27.885 135.504 1.00 44.81 ATOM 1572 CG LEU B 82 117.161 28.639 135.289 1.00 43.76 ATOM 1573 CD1 LEU B 82 116.270 27.844 134.357 1.00 43.35 ATOM 1574 CD2 LEU B 82 116.475 28.865 136.623 1.00 42.51 ATOM 1575 C LEU B 82 120.747 27.659 136.432 1.00 44.48 ATOM 1576 O LEU B 82 121.666 27.784 135.638 1.00 44.80 ATOM 1577 N LEU B 83 120.732 26.747 137.394 1.00 44.12 ATOM 1578 CA LEU B 83 121.787 25.759 137.555 1.00 43.94 ATOM 1579 CB LEU B 83 123.105 26.406 137.989 1.00 44.49 ATOM 1580 CG LEU B 83 123.219 27.253 139.250 1.00 47.44 ATOM 1581 CD1 LEU B 83 123.023 26.367 140.485 1.00 47.58 ATOM 1582 CD2 LEU B 83 124.606 27.928 139.272 1.00 45.96 ATOM 1583 C LEU B 83 121.276 24.759 138.572 1.00 43.94 ATOM 1584 O LEU B 83 120.284 25.024 139.252 1.00 43.82 ATOM 1585 N ALA B 84 121.919 23.603 138.658 1.00 44.85 ATOM 1586 CA ALA B 84 121.466 22.577 139.589 1.00 46.61 ATOM 1587 CB ALA B 84 121.174 21.274 138.841 1.00 46.16 ATOM 1588 C ALA B 84 122.495 22.346 140.674 1.00 46.94 ATOM 1589 O ALA B 84 123.552 21.774 140.424 1.00 48.51 ATOM 1590 N SER B 85 122.166 22.806 141.878 1.00 47.21 ATOM 1591 CA SER B 85 123.029 22.689 143.040 1.00 46.19 ATOM 1592 CB SER B 85 122.485 23.579 144.153 1.00 45.16 ATOM 1593 OG SER B 85 123.154 23.322 145.364 1.00 48.28 ATOM 1594 C SER B 85 123.172 21.246 143.525 1.00 46.62 ATOM 1595 O SER B 85 122.293 20.411 143.310 1.00 46.65 ATOM 1596 N LYS B 86 124.295 20.952 144.171 1.00 47.71 ATOM 1597 CA LYS B 86 124.548 19.605 144.675 1.00 47.68 ATOM 1598 CB LYS B 86 126.028 19.438 145.025 1.00 49.80 ATOM 1599 CG LYS B 86 126.566 18.033 144.786 1.00 53.25 ATOM 1600 CD LYS B 86 126.384 17.633 143.330 1.00 56.56 ATOM 1601 CE LYS B 86 127.312 16.493 142.943 1.00 60.15 ATOM 1602 NZ LYS B 86 127.290 16.233 141.465 1.00 62.57 ATOM 1603 C LYS B 86 123.695 19.359 145.908 1.00 45.92 ATOM 1604 O LYS B 86 123.088 18.302 146.060 1.00 45.78 ATOM 1605 N SER B 87 123.663 20.345 146.794 1.00 44.95 ATOM 1606 CA SER B 87 122.859 20.251 148.004 1.00 44.18 ATOM 1607 CB SER B 87 123.744 20.317 149.253 1.00 44.78 ATOM 1608 OG SER B 87 124.591 21.449 149.210 1.00 45.74 ATOM 1609 C SER B 87 121.847 21.394 148.010 1.00 42.91 ATOM 1610 O SER B 87 122.017 22.403 147.324 1.00 41.78 ATOM 1611 N VAL B 88 120.789 21.220 148.785 1.00 40.56 ATOM 1612 CA VAL B 88 119.733 22.207 148.881 1.00 38.85 ATOM 1613 CB VAL B 88 118.567 21.602 149.674 1.00 37.72 ATOM 1614 CG1 VAL B 88 117.461 22.626 149.871 1.00 38.20 ATOM 1615 CG2 VAL B 88 118.059 20.377 148.960 1.00 35.37 ATOM 1616 C VAL B 88 120.150 23.536 149.534 1.00 39.23 ATOM 1617 O VAL B 88 120.736 23.553 150.620 1.00 39.42 ATOM 1618 N THR B 89 119.845 24.642 148.857 1.00 38.16 ATOM 1619 CA THR B 89 120.125 25.980 149.365 1.00 38.00 ATOM 1620 CB THR B 89 121.119 26.779 148.452 1.00 38.35 ATOM 1621 OG1 THR B 89 120.462 27.238 147.262 1.00 36.90 ATOM 1622 CG2 THR B 89 122.278 25.903 148.059 1.00 37.82 ATOM 1623 C THR B 89 118.776 26.685 149.378 1.00 38.23 ATOM 1624 O THR B 89 117.757 26.067 149.092 1.00 38.55 ATOM 1625 N ASP B 90 118.767 27.974 149.689 1.00 39.48 ATOM 1626 CA ASP B 90 117.531 28.747 149.751 1.00 40.53 ATOM 1627 CB ASP B 90 117.766 29.980 150.619 1.00 45.07 ATOM 1628 CG ASP B 90 118.708 30.983 149.963 1.00 49.28 ATOM 1629 OD1 ASP B 90 119.724 30.564 149.352 1.00 51.36 ATOM 1630 OD2 ASP B 90 118.432 32.198 150.066 1.00 50.64 ATOM 1631 C ASP B 90 117.020 29.184 148.378 1.00 39.14 ATOM 1632 O ASP B 90 115.947 29.777 148.263 1.00 39.83 ATOM 1633 N GLU B 91 117.794 28.908 147.339 1.00 37.50 ATOM 1634 CA GLU B 91 117.396 29.283 145.989 1.00 36.18 ATOM 1635 CB GLU B 91 118.600 29.828 145.214 1.00 34.46 ATOM 1636 CG GLU B 91 119.385 30.900 145.952 1.00 35.83 ATOM 1637 CD GLU B 91 120.581 31.430 145.146 1.00 37.27 ATOM 1638 OE1 GLU B 91 121.449 30.619 144.757 1.00 37.05 ATOM 1639 OE2 GLU B 91 120.655 32.657 144.902 1.00 36.08 ATOM 1640 C GLU B 91 116.815 28.066 145.263 1.00 34.93 ATOM 1641 O GLU B 91 116.515 28.121 144.070 1.00 32.42 ATOM 1642 N CYS B 92 116.648 26.973 145.998 1.00 33.43 ATOM 1643 CA CYS B 92 116.133 25.753 145.410 1.00 33.96 ATOM 1644 CB CYS B 92 116.918 24.558 145.956 1.00 33.84 ATOM 1645 SG CYS B 92 118.642 24.511 145.386 1.00 31.04 ATOM 1646 C CYS B 92 114.634 25.545 145.604 1.00 33.90 ATOM 1647 O CYS B 92 114.114 24.447 145.378 1.00 34.76 ATOM 1648 N PHE B 93 113.934 26.604 145.993 1.00 32.95 ATOM 1649 CA PHE B 93 112.495 26.513 146.204 1.00 31.87 ATOM 1650 CB PHE B 93 112.182 26.819 147.659 1.00 31.02 ATOM 1651 CG PHE B 93 112.813 25.853 148.604 1.00 31.34 ATOM 1652 CD1 PHE B 93 112.373 24.532 148.660 1.00 32.18 ATOM 1653 CD2 PHE B 93 113.882 26.235 149.401 1.00 30.66 ATOM 1654 CE1 PHE B 93 112.996 23.606 149.502 1.00 29.81 ATOM 1655 CE2 PHE B 93 114.508 25.318 150.242 1.00 29.19 ATOM 1656 CZ PHE B 93 114.061 24.001 150.289 1.00 29.42 ATOM 1657 C PHE B 93 111.692 27.409 145.266 1.00 31.34 ATOM 1658 O PHE B 93 112.080 28.542 144.967 1.00 31.56 ATOM 1659 N PHE B 94 110.564 26.886 144.798 1.00 29.36 ATOM 1660 CA PHE B 94 109.731 27.621 143.860 1.00 26.56 ATOM 1661 CB PHE B 94 109.992 27.093 142.452 1.00 25.63 ATOM 1662 CG PHE B 94 111.426 27.126 142.071 1.00 24.51 ATOM 1663 CD1 PHE B 94 112.004 28.299 141.607 1.00 25.06 ATOM 1664 CD2 PHE B 94 112.220 26.000 142.243 1.00 25.56 ATOM 1665 CE1 PHE B 94 113.356 28.356 141.321 1.00 25.77 ATOM 1666 CE2 PHE B 94 113.574 26.039 141.962 1.00 25.63 ATOM 1667 CZ PHE B 94 114.148 27.219 141.499 1.00 25.73 ATOM 1668 C PHE B 94 108.255 27.503 144.175 1.00 25.19 ATOM 1669 O PHE B 94 107.820 26.531 144.803 1.00 23.94 ATOM 1670 N PHE B 95 107.493 28.502 143.742 1.00 22.53 ATOM 1671 CA PHE B 95 106.055 28.485 143.944 1.00 23.75 ATOM 1672 CB PHE B 95 105.469 29.894 143.954 1.00 21.99 ATOM 1673 CG PHE B 95 105.775 30.663 145.196 1.00 22.80 ATOM 1674 CD1 PHE B 95 106.414 31.901 145.120 1.00 22.56 ATOM 1675 CD2 PHE B 95 105.441 30.144 146.448 1.00 21.37 ATOM 1676 CE1 PHE B 95 106.723 32.608 146.274 1.00 24.07 ATOM 1677 CE2 PHE B 95 105.743 30.836 147.610 1.00 20.75 ATOM 1678 CZ PHE B 95 106.386 32.072 147.530 1.00 23.23 ATOM 1679 C PHE B 95 105.425 27.707 142.804 1.00 25.56 ATOM 1680 O PHE B 95 105.349 28.188 141.670 1.00 27.02 ATOM 1681 N GLU B 96 104.991 26.489 143.089 1.00 26.35 ATOM 1682 CA GLU B 96 104.359 25.706 142.056 1.00 27.18 ATOM 1683 CB GLU B 96 104.443 24.212 142.361 1.00 26.72 ATOM 1684 CG GLU B 96 103.867 23.337 141.254 1.00 26.24 ATOM 1685 CD GLU B 96 103.691 21.901 141.685 1.00 28.35 ATOM 1686 OE1 GLU B 96 103.162 21.678 142.795 1.00 30.76 ATOM 1687 OE2 GLU B 96 104.064 20.988 140.920 1.00 31.23 ATOM 1688 C GLU B 96 102.909 26.158 142.020 1.00 28.96 ATOM 1689 O GLU B 96 102.167 26.018 142.993 1.00 31.23 ATOM 1690 N ARG B 97 102.509 26.726 140.897 1.00 29.93 ATOM 1691 CA ARG B 97 101.148 27.187 140.751 1.00 29.36 ATOM 1692 CB ARG B 97 101.105 28.718 140.754 1.00 32.52 ATOM 1693 CG ARG B 97 99.740 29.288 140.426 1.00 35.07 ATOM 1694 CD ARG B 97 99.770 30.797 140.343 1.00 41.18 ATOM 1695 NE ARG B 97 98.453 31.329 139.994 1.00 47.09 ATOM 1696 CZ ARG B 97 97.402 31.326 140.812 1.00 48.95 ATOM 1697 NH1 ARG B 97 97.520 30.823 142.036 1.00 50.33 ATOM 1698 NH2 ARG B 97 96.231 31.812 140.405 1.00 48.08 ATOM 1699 C ARG B 97 100.526 26.663 139.471 1.00 27.73 ATOM 1700 O ARG B 97 101.104 26.783 138.392 1.00 26.45 ATOM 1701 N LEU B 98 99.350 26.059 139.611 1.00 27.65 ATOM 1702 CA LEU B 98 98.585 25.555 138.473 1.00 27.40 ATOM 1703 CB LEU B 98 97.707 24.376 138.909 1.00 23.68 ATOM 1704 CG LEU B 98 96.669 23.882 137.894 1.00 21.58 ATOM 1705 CD1 LEU B 98 97.341 23.545 136.586 1.00 20.86 ATOM 1706 CD2 LEU B 98 95.952 22.658 138.444 1.00 20.79 ATOM 1707 C LEU B 98 97.720 26.737 137.990 1.00 27.81 ATOM 1708 O LEU B 98 96.682 27.043 138.571 1.00 29.38 ATOM 1709 N GLU B 99 98.177 27.409 136.940 1.00 28.61 ATOM 1710 CA GLU B 99 97.493 28.572 136.394 1.00 28.93 ATOM 1711 CB GLU B 99 98.395 29.219 135.349 1.00 28.89 ATOM 1712 CG GLU B 99 99.753 29.616 135.912 1.00 28.08 ATOM 1713 CD GLU B 99 99.671 30.824 136.832 1.00 31.83 ATOM 1714 OE1 GLU B 99 100.684 31.141 137.499 1.00 30.76 ATOM 1715 OE2 GLU B 99 98.589 31.463 136.878 1.00 33.87 ATOM 1716 C GLU B 99 96.128 28.243 135.810 1.00 29.29 ATOM 1717 O GLU B 99 95.766 27.069 135.659 1.00 28.75 ATOM 1718 N SER B 100 95.374 29.289 135.483 1.00 29.92 ATOM 1719 CA SER B 100 94.028 29.126 134.939 1.00 30.61 ATOM 1720 CB SER B 100 93.283 30.467 134.926 1.00 28.25 ATOM 1721 OG SER B 100 93.858 31.384 134.009 1.00 24.98 ATOM 1722 C SER B 100 94.002 28.527 133.538 1.00 32.21 ATOM 1723 O SER B 100 92.957 28.065 133.087 1.00 34.96 ATOM 1724 N ASN B 101 95.141 28.527 132.853 1.00 32.04 ATOM 1725 CA ASN B 101 95.221 27.972 131.503 1.00 30.78 ATOM 1726 CB ASN B 101 96.303 28.694 130.704 1.00 29.70 ATOM 1727 CG ASN B 101 97.627 28.688 131.416 1.00 28.96 ATOM 1728 OD1 ASN B 101 97.688 28.381 132.603 1.00 29.57 ATOM 1729 ND2 ASN B 101 98.695 29.036 130.708 1.00 28.13 ATOM 1730 C ASN B 101 95.541 26.490 131.559 1.00 29.90 ATOM 1731 O ASN B 101 95.611 25.823 130.528 1.00 31.66 ATOM 1732 N ASN B 102 95.740 25.988 132.772 1.00 28.75 ATOM 1733 CA ASN B 102 96.054 24.580 133.010 1.00 27.81 ATOM 1734 CB ASN B 102 95.143 23.695 132.193 1.00 25.64 ATOM 1735 CG ASN B 102 93.733 23.887 132.576 1.00 25.66 ATOM 1736 OD1 ASN B 102 93.384 23.686 133.737 1.00 27.29 ATOM 1737 ND2 ASN B 102 92.901 24.313 131.627 1.00 27.10 ATOM 1738 C ASN B 102 97.494 24.199 132.779 1.00 26.40 ATOM 1739 O ASN B 102 97.812 23.049 132.472 1.00 24.65 ATOM 1740 N TYR B 103 98.358 25.192 132.937 1.00 26.13 ATOM 1741 CA TYR B 103 99.795 25.017 132.810 1.00 26.46 ATOM 1742 CB TYR B 103 100.380 25.977 131.781 1.00 26.68 ATOM 1743 CG TYR B 103 100.227 25.513 130.360 1.00 28.89 ATOM 1744 CD1 TYR B 103 101.046 24.506 129.852 1.00 29.01 ATOM 1745 CE1 TYR B 103 100.901 24.047 128.551 1.00 31.54 ATOM 1746 CD2 TYR B 103 99.246 26.059 129.528 1.00 27.75 ATOM 1747 CE2 TYR B 103 99.084 25.604 128.214 1.00 30.75 ATOM 1748 CZ TYR B 103 99.918 24.596 127.728 1.00 32.28 ATOM 1749 OH TYR B 103 99.787 24.135 126.429 1.00 32.13 ATOM 1750 C TYR B 103 100.355 25.382 134.163 1.00 26.02 ATOM 1751 O TYR B 103 99.770 26.184 134.880 1.00 27.29 ATOM 1752 N ASN B 104 101.485 24.793 134.511 1.00 24.28 ATOM 1753 CA ASN B 104 102.130 25.083 135.773 1.00 22.21 ATOM 1754 CB ASN B 104 102.798 23.831 136.329 1.00 23.81 ATOM 1755 CG ASN B 104 101.841 22.940 137.065 1.00 22.38 ATOM 1756 OD1 ASN B 104 100.634 23.190 137.090 1.00 24.27 ATOM 1757 ND2 ASN B 104 102.372 21.887 137.674 1.00 19.93 ATOM 1758 C ASN B 104 103.200 26.123 135.559 1.00 21.77 ATOM 1759 O ASN B 104 103.741 26.258 134.466 1.00 18.48 ATOM 1760 N THR B 105 103.505 26.856 136.620 1.00 23.55 ATOM 1761 CA THR B 105 104.555 27.862 136.580 1.00 25.40 ATOM 1762 CB THR B 105 103.987 29.298 136.497 1.00 23.35 ATOM 1763 OG1 THR B 105 103.069 29.521 137.576 1.00 24.27 ATOM 1764 CG2 THR B 105 103.293 29.509 135.178 1.00 19.24 ATOM 1765 C THR B 105 105.380 27.713 137.851 1.00 26.45 ATOM 1766 O THR B 105 104.847 27.446 138.924 1.00 27.70 ATOM 1767 N TYR B 106 106.685 27.882 137.727 1.00 27.80 ATOM 1768 CA TYR B 106 107.554 27.755 138.881 1.00 28.15 ATOM 1769 CB TYR B 106 108.503 26.592 138.646 1.00 24.96 ATOM 1770 CG TYR B 106 107.735 25.288 138.599 1.00 23.60 ATOM 1771 CD1 TYR B 106 107.488 24.566 139.769 1.00 21.27 ATOM 1772 CE1 TYR B 106 106.742 23.395 139.750 1.00 21.89 ATOM 1773 CD2 TYR B 106 107.208 24.800 137.394 1.00 21.41 ATOM 1774 CE2 TYR B 106 106.456 23.626 137.360 1.00 21.03 ATOM 1775 CZ TYR B 106 106.229 22.925 138.548 1.00 24.06 ATOM 1776 OH TYR B 106 105.515 21.741 138.546 1.00 23.62 ATOM 1777 C TYR B 106 108.280 29.061 139.145 1.00 30.41 ATOM 1778 O TYR B 106 109.245 29.426 138.469 1.00 31.45 ATOM 1779 N ARG B 107 107.780 29.768 140.149 1.00 31.96 ATOM 1780 CA ARG B 107 108.312 31.061 140.535 1.00 32.79 ATOM 1781 CE ARG B 107 107.152 31.979 140.912 1.00 32.00 ATOM 1782 CG ARG B 107 107.533 33.406 141.148 1.00 33.23 ATOM 1783 CD ARG B 107 106.334 34.300 140.910 1.00 35.90 ATOM 1784 NE ARG B 107 105.191 33.986 141.771 1.00 40.00 ATOM 1785 CZ ARG B 107 105.077 34.354 143.045 1.00 39.85 ATOM 1786 NH1 ARG B 107 106.034 35.054 143.638 1.00 38.97 ATOM 1787 NH2 ARG B 107 103.996 34.019 143.729 1.00 41.38 ATOM 1788 C ARG B 107 109.274 30.938 141.696 1.00 33.01 ATOM 1789 O ARG B 107 108.957 30.282 142.690 1.00 32.53 ATOM 1790 N SER B 108 110.441 31.571 141.558 1.00 34.47 ATOM 1791 CA SER B 108 111.481 31.557 142.595 1.00 36.46 ATOM 1792 CB SER B 108 112.690 32.402 142.178 1.00 37.32 ATOM 1793 OG SER B 108 113.657 32.459 143.215 1.00 36.67 ATOM 1794 C SER B 108 110.947 32.111 143.898 1.00 36.91 ATOM 1795 O SER B 108 110.438 33.233 143.932 1.00 37.00 ATOM 1796 N ARG B 109 111.059 31.335 144.970 1.00 37.99 ATOM 1797 CA ARG B 109 110.564 31.808 146.249 1.00 40.27 ATOM 1798 CE ARG B 109 110.465 30.672 147.263 1.00 40.19 ATOM 1799 CG ARG B 109 109.690 31.068 148.511 1.00 41.08 ATOM 1800 CD ARG B 109 109.061 29.853 149.173 1.00 42.63 ATOM 1801 NE ARG B 109 110.060 28.944 149.723 1.00 44.24 ATOM 1802 CZ ARG B 109 110.484 28.960 150.984 1.00 45.28 ATOM 1803 NH1 ARG B 109 109.993 29.843 151.848 1.00 46.59 ATOM 1804 NH2 ARG B 109 111.402 28.084 151.379 1.00 45.30 ATOM 1805 C ARG B 109 111.485 32.895 146.769 1.00 42.63 ATOM 1806 O ARG B 109 111.067 33.741 147.570 1.00 43.11 ATOM 1807 N LYS B 110 112.736 32.890 146.308 1.00 43.86 ATOM 1808 CA LYS B 110 113.673 33.913 146.748 1.00 44.94 ATOM 1809 CB LYS B 110 115.098 33.364 146.858 1.00 46.17 ATOM 1810 CG LYS B 110 116.062 34.455 147.292 1.00 47.98 ATOM 1811 CD LYS B 110 117.294 33.939 147.986 1.00 50.45 ATOM 1812 CE LYS B 110 117.932 35.064 148.805 1.00 51.51 ATOM 1813 NZ LYS B 110 119.185 34.665 149.515 1.00 52.68 ATOM 1814 C LYS B 110 113.666 35.166 145.865 1.00 45.12 ATOM 1815 O LYS B 110 113.757 36.278 146.375 1.00 45.84 ATOM 1816 N TYR B 111 113.559 34.992 144.553 1.00 45.15 ATOM 1817 CA TYR B 111 113.520 36.128 143.636 1.00 45.47 ATOM 1818 CB TYR B 111 114.595 35.945 142.570 1.00 44.77 ATOM 1819 CG TYR B 111 115.949 35.789 143.216 1.00 45.41 ATOM 1820 CD1 TYR B 111 116.546 36.858 143.883 1.00 46.17 ATOM 1821 CE1 TYR B 111 117.744 36.700 144.573 1.00 44.71 ATOM 1822 CD2 TYR B 111 116.595 34.553 143.249 1.00 45.96 ATOM 1823 CE2 TYR B 111 117.794 34.388 143.936 1.00 45.72 ATOM 1824 CZ TYR B 111 118.357 35.467 144.596 1.00 44.93 ATOM 1825 OH TYR B 111 119.524 35.317 145.296 1.00 45.11 ATOM 1826 C TYR B 111 112.114 36.172 143.056 1.00 46.44 ATOM 1827 O TYR B 111 111.892 36.091 141.848 1.00 48.14 ATOM 1828 N THR B 112 111.174 36.301 143.983 1.00 47.26 ATOM 1829 CA THR B 112 109.738 36.320 143.740 1.00 48.53 ATOM 1830 CB THR B 112 109.021 37.059 144.878 1.00 49.29 ATOM 1831 OG1 THR B 112 109.774 38.227 145.246 1.00 49.98 ATOM 1832 CG2 THR B 112 108.870 36.133 146.086 1.00 49.24 ATOM 1833 C THR B 112 109.133 36.786 142.422 1.00 48.60 ATOM 1834 O THR B 112 108.006 36.406 142.115 1.00 48.90 ATOM 1835 N SER B 113 109.839 37.594 141.638 1.00 48.32 ATOM 1836 CA SER B 113 109.263 38.035 140.369 1.00 46.93 ATOM 1837 CB SER B 113 109.375 39.548 140.241 1.00 45.36 ATOM 1838 OG SER B 113 110.696 39.952 140.511 1.00 48.70 ATOM 1839 C SER B 113 109.842 37.360 139.120 1.00 45.91 ATOM 1840 O SER B 113 109.622 37.831 138.005 1.00 46.93 ATOM 1841 N TRP B 114 110.570 36.260 139.295 1.00 43.86 ATOM 1842 CA TRP B 114 111.122 35.566 138.143 1.00 43.51 ATOM 1843 CB TRP B 114 112.641 35.650 138.130 1.00 47.61 ATOM 1844 CG TRP B 114 113.203 37.028 138.254 1.00 50.02 ATOM 1845 CD2 TRP B 114 114.484 37.368 138.779 1.00 51.18 ATOM 1846 CE2 TRP B 114 114.627 38.765 138.660 1.00 51.19 ATOM 1847 CE3 TRP B 114 115.531 36.624 139.340 1.00 52.31 ATOM 1848 CD1 TRP B 114 112.631 38.199 137.845 1.00 50.13 ATOM 1849 NE1 TRP B 114 113.481 39.247 138.085 1.00 50.60 ATOM 1850 CZ2 TRP B 114 115.772 39.434 139.081 1.00 51.87 ATOM 1851 CZ3 TRP B 114 116.670 37.288 139.759 1.00 52.13 ATOM 1852 CH2 TRP B 114 116.782 38.680 139.628 1.00 52.79 ATOM 1853 C TRP B 114 110.702 34.109 138.121 1.00 42.54 ATOM 1854 O TRP B 114 110.521 33.493 139.173 1.00 42.95 ATOM 1855 N TYR B 115 110.561 33.559 136.917 1.00 40.61 ATOM 1856 CA TYR B 115 110.139 32.170 136.740 1.00 39.09 ATOM 1857 CB TYR B 115 108.873 32.068 135.879 1.00 40.31 ATOM 1858 CG TYR B 115 107.669 32.872 136.301 1.00 39.72 ATOM 1859 CD1 TYR B 115 107.651 34.250 136.156 1.00 39.96 ATOM 186O CE1 TYR B 115 106.527 34.992 136.490 1.00 40.25 ATOM 1861 CD2 TYR B 115 106.522 32.242 136.799 1.00 39.15 ATOM 1862 CE2 TYR B 115 105.393 32.975 137.135 1.00 37.77 ATOM 1863 CZ TYR B 115 105.402 34.353 136.979 1.00 39.46 ATOM 1864 OH TYR B 115 104.299 35.113 137.315 1.00 40.52 ATOM 1865 C TYR B 115 111.161 31.286 136.050 1.00 37.81 ATOM 1866 O TYR B 115 111.996 31.755 135.276 1.00 38.99 ATOM 1867 N VAL B 116 111.069 29.990 136.317 1.00 36.36 ATOM 1868 CA VAL B 116 111.929 29.032 135.645 1.00 36.77 ATOM 1869 CB VAL B 116 111.813 27.616 136.261 1.00 35.73 ATOM 1870 CG1 VAL B 116 112.514 26.622 135.379 1.00 32.37 ATOM 1871 CG2 VAL B 116 112.433 27.595 137.653 1.00 35.38 ATOM 1872 C VAL B 116 111.296 29.035 134.251 1.00 37.90 ATOM 1873 O VAL B 116 110.076 28.899 134.131 1.00 37.90 ATOM 1874 N ALA B 117 112.102 29.215 133.206 1.00 38.53 ATOM 1875 CA ALA B 117 111.563 29.264 131.847 1.00 37.77 ATOM 1876 CB ALA B 117 111.060 30.683 131.543 1.00 37.53 ATOM 1877 C ALA B 117 112.568 28.839 130.782 1.00 37.82 ATOM 1878 O ALA B 117 113.770 28.957 130.977 1.00 37.72 ATOM 1879 N LEU B 118 112.066 28.355 129.650 1.00 37.80 ATOM 1880 CA LEU B 118 112.925 27.930 128.558 1.00 37.19 ATOM 1881 CB LEU B 118 112.734 26.439 128.292 1.00 36.09 ATOM 1882 CG LEU B 118 113.087 25.465 129.422 1.00 35.69 ATOM 1883 CD1 LEU B 118 112.965 24.001 128.912 1.00 31.91 ATOM 1884 CD2 LEU B 118 114.497 25.764 129.928 1.00 31.08 ATOM 1885 C LEU B 118 112.631 28.712 127.281 1.00 38.86 ATOM 1886 O LEU B 118 111.471 28.991 126.969 1.00 39.01 ATOM 1887 N LYS B 119 113.689 29.062 126.551 1.00 40.20 ATOM 1888 CA LYS B 119 113.570 29.798 125.296 1.00 41.60 ATOM 1889 CB LYS B 119 114.916 30.418 124.914 1.00 44.91 ATOM 1890 CG LYS B 119 115.443 31.523 125.817 1.00 46.42 ATOM 1891 CD LYS B 119 116.928 31.754 125.510 1.00 48.54 ATOM 1892 CE LYS B 119 117.424 33.128 125.955 1.00 49.92 ATOM 1893 NZ LYS B 119 116.958 34.230 125.056 1.00 51.60 ATOM 1894 C LYS B 119 113.147 28.852 124.174 1.00 42.37 ATOM 1895 O LYS B 119 113.285 27.626 124.296 1.00 40.67 ATOM 1896 N ARG B 120 112.656 29.436 123.078 1.00 44.22 ATOM 1897 CA ARG B 120 112.203 28.687 121.906 1.00 46.02 ATOM 1898 CB ARG B 120 111.619 29.677 120.874 1.00 48.48 ATOM 1899 CG ARG B 120 110.660 30.706 121.512 1.00 54.41 ATOM 1900 CD ARG B 120 109.937 31.661 120.535 1.00 58.66 ATOM 1901 NE ARG B 120 108.765 31.067 119.876 1.00 63.50 ATOM 1902 CZ ARG B 120 107.764 31.765 119.330 1.00 65.20 ATOM 1903 NH1 ARG B 120 107.778 33.094 119.368 1.00 64.73 ATOM 1904 NH2 ARG B 120 106.754 31.138 118.724 1.00 65.86 ATOM 1905 C ARG B 120 113.384 27.882 121.323 1.00 45.52 ATOM 1906 O ARG B 120 113.198 26.924 120.562 1.00 44.84 ATOM 1907 N THR B 121 114.594 28.265 121.734 1.00 45.23 ATOM 1908 CA THR B 121 115.844 27.638 121.294 1.00 43.96 ATOM 1909 CE THR B 121 116.992 28.637 121.360 1.00 42.69 ATOM 1910 OG1 THR B 121 117.419 28.774 122.723 1.00 41.94 ATOM 1911 CG2 THR B 121 116.534 29.992 120.844 1.00 42.10 ATOM 1912 C THR B 121 116.277 26.426 122.124 1.00 44.14 ATOM 1913 O THR B 121 117.222 25.723 121.759 1.00 43.98 ATOM 1914 N GLY B 122 115.611 26.198 123.252 1.00 44.98 ATOM 1915 CA GLY B 122 115.970 25.069 124.093 1.00 45.39 ATOM 1916 C GLY B 122 116.937 25.422 125.214 1.00 45.75 ATOM 1917 O GLY B 122 117.535 24.541 125.828 1.00 45.93 ATOM 1918 N GLN B 123 117.099 26.707 125.492 1.00 45.97 ATOM 1919 CA GLN B 123 118.001 27.116 126.555 1.00 47.84 ATOM 1920 CB GLN B 123 119.074 28.046 126.012 1.00 51.23 ATOM 1921 CG GLN B 123 119.943 27.391 124.991 1.00 56.90 ATOM 1922 CD GLN B 123 120.689 28.407 124.187 1.00 61.76 ATOM 1923 OE1 GLN B 123 120.084 29.321 123.616 1.00 63.94 ATOM 1924 NE2 GLN B 123 122.015 28.266 124.129 1.00 63.33 ATOM 1925 CG LN B 123 117.209 27.829 127.618 1.00 46.32 ATOM 1926 O GLN B 123 116.221 28.495 127.310 1.00 46.58 ATOM 1927 N TYR B 124 117.635 27.701 128.869 1.00 43.86 ATOM 1928 CA TYR B 124 116.907 28.360 129.927 1.00 42.11 ATOM 1929 CB TYR B 124 117.518 28.026 131.294 1.00 41.58 ATOM 1930 CG TYR B 124 118.722 28.851 131.700 1.00 42.91 ATOM 1931 CD1 TYR B 124 118.594 30.204 132.041 1.00 42.19 ATOM 1932 CE1 TYR B 124 119.697 30.951 132.453 1.00 42.26 ATOM 1933 CD2 TYR B 124 119.989 28.269 131.781 1.00 42.35 ATOM 1934 CE2 TYR B 124 121.096 29.005 132.193 1.00 41.60 ATOM 1935 CZ TYR B 124 120.946 30.339 132.527 1.00 42.23 ATOM 1936 OH TYR B 124 122.046 31.048 132.944 1.00 41.91 ATOM 1937 C TYR B 124 116.889 29.866 129.672 1.00 41.35 ATOM 1938 O TYR B 124 117.800 30.423 129.065 1.00 40.98 ATOM 1939 N LYS B 125 115.821 30.507 130.126 1.00 40.27 ATOM 1940 CA LYS B 125 115.643 31.934 129.978 1.00 37.43 ATOM 1941 CB LYS B 125 114.227 32.210 129.493 1.00 37.31 ATOM 1942 CG LYS B 125 113.893 33.657 129.377 1.00 37.20 ATOM 1943 CD LYS B 125 112.614 33.812 128.619 1.00 39.57 ATOM 1944 CE LYS B 125 112.257 35.271 128.448 1.00 41.27 ATOM 1945 NZ LYS B 125 111.167 35.402 127.445 1.00 43.99 ATOM 1946 C LYS B 125 115.891 32.583 131.331 1.00 36.74 ATOM 1947 O LYS B 125 115.408 32.110 132.368 1.00 35.41 ATOM 1948 N LEU B 126 116.662 33.662 131.312 1.00 36.70 ATOM 1949 CA LEU B 126 117.005 34.383 132.522 1.00 36.52 ATOM 1950 CB LEU B 126 117.877 35.586 132.186 1.00 37.09 ATOM 1951 CG LEU B 126 119.375 35.336 132.036 1.00 37.50 ATOM 1952 CD1 LEU B 126 120.054 36.676 131.792 1.00 36.55 ATOM 1953 CD2 LEU B 126 119.933 34.674 133.298 1.00 36.86 ATOM 1954 C LEU B 126 115.802 34.859 133.298 1.00 36.94 ATOM 1955 O LEU B 126 114.878 35.432 132.732 1.00 38.21 ATOM 1956 N GLY B 127 115.823 34.635 134.603 1.00 36.87 ATOM 1957 CA GLY B 127 114.716 35.075 135.417 1.00 39.12 ATOM 1958 C GLY B 127 114.457 36.539 135.139 1.00 40.81 ATOM 1959 O GLY B 127 113.333 36.949 134.886 1.00 42.21 ATOM 1960 N SER B 128 115.515 37.332 135.174 1.00 42.67 ATOM 1961 CA SER B 128 115.409 38.761 134.929 1.00 44.81 ATOM 1962 CB SER B 128 116.826 39.362 134.873 1.00 46.60 ATOM 1963 OG SER B 128 117.725 38.527 134.145 1.00 48.48 ATOM 1964 C SER B 128 114.618 39.107 133.658 1.00 44.99 ATOM 1965 O SER B 128 114.206 40.256 133.465 1.00 44.55 ATOM 1966 N LYS B 129 114.393 38.113 132.803 1.00 45.58 ATOM 1967 CA LYS B 129 113.674 38.336 131.552 1.00 46.27 ATOM 1968 CB LYS B 129 114.514 37.864 130.358 1.00 46.90 ATOM 1969 CG LYS B 129 115.839 38.592 130.121 1.00 49.02 ATOM 1970 CD LYS B 129 116.341 38.312 128.697 1.00 49.89 ATOM 1971 CE LYS B 129 116.306 36.810 128.359 1.00 50.63 ATOM 1972 NZ LYS B 129 116.042 36.545 126.905 1.00 49.75 ATOM 1973 C LYS B 129 112.311 37.646 131.461 1.00 46.33 ATOM 1974 O LYS B 129 111.671 37.690 130.404 1.00 46.91 ATOM 1975 N THR B 130 111.860 37.018 132.544 1.00 44.73 ATOM 1976 CA THR B 130 110.581 36.307 132.517 1.00 43.35 ATOM 1977 CB THR B 130 110.621 35.062 133.386 1.00 41.73 ATOM 1978 OG1 THR B 130 110.608 35.455 134.763 1.00 39.55 ATOM 1979 CG2 THR B 130 111.874 34.249 133.090 1.00 41.36 ATOM 1980 C THR B 130 109.385 37.114 132.991 1.00 43.61 ATOM 1981 O THR B 130 109.473 37.861 133.959 1.00 43.97 ATOM 1982 N GLY B 131 108.259 36.927 132.314 1.00 43.39 ATOM 1983 CA GLY B 131 107.039 37.629 132.668 1.00 43.69 ATOM 1984 C GLY B 131 105.821 36.716 132.602 1.00 44.30 ATOM 1985 O GLY B 131 105.876 35.637 132.003 1.00 45.45 ATOM 1986 N PRO B 132 104.701 37.118 133.218 1.00 42.51 ATOM 1987 CD PRO B 132 104.560 38.310 134.066 1.00 40.46 ATOM 1988 CA PRO B 132 103.470 36.326 133.226 1.00 41.94 ATOM 1989 CB PRO B 132 102.560 37.119 134.155 1.00 42.03 ATOM 1990 CG PRO B 132 103.090 38.521 134.041 1.00 42.39 ATOM 1991 C PRO B 132 102.845 36.068 131.858 1.00 42.14 ATOM 1992 O PRO B 132 102.262 35.006 131.625 1.00 43.05 ATOM 1993 N GLY B 133 102.967 37.029 130.951 1.00 41.52 ATOM 1994 CA GLY B 133 102.398 36.844 129.632 1.00 40.35 ATOM 1995 C GLY B 133 103.299 36.031 128.728 1.00 39.56 ATOM 1996 O GLY B 133 103.087 35.995 127.526 1.00 41.25 ATOM 1997 N GLN B 134 104.293 35.361 129.298 1.00 38.32 ATOM 1998 CA GLN B 134 105.228 34.575 128.501 1.00 37.83 ATOM 1999 CB GLN B 134 106.643 34.795 129.015 1.00 36.88 ATOM 2000 CG GLN B 134 107.170 36.177 128.703 1.00 37.38 ATOM 2001 CD GLN B 134 108.506 36.441 129.351 1.00 37.57 ATOM 2002 OE1 GLN B 134 109.404 35.600 129.301 1.00 38.74 ATOM 2003 NE2 GLN B 134 108.651 37.614 129.960 1.00 34.92 ATOM 2004 C GLN B 134 104.969 33.079 128.378 1.00 38.13 ATOM 2005 O GLN B 134 104.701 32.387 129.362 1.00 39.42 ATOM 2006 N LYS B 135 105.084 32.595 127.146 1.00 37.17 ATOM 2007 CA LYS B 135 104.874 31.195 126.799 1.00 36.17 ATOM 2008 CB LYS B 135 104.796 31.095 125.273 1.00 35.42 ATOM 2009 CG LYS B 135 104.557 29.715 124.683 1.00 38.19 ATOM 2010 CD LYS B 135 104.243 29.862 123.193 1.00 40.23 ATOM 2011 CE LYS B 135 104.527 28.601 122.385 1.00 42.09 ATOM 2012 NZ LYS B 135 104.390 28.870 120.910 1.00 43.39 ATOM 2013 C LYS B 135 106.009 30.325 127.353 1.00 35.89 ATOM 2014 O LYS B 135 105.863 29.109 127.525 1.00 34.50 ATOM 2015 N ALA B 136 107.134 30.970 127.651 1.00 35.18 ATOM 2016 CA ALA B 136 108.310 30.278 128.170 1.00 34.66 ATOM 2017 CB ALA B 136 109.556 31.186 128.044 1.00 34.18 ATOM 2018 C ALA B 136 108.167 29.807 129.613 1.00 34.08 ATOM 2019 O ALA B 136 108.778 28.817 129.996 1.00 34.88 ATOM 2020 N ILE B 137 107.362 30.503 130.412 1.00 33.51 ATOM 2021 CA ILE B 137 107.206 30.131 131.813 1.00 31.04 ATOM 2022 CB ILE B 137 106.839 31.333 132.687 1.00 30.89 ATOM 2023 CG2 ILE B 137 107.918 32.402 132.550 1.00 30.26 ATOM 2024 CG1 ILE B 137 105.438 31.848 132.307 1.00 30.69 ATOM 2025 CD1 ILE B 137 104.692 32.539 133.443 1.00 26.19 ATOM 2026 C ILE B 137 106.176 29.064 132.071 1.00 29.74 ATOM 2027 O ILE B 137 106.022 28.617 133.206 1.00 31.83 ATOM 2028 N LEU B 138 105.478 28.642 131.030 1.00 28.62 ATOM 2029 CA LEU B 138 104.451 27.622 131.194 1.00 28.23 ATOM 2030 CB LEU B 138 103.284 27.930 130.259 1.00 29.47 ATOM 2031 CG LEU B 138 102.865 29.413 130.203 1.00 30.75 ATOM 2032 CD1 LEU B 138 101.796 29.566 129.128 1.00 29.77 ATOM 2033 CD2 LEU B 138 102.351 29.906 131.561 1.00 27.45 ATOM 2034 C LEU B 138 104.954 26.198 130.960 1.00 26.47 ATOM 2035 O LEU B 138 105.544 25.903 129.923 1.00 25.23 ATOM 2036 N PHE B 139 104.725 25.326 131.941 1.00 25.68 ATOM 2037 CA PHE B 139 105.131 23.923 131.846 1.00 25.87 ATOM 2038 CB PHE B 139 106.234 23.569 132.859 1.00 23.51 ATOM 2039 CG PHE B 139 107.506 24.311 132.656 1.00 21.66 ATOM 2040 CD1 PHE B 139 107.580 25.683 132.927 1.00 21.05 ATOM 2041 CD2 PHE B 139 108.625 23.657 132.148 1.00 20.83 ATOM 2042 CE1 PHE B 139 108.744 26.393 132.693 1.00 18.61 ATOM 2043 CE2 PHE B 139 109.801 24.358 131.908 1.00 19.33 ATOM 2044 CZ PHE B 139 109.859 25.732 132.181 1.00 20.03 ATOM 2045 C PHE B 139 103.951 23.010 132.110 1.00 26.53 ATOM 2046 O PHE B 139 102.993 23.380 132.786 1.00 27.10 ATOM 2047 N LEU B 140 104.050 21.800 131.588 1.00 28.27 ATOM 2048 CA LEU B 140 103.017 20.802 131.754 1.00 29.97 ATOM 2049 CB LEU B 140 102.468 20.429 130.382 1.00 30.53 ATOM 2050 CG LEU B 140 101.082 19.808 130.334 1.00 32.58 ATOM 2051 CD1 LEU B 140 100.063 20.784 130.918 1.00 33.58 ATOM 2052 CD2 LEU B 140 100.746 19.475 128.892 1.00 34.10 ATOM 2053 C LEU B 140 103.665 19.587 132.409 1.00 30.35 ATOM 2054 O LEU B 140 104.602 19.021 131.860 1.00 31.65 ATOM 2055 N PRO B 141 103.192 19.188 133.603 1.00 31.28 ATOM 2056 CD PRO B 141 102.215 19.891 134.457 1.00 31.64 ATOM 2057 CA PRO B 141 103.753 18.026 134.306 1.00 30.12 ATOM 2058 CB PRO B 141 103.109 18.105 135.693 1.00 29.44 ATOM 2059 CG PRO B 141 102.705 19.544 135.838 1.00 29.32 ATOM 2060 C PRO B 141 103.360 16.747 133.590 1.00 30.75 ATOM 2061 O PRO B 141 102.237 16.614 133.121 1.00 30.24 ATOM 2062 N MET B 142 104.282 15.801 133.509 1.00 33.53 ATOM 2063 CA MET B 142 104.011 14.533 132.847 1.00 35.21 ATOM 2064 CB MET B 142 104.585 14.543 131.428 1.00 35.75 ATOM 2065 CG MET B 142 103.932 15.558 130.502 1.00 40.96 ATOM 2066 SD MET B 142 104.611 15.593 128.806 1.00 48.60 ATOM 2067 CE MET B 142 103.935 14.039 128.108 1.00 46.52 ATOM 2068 C MET B 142 104.626 13.403 133.654 1.00 36.87 ATOM 2069 O MET B 142 105.849 13.302 133.791 1.00 36.47 ATOM 2070 N SER B 143 103.752 12.568 134.196 1.00 39.98 ATOM 2071 CA SER B 143 104.128 11.416 135.005 1.00 44.38 ATOM 2072 CB SER B 143 102.893 10.545 135.233 1.00 46.66 ATOM 2073 OG SER B 143 102.443 9.997 133.993 1.00 45.56 ATOM 2074 C SER B 143 105.188 40.565 134.310 1.00 46.01 ATOM 2075 O SER B 143 105.105 10.348 133.098 1.00 45.47 ATOM 2076 N ALA B 144 106.167 10.080 135.082 1.00 47.58 ATOM 2077 CA ALA B 144 107.235 9.220 134.557 1.00 47.58 ATOM 2078 CB ALA B 144 108.488 10.044 134.232 1.00 45.10 ATOM 2079 C ALA B 144 107.568 8.132 135.575 1.00 48.22 ATOM 2080 O ALA B 144 107.809 6.990 135.125 1.00 50.48 ATOM 2081 CB MET C 149 100.101 52.077 93.481 1.00 65.25 ATOM 2082 CG MET C 149 98.567 51.932 93.495 1.00 67.19 ATOM 2083 SD MET C 149 97.646 53.284 92.696 1.00 68.98 ATOM 2084 CE MET C 149 97.301 52.545 91.082 1.00 67.30 ATOM 2085 C MET C 149 99.985 53.283 95.664 1.00 60.59 ATOM 2086 O MET C 149 99.450 52.273 96.122 1.00 59.30 ATOM 2087 N MET C 149 102.131 53.199 94.388 1.00 62.84 ATOM 2088 CA MET C 149 100.638 53.271 94.282 1.00 62.68 ATOM 2089 N PRO C 150 100.005 54.441 96.338 1.00 58.42 ATOM 2090 CD PRO C 150 100.461 55.734 95.798 1.00 57.88 ATOM 2091 CA PRO C 150 99.424 54.610 97.675 1.00 56.45 ATOM 2092 CB PRO C 150 99.456 56.126 97.873 1.00 57.14 ATOM 2093 CG PRO C 150 100.633 56.551 97.044 1.00 57.64 ATOM 2094 C PRO C 150 98.005 54.048 97.816 1.00 53.83 ATOM 2095 O PRO C 150 97.107 54.416 97.055 1.00 53.21 ATOM 2096 N VAL C 151 97.816 53.165 98.796 1.00 50.88 ATOM 2097 CA VAL C 151 96.517 52.557 99.063 1.00 47.57 ATOM 2098 CB VAL C 151 96.416 51.143 98.490 1.00 48.19 ATOM 2099 CG1 VAL C 151 95.068 50.539 98.847 1.00 48.29 ATOM 2100 CG2 VAL C 151 96.594 51.184 96.983 1.00 50.20 ATOM 2101 C VAL C 151 96.272 52.448 100.554 1.00 45.11 ATOM 2102 O VAL C 151 97.118 51.951 101.287 1.00 43.01 ATOM 2103 N ALA C 152 95.110 52.927 100.993 1.00 44.71 ATOM 2104 CA ALA C 152 94.723 52.868 102.399 1.00 42.52 ATOM 2105 CB ALA C 152 93.535 53.769 102.656 1.00 40.04 ATOM 2106 C ALA C 152 94.359 51.418 102.712 1.00 41.56 ATOM 2107 O ALA C 152 93.933 50.671 101.827 1.00 41.60 ATOM 2108 N PRO C 153 94.526 50.995 103.974 1.00 40.07 ATOM 2109 CD PRO C 153 95.014 51.703 105.165 1.00 39.42 ATOM 2110 CA PRO C 153 94.186 49.607 104.289 1.00 38.59 ATOM 2111 CB PRO C 153 94.527 49.492 105.776 1.00 39.06 ATOM 2112 CG PRO C 153 94.411 50.890 106.270 1.00 41.48 ATOM 2113 C PRO C 153 92.747 49.217 103.964 1.00 37.37 ATOM 2114 O PRO C 153 91.816 50.015 104.083 1.00 38.28 ATOM 2115 N TYR C 154 92.579 47.981 103.522 1.00 35.32 ATOM 2116 CA TYR C 154 91.266 47.474 103.184 1.00 33.69 ATOM 2117 CB TYR C 154 90.978 47.693 101.702 1.00 32.71 ATOM 2118 CG TYR C 154 91.927 46.970 100.783 1.00 34.21 ATOM 2119 CD1 TYR C 154 93.190 47.490 100.492 1.00 34.37 ATOM 2120 CE1 TYR C 154 94.079 46.795 99.663 1.00 34.30 ATOM 2121 CD2 TYR C 154 91.576 45.743 100.228 1.00 34.12 ATOM 2122 CE2 TYR C 154 92.453 45.044 99.411 1.00 33.65 ATOM 2123 CZ TYR C 154 93.698 45.570 99.129 1.00 34.17 ATOM 2124 OH TYR C 154 94.547 44.866 98.308 1.00 34.07 ATOM 2125 C TYR C 154 91.185 45.986 103.517 1.00 32.85 ATOM 2126 O TYR C 154 92.190 45.273 103.508 1.00 30.45 ATOM 2127 N TRP C 155 89.981 45.523 102.814 1.00 32.07 ATOM 2128 CA TRP C 155 89.775 44.128 104.156 1.00 31.61 ATOM 2129 CB TRP C 155 88.371 43.940 104.721 1.00 27.53 ATOM 2130 CG TRP C 155 88.090 44.839 105.865 1.00 21.45 ATOM 2131 CD2 TRP C 155 88.848 44.946 107.074 1.00 18.68 ATOM 2132 CE2 TRP C 155 88.212 45.910 107.881 1.00 16.98 ATOM 2133 CE3 TRP C 155 90.005 44.319 107.553 1.00 14.94 ATOM 2134 CD1 TRP C 155 87.059 45.714 105.978 1.00 19.22 ATOM 2135 NE1 TRP C 155 87.122 46.365 107.188 1.00 19.31 ATOM 2136 CZ2 TRP C 155 88.687 46.264 109.143 1.00 15.29 ATOM 2137 CZ3 TRP C 155 90.478 44.670 108.803 1.00 13.39 ATOM 2138 CH2 TRP C 155 89.819 45.634 109.586 1.00 14.61 ATOM 2139 C TRP C 155 89.938 43.229 102.940 1.00 33.45 ATOM 2140 O TRP C 155 89.303 43.450 101.909 1.00 33.14 ATOM 2141 N THR C 156 90.782 42.209 103.071 1.00 35.38 ATOM 2142 CA THR C 156 90.996 41.265 101.985 1.00 36.52 ATOM 2143 CB THR C 156 92.456 40.730 101.936 1.00 33.61 ATOM 2144 OG1 THR C 156 92.835 40.196 103.207 1.00 32.46 ATOM 2145 CG2 THR C 156 93.401 41.832 101.566 1.00 34.29 ATOM 2146 C THR C 156 90.047 40.075 102.090 1.00 38.59 ATOM 2147 O THR C 156 89.808 39.388 101.103 1.00 38.35 ATOM 2148 N SER C 157 89.491 39.840 103.275 1.00 40.70 ATOM 2149 CA SER C 157 88.579 38.717 103.466 1.00 43.38 ATOM 2150 CB SER C 157 89.344 37.529 104.044 1.00 43.82 ATOM 2151 OG SER C 157 90.408 37.166 103.185 1.00 45.77 ATOM 2152 C SER C 157 87.420 39.060 104.383 1.00 44.72 ATOM 2153 O SER C 157 87.261 38.476 105.450 1.00 45.26 ATOM 2154 N PRO C 158 86.580 40.006 103.970 1.00 46.25 ATOM 2155 CD PRO C 158 86.466 40.509 102.593 1.00 46.97 ATOM 2156 C PRO C 158 85.429 40.426 104.774 1.00 46.67 ATOM 2157 CB PRO C 158 84.771 41.465 103.889 1.00 47.50 ATOM 2158 CG PRO C 158 85.000 40.879 102.520 1.00 48.42 ATOM 2159 C PRO C 158 84.491 39.267 105.075 1.00 47.02 ATOM 2160 O PRO C 158 83.680 39.332 106.001 1.00 46.75 ATOM 2161 N GLU C 159 84.605 38.212 104.272 1.00 48.26 ATOM 2162 CA GLU C 159 83.780 37.014 104.422 1.00 47.93 ATOM 2163 CB GLU C 159 84.023 36.060 103.250 1.00 48.14 ATOM 2164 C GLU C 159 84.116 36.300 105.725 1.00 47.69 ATOM 2165 O GLU C 159 83.256 35.678 106.347 1.00 48.83 ATOM 2166 N LYS C 160 85.380 36.395 106.127 1.00 46.16 ATOM 2167 CA LYS C 160 85.859 35.764 107.355 1.00 44.33 ATOM 2168 CB LYS C 160 87.342 35.382 107.208 1.00 41.06 ATOM 2169 C LYS C 160 85.686 36.662 108.587 1.00 42.94 ATOM 2170 O LYS C 160 86.342 36.456 109.604 1.00 42.81 ATOM 2171 N MET C 161 84.793 37.642 108.509 1.00 41.39 ATOM 2172 CA MET C 161 84.595 38.558 109.628 1.00 39.39 ATOM 2173 CB MET C 161 85.216 39.934 109.294 1.00 38.51 ATOM 2174 CG MET C 161 86.759 39.909 109.157 1.00 37.19 ATOM 2175 SD MET C 161 87.570 41.276 108.213 1.00 35.28 ATOM 2176 CE MET C 161 87.835 42.474 109.497 1.00 32.14 ATOM 2177 C MET C 161 83.128 38.711 110.002 1.00 38.73 ATOM 2178 O MET C 161 82.798 39.400 110.962 1.00 38.29 ATOM 2179 N GLU C 162 82.254 38.048 109.254 1.00 38.86 ATOM 2180 CA GLU C 162 80.812 38.108 109.503 1.00 38.59 ATOM 2181 CB GLU C 162 80.080 37.201 108.502 1.00 35.61 ATOM 2182 C GLU C 162 80.398 37.733 110.944 1.00 38.75 ATOM 2183 O GLU C 162 79.430 38.274 111.487 1.00 39.79 ATOM 2184 N LYS C 163 81.126 36.815 111.568 1.00 38.04 ATOM 2185 CA LYS C 163 80.793 36.386 112.926 1.00 36.88 ATOM 2186 CB LYS C 163 81.329 34.972 113.155 1.00 37.78 ATOM 2187 CG LYS C 163 81.010 34.345 114.504 1.00 37.86 ATOM 2188 CD LYS C 163 81.898 33.115 114.723 1.00 37.39 ATOM 2189 CE LYS C 163 82.049 32.836 116.206 1.00 41.05 ATOM 2190 NZ LYS C 163 83.124 31.856 116.549 1.00 43.85 ATOM 2191 C LYS C 163 81.369 37.344 113.959 1.00 36.41 ATOM 2192 O LYS C 163 82.474 37.129 114.464 1.00 38.35 ATOM 2193 N LYS C 164 80.618 38.399 114.271 1.00 34.77 ATOM 2194 CA LYS C 164 81.061 39.405 115.233 1.00 33.48 ATOM 2195 CB LYS C 164 80.155 40.645 115.153 1.00 31.00 ATOM 2196 C LYS C 164 81.141 38.879 116.677 1.00 33.76 ATOM 2197 O LYS C 164 82.067 39.239 117.410 1.00 34.50 ATOM 2198 N LEU C 165 80.192 38.026 117.081 1.00 33.68 ATOM 2199 CA LEU C 165 80.182 37.450 118.435 1.00 31.67 ATOM 2200 CB LEU C 165 78.764 37.376 118.989 1.00 32.15 ATOM 2201 CG LEU C 165 78.678 36.482 120.242 1.00 32.85 ATOM 2202 CD1 LEU C 165 79.467 37.102 121.383 1.00 30.15 ATOM 2203 CD2 LEU C 165 77.244 36.289 120.648 1.00 32.03 ATOM 2204 C LEU C 165 80.778 36.046 118.571 1.00 31.11 ATOM 2205 O LEU C 165 80.331 35.112 117.914 1.00 28.78 ATOM 2206 N HIS C 166 81.766 35.908 119.454 1.00 32.82 ATOM 2207 CA HIS C 166 82.404 34.618 119.736 1.00 33.88 ATOM 2208 CB HIS C 166 83.919 34.710 119.632 1.00 35.77 ATOM 2209 CG HIS C 166 84.413 34.914 118.243 1.00 41.33 ATOM 2210 CD2 HIS C 166 85.227 34.159 117.469 1.00 43.37 ATOM 2211 ND1 HIS C 166 84.069 36.015 117.487 1.00 42.96 ATOM 2212 CE1 HIS C 166 84.651 35.930 116.303 1.00 44.52 ATOM 2213 NE2 HIS C 166 85.360 34.814 116.267 1.00 45.66 ATOM 2214 C HIS C 166 82.068 34.159 121.151 1.00 33.19 ATOM 2215 O HIS C 166 82.627 34.669 122.132 1.00 30.45 ATOM 2216 N ALA C 167 81.152 33.198 121.249 1.00 32.79 ATOM 2217 CA ALA C 167 80.745 32.641 122.534 1.00 33.37 ATOM 2218 CB ALA C 167 79.227 32.558 122.627 1.00 32.85 ATOM 2219 C ALA C 167 81.352 31.252 122.595 1.00 33.26 ATOM 2220 O ALA C 167 81.205 30.459 121.654 1.00 32.87 ATOM 2221 N VAL C 168 82.027 30.955 123.702 1.00 32.58 ATOM 2222 CA VAL C 168 82.683 29.669 123.849 1.00 31.16 ATOM 2223 CB VAL C 168 84.114 29.747 123.277 1.00 30.30 ATOM 2224 CG1 VAL C 168 84.071 30.079 121.815 1.00 29.14 ATOM 2225 CG2 VAL C 168 84.911 30.820 124.018 1.00 29.56 ATOM 2226 C VAL C 168 82.794 29.160 125.283 1.00 30.45 ATOM 2227 O VAL C 168 82.688 29.921 126.245 1.00 29.08 ATOM 2228 N PRO C 169 82.971 27.842 125.436 1.00 30.30 ATOM 2229 CD PRO C 169 82.654 26.785 124.457 1.00 28.93 ATOM 2230 CA PRO C 169 83.110 27.285 126.781 1.00 30.64 ATOM 2231 CB PRO C 169 82.783 25.806 126.581 1.00 28.08 ATOM 2232 CG PRO C 169 83.173 25.558 125.144 1.00 28.90 ATOM 2233 C PRO C 169 84.562 27.535 127.237 1.00 32.73 ATOM 2234 O PRO C 169 85.511 27.347 126.458 1.00 34.04 ATOM 2235 N ALA C 170 84.725 27.979 128.482 1.00 32.44 ATOM 2236 CA ALA C 170 86.039 28.261 129.046 1.00 31.35 ATOM 2237 CB ALA C 170 85.928 28.414 130.554 1.00 31.49 ATOM 2238 C ALA C 170 87.053 27.175 128.712 1.00 31.45 ATOM 2239 O ALA C 170 86.693 26.005 128.575 1.00 30.29 ATOM 2240 N ALA C 171 88.314 27.588 128.580 1.00 31.27 ATOM 2241 CA ALA C 171 89.436 26.705 128.280 1.00 31.34 ATOM 2242 CB ALA C 171 89.218 25.326 128.910 1.00 30.46 ATOM 2243 C ALA C 171 89.696 26.571 126.793 1.00 31.73 ATOM 2244 O ALA C 171 90.701 25.989 126.387 1.00 33.59 ATOM 2245 N LYS C 172 88.800 27.115 125.981 1.00 32.03 ATOM 2246 CA LYS C 172 88.960 27.043 124.533 1.00 32.88 ATOM 2247 CB LYS C 172 87.599 27.256 123.846 1.00 30.96 ATOM 2248 C LYS C 172 89.987 28.080 124.030 1.00 33.39 ATOM 2249 O LYS C 172 90.207 29.110 124.665 1.00 32.67 ATOM 2250 N THR C 173 90.623 27.773 122.902 1.00 33.31 ATOM 2251 CA THR C 173 91.600 28.649 122.261 1.00 32.28 ATOM 2252 CB THR C 173 92.572 27.846 121.364 1.00 33.35 ATOM 2253 OG1 THR C 173 93.408 27.012 122.176 1.00 36.76 ATOM 2254 CG2 THR C 173 93.419 28.780 120.513 1.00 30.69 ATOM 2255 C THR C 173 90.832 29.570 121.327 1.00 32.19 ATOM 2256 O THR C 173 90.104 29.097 120.463 1.00 31.00 ATOM 2257 N VAL C 174 91.002 30.877 121.486 1.00 33.05 ATOM 2258 CA VAL C 174 90.322 31.856 120.635 1.00 32.11 ATOM 2259 CB VAL C 174 89.621 32.944 121.499 1.00 30.78 ATOM 2260 CG1 VAL C 174 89.310 34.173 120.656 1.00 30.69 ATOM 2261 CG2 VAL C 174 88.335 32.393 122.085 1.00 30.31 ATOM 2262 C VAL C 174 91.287 32.555 119.664 1.00 31.79 ATOM 2263 O VAL C 174 92.390 32.929 120.049 1.00 32.17 ATOM 2264 N LYS C 175 90.865 32.728 118.410 1.00 31.18 ATOM 2265 CA LYS C 175 91.675 33.408 117.399 1.00 30.82 ATOM 2266 CB LYS C 175 92.271 32.392 116.408 1.00 26.76 ATOM 2267 C LYS C 175 90.801 34.409 116.641 1.00 31.23 ATOM 2268 O LYS C 175 89.760 34.048 116.119 1.00 31.11 ATOM 2269 N PHE C 176 91.216 35.671 116.606 1.00 33.39 ATOM 2270 CA PHE C 176 90.481 36.716 115.893 1.00 33.06 ATOM 2271 CB PHE C 176 90.184 37.888 116.820 1.00 30.10 ATOM 2272 CG PHE C 176 89.218 37.552 117.903 1.00 29.97 ATOM 2273 CD1 PHE C 176 88.000 36.942 117.597 1.00 28.34 ATOM 2274 CD2 PHE C 176 89.512 37.839 119.234 1.00 27.98 ATOM 2275 CE1 PHE C 176 87.096 36.627 118.606 1.00 27.80 ATOM 2276 CE2 PHE C 176 88.607 37.524 120.249 1.00 26.08 ATOM 2277 CZ PHE C 176 87.400 36.921 119.935 1.00 25.99 ATOM 2278 C PHE C 176 91.294 37.197 114.700 1.00 33.94 ATOM 2279 O PHE C 176 92.437 37.622 114.856 1.00 33.78 ATOM 2280 N LYS C 177 90.693 37.128 113.515 1.00 35.23 ATOM 2281 CA LYS C 177 91.364 37.530 112.284 1.00 35.59 ATOM 2282 CB LYS C 177 91.323 36.373 111.276 1.00 34.19 ATOM 2283 C LYS C 177 90.784 38.794 111.644 1.00 34.98 ATOM 2284 O LYS C 177 89.571 38.993 111.601 1.00 33.90 ATOM 2285 N CYS C 178 91.676 39.648 111.155 1.00 35.07 ATOM 2286 CA CYS C 178 91.300 40.888 110.475 1.00 35.44 ATOM 2287 C CYS C 178 92.115 41.000 109.186 1.00 35.69 ATOM 2288 O CYS C 178 92.889 41.941 109.003 1.00 32.89 ATOM 2289 CB CYS C 178 91.578 42.094 111.366 1.00 34.12 ATOM 2290 SG CYS C 178 90.402 42.228 112.746 1.00 36.50 ATOM 2291 N PRO C 179 91.940 40.032 108.273 1.00 36.77 ATOM 2292 CD PRO C 179 90.908 38.987 108.287 1.00 36.42 ATOM 2293 CA PRO C 179 92.665 40.019 107.003 1.00 38.32 ATOM 2294 CB PRO C 179 92.048 38.836 106.259 1.00 37.75 ATOM 2295 CG PRO C 179 91.493 37.977 107.357 1.00 37.51 ATOM 2296 C PRO C 179 92.456 41.324 106.259 1.00 39.57 ATOM 2297 O PRO C 179 91.340 41.645 105.845 1.00 39.56 ATOM 2298 N SER C 180 93.539 42.071 106.103 1.00 40.72 ATOM 2299 CA SER C 180 93.494 43.345 105.413 1.00 42.44 ATOM 2300 CB SER C 180 93.452 44.488 106.436 1.00 41.84 ATOM 2301 OG SER C 180 94.668 44.587 107.145 1.00 38.33 ATOM 2302 C SER C 180 94.719 43.493 104.513 1.00 43.44 ATOM 2303 O SER C 180 95.564 42.597 104.446 1.00 44.06 ATOM 2304 N SER C 181 94.809 44.626 103.821 1.00 43.27 ATOM 2305 CA SER C 181 95.936 44.892 102.941 1.00 42.03 ATOM 2306 CB SER C 181 95.782 44.108 101.635 1.00 40.63 ATOM 2307 OG SER C 181 96.947 44.184 100.837 1.00 38.12 ATOM 2308 C SER C 181 96.023 46.378 102.648 1.00 42.50 ATOM 2309 O SER C 181 95.125 47.143 102.995 1.00 41.78 ATOM 2310 N GLY C 182 97.120 46.777 102.014 1.00 44.44 ATOM 2311 CA GLY C 182 97.320 48.171 101.656 1.00 45.04 ATOM 2312 C GLY C 182 98.783 48.471 101.418 1.00 44.61 ATOM 2313 O GLY C 182 99.645 47.695 101.829 1.00 44.78 ATOM 2314 N THR C 183 99.070 49.577 100.735 1.00 44.98 ATOM 2315 CA THR C 183 100.456 49.970 100.486 1.00 43.50 ATOM 2316 CB THR C 183 100.890 49.698 99.019 1.00 42.33 ATOM 2317 OG1 THR C 183 100.264 50.645 98.148 1.00 43.45 ATOM 2318 CG2 THR C 183 100.513 48.279 98.599 1.00 39.10 ATOM 2319 C THR C 183 100.666 51.455 100.816 1.00 42.89 ATOM 2320 O THR C 183 99.935 52.329 100.345 1.00 42.37 ATOM 2321 N PRO C 184 101.659 51.749 101.670 1.00 43.03 ATOM 2322 CD PRO C 184 101.978 53.103 102.159 1.00 43.09 ATOM 2323 CA PRO C 184 102.540 50.755 102.290 1.00 42.57 ATOM 2324 CB PRO C 184 103.592 51.618 102.977 1.00 41.56 ATOM 2325 CG PRO C 184 102.811 52.817 103.396 1.00 41.09 ATOM 2326 C PRO C 184 101.825 49.814 103.268 1.00 43.39 ATOM 2327 O PRO C 184 100.795 50.162 103.861 1.00 43.41 ATOM 2328 N GLN C 185 102.386 48.619 103.418 1.00 43.86 ATOM 2329 CA GLN C 185 101.862 47.586 104.312 1.00 43.86 ATOM 2330 CB GLN C 185 102.944 46.527 104.538 1.00 45.08 ATOM 2331 CG GLN C 185 102.489 45.299 105.297 1.00 46.91 ATOM 2332 CD GLN C 185 101.676 44.346 104.437 1.00 48.43 ATOM 2333 OE1 GLN C 185 101.304 43.264 104.891 1.00 50.68 ATOM 2334 NE2 GLN C 185 101.397 44.741 103.192 1.00 46.11 ATOM 2335 C GLN C 185 101.446 48.171 105.660 1.00 42.38 ATOM 2336 O GLN C 185 102.272 48.724 106.381 1.00 43.07 ATOM 2337 N PRO C 186 100.157 48.053 106.021 1.00 41.59 ATOM 2338 CD PRO C 186 99.013 47.664 105.175 1.00 40.45 ATOM 2339 CA PRO C 186 99.704 48.599 107.308 1.00 40.23 ATOM 2340 CB PRO C 186 98.188 48.660 107.143 1.00 39.29 ATOM 2341 CG PRO C 186 97.905 47.553 106.177 1.00 40.98 ATOM 2342 C PRO C 186 100.143 47.865 108.583 1.00 39.30 ATOM 2343 O PRO C 186 100.686 46.758 108.545 1.00 39.33 ATOM 2344 N THR C 187 99.915 48.523 109.711 1.00 39.08 ATOM 2345 CA THR C 187 100.268 47.999 111.029 1.00 39.63 ATOM 2346 CB THR C 187 100.741 49.125 111.967 1.00 39.84 ATOM 2347 OG1 THR C 187 99.591 49.774 112.531 1.00 38.71 ATOM 2348 CG2 THR C 187 101.560 50.155 111.206 1.00 37.86 ATOM 2349 C THR C 187 99.025 47.407 111.684 1.00 39.39 ATOM 2350 O THR C 187 97.924 47.939 111.515 1.00 39.66 ATOM 2351 N LEU C 188 99.211 46.340 112.459 1.00 38.00 ATOM 2352 CA LEU C 188 98.103 45.682 113.148 1.00 36.36 ATOM 2353 CB LEU C 188 98.017 44.207 112.725 1.00 33.97 ATOM 2354 CG LEU C 188 96.738 43.357 112.848 1.00 31.46 ATOM 2355 CD1 LEU C 188 97.137 41.908 113.017 1.00 28.72 ATOM 2356 CD2 LEU C 188 95.886 43.779 114.021 1.00 33.12 ATOM 2357 C LEU C 188 98.298 45.731 114.661 1.00 36.78 ATOM 2358 O LEU C 188 99.316 45.271 115.176 1.00 37.59 ATOM 2359 N ARG C 189 97.332 46.297 115.371 1.00 37.19 ATOM 2360 CA ARG C 189 97.391 46.323 116.829 1.00 38.17 ATOM 2361 CB ARG C 189 97.843 47.685 117.345 1.00 39.09 ATOM 2362 CG ARG C 189 96.901 48.786 117.030 1.00 44.89 ATOM 2363 CD ARG C 189 97.431 50.096 117.534 1.00 50.33 ATOM 2364 NE ARG C 189 96.532 51.182 117.161 1.00 57.72 ATOM 2365 CZ ARG C 189 96.804 52.473 117.326 1.00 61.98 ATOM 2366 NH1 ARG C 189 97.960 52.847 117.863 1.00 65.57 ATOM 2367 NH2 ARG C 189 95.922 53.394 116.948 1.00 64.03 ATOM 2368 C ARG C 189 95.993 45.984 117.344 1.00 36.93 ATOM 2369 O ARG C 189 95.005 46.220 116.650 1.00 37.99 ATOM 2370 N TRP C 190 95.908 45.407 118.540 1.00 35.51 ATOM 2371 CA TRP C 190 94.613 45.041 119.111 1.00 33.97 ATOM 2372 CB TRP C 190 94.537 43.550 119.414 1.00 32.32 ATOM 2373 CG TRP C 190 94.615 42.690 118.212 1.00 33.64 ATOM 2374 CD2 TRP C 190 93.514 42.111 117.497 1.00 35.85 ATOM 2375 CE2 TRP C 190 94.057 41.391 116.409 1.00 34.62 ATOM 2376 CE3 TRP C 190 92.117 42.131 117.670 1.00 36.09 ATOM 2377 CD1 TRP C 190 95.741 42.309 117.549 1.00 32.67 ATOM 2378 NE1 TRP C 190 95.419 41.531 116.468 1.00 32.98 ATOM 2379 CZ2 TRP C 190 93.255 40.694 115.495 1.00 31.94 ATOM 2380 CZ3 TRP C 190 91.322 41.438 116.760 1.00 32.93 ATOM 2381 CH2 TRP C 190 91.898 40.730 115.688 1.00 33.05 ATOM 2382 C TRP C 190 94.301 45.793 120.382 1.00 34.67 ATOM 2383 O TRP C 190 95.201 46.292 121.059 1.00 35.92 ATOM 2384 N LEU C 191 93.014 45.860 120.705 1.00 34.12 ATOM 2385 CA LEU C 191 92.568 46.547 121.900 1.00 33.44 ATOM 2386 CB LEU C 191 91.985 47.911 121.546 1.00 33.52 ATOM 2387 CG LEU C 191 92.809 48.949 120.790 1.00 32.72 ATOM 2388 CD1 LEU C 191 91.974 50.219 120.686 1.00 30.58 ATOM 2389 CD2 LEU C 191 94.127 49.217 121.508 1.00 32.65 ATOM 2390 C LEU C 191 91.504 45.750 122.634 1.00 34.98 ATOM 2391 O LEU C 191 90.497 45.348 122.038 1.00 35.62 ATOM 2392 N LYS C 192 91.726 45.516 123.925 1.00 34.06 ATOM 2393 CA LYS C 192 90.749 44.804 124.737 1.00 32.83 ATOM 2394 CB LYS C 192 91.461 43.992 125.814 1.00 32.77 ATOM 2395 CG LYS C 192 90.590 43.068 126.641 1.00 30.53 ATOM 2396 CD LYS C 192 91.486 42.167 127.481 1.00 30.45 ATOM 2397 CE LYS C 192 90.737 41.003 128.119 1.00 29.54 ATOM 2398 NZ LYS C 192 89.698 41.499 129.062 1.00 29.96 ATOM 2399 C LYS C 192 89.900 45.906 125.357 1.00 33.41 ATOM 2400 O LYS C 192 90.403 46.752 126.100 1.00 33.66 ATOM 2401 N ASN C 193 88.620 45.909 125.011 1.00 34.21 ATOM 2402 CA ASN C 193 87.670 46.902 125.495 1.00 35.18 ATOM 2403 CB ASN C 193 87.418 46.694 126.982 1.00 36.87 ATOM 2404 CG ASN C 193 87.001 45.274 127.301 1.00 39.31 ATOM 2405 OD1 ASN C 193 86.035 44.750 126.742 1.00 41.66 ATOM 2406 ND2 ASN C 193 87.732 44.640 128.204 1.00 41.39 ATOM 2407 C ASN C 193 88.103 48.343 125.229 1.00 35.22 ATOM 2408 O ASN C 193 87.892 49.226 126.056 1.00 34.17 ATOM 2409 N GLY C 194 88.714 48.569 124.070 1.00 34.49 ATOM 2410 CA GLY C 194 89.139 49.910 123.719 1.00 36.02 ATOM 2411 C GLY C 194 90.462 50.383 124.290 1.00 35.90 ATOM 2412 O GLY C 194 90.927 51.468 123.948 1.00 36.63 ATOM 2413 N LYS C 195 91.083 49.582 125.145 1.00 34.82 ATOM 2414 CA LYS C 195 92.356 49.975 125.726 1.00 35.14 ATOM 2415 CB LYS C 195 92.303 49.785 127.246 1.00 33.76 ATOM 2416 C LYS C 195 93.526 49.184 125.136 1.00 35.43 ATOM 2417 O LYS C 195 93.327 48.132 124.530 1.00 35.33 ATOM 2418 N GLU C 196 94.741 49.705 125.292 1.00 36.75 ATOM 2419 CA GLU C 196 95.931 49.013 124.802 1.00 39.16 ATOM 2420 CB GLU C 196 97.214 49.728 125.252 1.00 38.19 ATOM 2421 C GLU C 196 95.883 47.609 125.405 1.00 40.34 ATOM 2422 O GLU C 196 95.549 47.435 126.575 1.00 40.73 ATOM 2423 N PHE C 197 96.223 46.612 124.603 1.00 41.32 ATOM 2424 CA PHE C 197 96.172 45.230 125.047 1.00 41.76 ATOM 2425 CB PHE C 197 95.207 44.461 124.137 1.00 39.22 ATOM 2426 CG PHE C 197 94.989 43.030 124.540 1.00 38.70 ATOM 2427 CD1 PHE C 197 94.817 42.047 123.575 1.00 37.21 ATOM 2428 CD2 PHE C 197 94.933 42.662 125.882 1.00 39.36 ATOM 2429 CE1 PHE C 197 94.593 40.723 123.930 1.00 36.13 ATOM 2430 CE2 PHE C 197 94.706 41.330 126.248 1.00 39.06 ATOM 2431 CZ PHE C 197 94.538 40.362 125.265 1.00 35.94 ATOM 2432 C PHE C 197 97.539 44.554 125.021 1.00 42.62 ATOM 2433 O PHE C 197 97.909 43.977 124.007 1.00 41.17 ATOM 2434 N LYS C 198 98.286 44.615 126.121 1.00 43.49 ATOM 2435 CA LYS C 198 99.600 43.971 126.152 1.00 44.01 ATOM 2436 CB LYS C 198 100.535 44.686 127.129 1.00 42.32 ATOM 2437 C LYS C 198 99.436 42.512 126.561 1.00 45.04 ATOM 2438 O LYS C 198 98.508 42.171 127.286 1.00 43.90 ATOM 2439 N PRO C 199 100.330 41.624 126.084 1.00 47.00 ATOM 2440 CD PRO C 199 101.396 41.853 125.097 1.00 47.32 ATOM 2441 CA PRO C 199 100.251 40.199 126.421 1.00 47.52 ATOM 2442 CB PRO C 199 101.345 39.568 125.555 1.00 46.71 ATOM 2443 CG PRO C 199 102.313 40.681 125.355 1.00 47.16 ATOM 2444 C PRO C 199 100.369 39.829 127.893 1.00 48.67 ATOM 2445 O PRO C 199 99.992 38.722 128.282 1.00 49.53 ATOM 2446 N ASP C 200 100.878 40.733 128.724 1.00 49.32 ATOM 2447 CA ASP C 200 100.991 40.428 130.143 1.00 49.39 ATOM 2448 CB ASP C 200 102.074 41.281 130.785 1.00 52.43 ATOM 2449 CG ASP C 200 103.436 41.042 130.149 1.00 55.59 ATOM 2450 OD1 ASP C 200 103.565 41.275 128.927 1.00 58.24 ATOM 2451 OD2 ASP C 200 104.370 40.607 130.866 1.00 56.58 ATOM 2452 C ASP C 200 99.651 40.664 130.808 1.00 48.50 ATOM 2453 O ASP C 200 99.503 40.490 132.022 1.00 49.38 ATOM 2454 N HIS C 201 98.668 41.046 130.003 1.00 46.95 ATOM 2455 CA HIS C 201 97.328 41.276 130.520 1.00 44.80 ATOM 2456 CB HIS C 201 96.488 42.086 129.558 1.00 45.08 ATOM 2457 CG HIS C 201 96.808 43.540 129.568 1.00 45.02 ATOM 2458 CD2 HIS C 201 96.109 44.598 130.026 1.00 44.68 ATOM 2459 ND1 HIS C 201 97.967 44.049 129.026 1.00 46.64 ATOM 2460 CE1 HIS C 201 97.972 45.361 129.144 1.00 45.48 ATOM 2461 NE2 HIS C 201 96.859 45.724 129.752 1.00 44.56 ATOM 2462 C HIS C 201 96.583 39.974 130.810 1.00 43.86 ATOM 2463 O HIS C 201 95.456 40.005 131.319 1.00 43.74 ATOM 2464 N ARG C 202 97.186 38.826 130.482 1.00 41.62 ATOM 2465 CA ARG C 202 96.542 37.554 130.763 1.00 40.68 ATOM 2466 CB ARG C 202 95.555 37.202 129.660 1.00 39.42 ATOM 2467 CG ARG C 202 96.157 36.684 128.370 1.00 37.72 ATOM 2468 CD ARG C 202 95.064 36.546 127.321 1.00 37.23 ATOM 2469 NE ARG C 202 94.048 35.571 127.694 1.00 34.77 ATOM 2470 CZ ARG C 202 94.172 34.262 127.510 1.00 37.24 ATOM 2471 NH1 ARG C 202 95.271 33.767 126.953 1.00 39.35 ATOM 2472 NH2 ARG C 202 93.197 33.444 127.882 1.00 34.91 ATOM 2473 C ARG C 202 97.589 36.476 130.874 1.00 42.16 ATOM 2474 O ARG C 202 98.590 36.509 130.160 1.00 43.04 ATOM 2475 N ILE C 203 97.359 35.524 131.772 1.00 42.53 ATOM 2476 CA ILE C 203 98.311 34.430 131.958 1.00 44.52 ATOM 2477 CB ILE C 203 97.821 33.391 133.016 1.00 45.70 ATOM 2478 CG2 ILE C 203 98.781 32.199 133.078 1.00 45.54 ATOM 2479 CG1 ILE C 203 97.776 34.034 134.403 1.00 48.01 ATOM 2480 CD1 ILE C 203 99.143 34.427 134.944 1.00 48.44 ATOM 2481 C ILE C 203 98.539 33.703 130.638 1.00 44.37 ATOM 2482 O ILE C 203 97.593 33.443 129.888 1.00 45.23 ATOM 2483 N GLY C 204 99.796 33.374 130.358 1.00 43.64 ATOM 2484 CA GLY C 204 100.115 32.691 129.118 1.00 42.70 ATOM 2485 C GLY C 204 100.151 33.673 127.964 1.00 41.41 ATOM 2486 O GLY C 204 100.620 33.346 126.881 1.00 40.04 ATOM 2487 N GLY C 205 99.643 34.880 128.208 1.00 41.20 ATOM 2488 CA GLY C 205 99.614 35.913 127.187 1.00 40.95 ATOM 2489 C GLY C 205 98.808 35.575 125.942 1.00 40.36 ATOM 2490 O GLY C 205 97.720 34.998 126.017 1.00 40.49 ATOM 2491 N TYR C 206 99.347 35.947 124.788 1.00 39.57 ATOM 2492 CA TYR C 206 98.691 35.683 123.515 1.00 38.69 ATOM 2493 CB TYR C 206 97.467 36.589 123.351 1.00 38.68 ATOM 2494 CG TYR C 206 97.801 38.060 123.281 1.00 38.74 ATOM 2495 CD1 TYR C 206 97.668 38.872 124.401 1.00 39.11 ATOM 2496 CE1 TYR C 206 97.957 40.217 124.339 1.00 39.50 ATOM 2497 CD2 TYR C 206 98.243 38.640 122.091 1.00 36.73 ATOM 2498 CE2 TYR C 206 98.538 39.973 122.022 1.00 37.36 ATOM 2499 CZ TYR C 206 98.393 40.761 123.148 1.00 40.01 ATOM 2500 OH TYR C 206 98.697 42.101 123.097 1.00 43.16 ATOM 2501 C TYR C 206 99.645 35.889 122.340 1.00 37.30 ATOM 2502 O TYR C 206 100.583 36.671 122.431 1.00 38.54 ATOM 2503 N LYS C 207 99.392 35.194 121.234 1.00 36.45 ATOM 2504 CA LYS C 207 100.237 35.300 120.046 1.00 36.87 ATOM 2505 CB LYS C 207 100.591 33.907 119.504 1.00 32.85 ATOM 2506 C LYS C 207 99.576 36.098 118.934 1.00 37.95 ATOM 2507 O LYS C 207 98.397 35.915 118.639 1.00 38.31 ATOM 2508 N VAL C 208 100.349 36.981 118.313 1.00 40.05 ATOM 2509 CA VAL C 208 99.850 37.796 117.207 1.00 41.07 ATOM 2510 CD VAL C 208 100.060 39.307 117.460 1.00 38.91 ATOM 2511 CG1 VAL C 208 99.653 40.100 116.237 1.00 38.42 ATOM 2512 CG2 VAL C 208 99.241 39.748 118.642 1.00 40.22 ATOM 2513 C VAL C 208 100.572 37.437 115.910 1.00 42.48 ATOM 2514 O VAL C 208 101.672 37.921 115.663 1.00 43.10 ATOM 2515 N ARG C 209 99.971 36.577 115.089 1.00 44.16 ATOM 2516 CA ARG C 209 100.587 36.204 113.811 1.00 45.44 ATOM 2517 CB ARG C 209 100.056 34.853 113.305 1.00 43.55 ATOM 2518 C ARG C 209 100.231 37.313 112.816 1.00 46.48 ATOM 2519 O ARG C 209 99.090 37.393 112.346 1.00 46.30 ATOM 2520 N TYR C 210 101.210 38.169 112.512 1.00 46.88 ATOM 2521 CA TYR C 210 101.003 39.299 111.605 1.00 46.66 ATOM 2522 CB TYR C 210 102.192 40.265 111.627 1.00 49.05 ATOM 2523 CG TYR C 210 102.532 40.780 113.008 1.00 54.11 ATOM 2524 CD1 TYR C 210 103.331 40.028 113.876 1.00 56.13 ATOM 2525 CE1 TYR C 210 103.602 40.468 115.170 1.00 57.60 ATOM 2526 CD2 TYR C 210 102.013 41.997 113.473 1.00 55.77 ATOM 2527 CE2 TYR C 210 102.275 42.447 114.765 1.00 57.07 ATOM 2528 CZ TYR C 210 103.069 41.676 115.608 1.00 58.31 ATOM 2529 OH TYR C 210 103.321 42.107 116.892 1.00 60.81 ATOM 2530 C TYR C 210 100.768 38.868 110.191 1.00 44.74 ATOM 2531 O TYR C 210 100.074 39.547 109.441 1.00 45.31 ATOM 2532 N ALA C 211 101.361 37.744 109.818 1.00 43.76 ATOM 2533 CA ALA C 211 101.194 37.231 108.471 1.00 43.74 ATOM 2534 CB ALA C 211 102.120 36.057 108.252 1.00 43.87 ATOM 2535 C ALA C 211 99.740 36.812 108.266 1.00 43.16 ATOM 2536 O ALA C 211 99.255 36.747 107.144 1.00 42.29 ATOM 2537 N THR C 212 99.052 36.548 109.370 1.00 44.47 ATOM 2538 CA THR C 212 97.652 36.126 109.351 1.00 45.66 ATOM 2539 CB THR C 212 97.380 34.968 110.343 1.00 48.23 ATOM 2540 OG1 THR C 212 98.597 34.273 110.634 1.00 52.50 ATOM 2541 CG2 THR C 212 96.351 34.000 109.770 1.00 49.52 ATOM 2542 C THR C 212 96.712 37.246 109.780 1.00 44.59 ATOM 2543 O THR C 212 95.491 37.092 109.704 1.00 45.13 ATOM 2544 N TRP C 213 97.268 38.352 110.263 1.00 42.58 ATOM 2545 CA TRP C 213 96.436 39.456 110.703 1.00 40.90 ATOM 2546 CB TRP C 213 95.598 39.986 109.537 1.00 42.74 ATOM 2547 CG TRP C 213 96.411 40.547 108.437 1.00 42.12 ATOM 2548 CD2 TRP C 213 97.005 41.842 108.402 1.00 41.92 ATOM 2549 CE2 TRP C 213 97.714 41.942 107.187 1.00 42.84 ATOM 2550 CE3 TRP C 213 97.007 42.934 109.281 1.00 41.10 ATOM 2551 CD1 TRP C 213 96.767 39.924 107.281 1.00 42.59 ATOM 2552 NE1 TRP C 213 97.552 40.756 106.521 1.00 43.69 ATOM 2553 CZ2 TRP C 213 98.421 43.089 106.824 1.00 43.35 ATOM 2554 CZ3 TRP C 213 97.705 44.075 108.925 1.00 42.32 ATOM 2555 CH2 TRP C 213 98.405 44.145 107.704 1.00 43.55 ATOM 2556 C TRP C 213 95.508 38.954 111.788 1.00 39.39 ATOM 2557 O TRP C 213 94.321 39.294 111.817 1.00 38.02 ATOM 2558 N SER C 214 96.040 38.138 112.684 1.00 38.04 ATOM 2559 CA SER C 214 95.195 37.612 113.735 1.00 38.52 ATOM 256O CB SER C 214 94.704 36.209 113.366 1.00 38.63 ATOM 2561 OG SER C 214 95.787 35.308 113.243 1.00 40.15 ATOM 2562 C SER C 214 95.831 37.588 115.109 1.00 37.44 ATOM 2563 O SER C 214 97.045 37.753 115.254 1.00 38.93 ATOM 2564 N ILE C 215 94.981 37.411 116.116 1.00 34.80 ATOM 2565 CA ILE C 215 95.423 37.335 117.497 1.00 32.54 ATOM 2566 CB ILE C 215 94.881 38.482 118.343 1.00 30.76 ATOM 2567 CG2 ILE C 215 93.351 38.494 118.285 1.00 27.37 ATOM 2568 CG1 ILE C 215 95.424 38.341 119.765 1.00 29.21 ATOM 2569 CD1 ILE C 215 95.232 39.566 120.634 1.00 31.69 ATOM 2570 C ILE C 215 94.872 36.034 118.044 1.00 32.55 ATOM 2571 O ILE C 215 93.739 35.654 117.753 1.00 32.98 ATOM 2572 N ILE C 216 95.670 35.347 118.843 1.00 30.59 ATOM 2573 CA ILE C 216 95.235 34.079 119.385 1.00 27.26 ATOM 2574 CB ILE C 216 96.011 32.945 118.732 1.00 27.82 ATOM 2575 CG2 ILE C 216 95.489 31.617 119.218 1.00 26.00 ATOM 2576 CG1 ILE C 216 95.889 33.072 117.210 1.00 30.26 ATOM 2577 CD1 ILE C 216 96.663 32.040 116.427 1.00 32.20 ATOM 2578 C ILE C 216 95.389 33.985 120.882 1.00 25.63 ATOM 2579 O ILE C 216 96.407 34.373 121.444 1.00 24.12 ATOM 2580 N MET C 217 94.357 33.482 121.533 1.00 25.01 ATOM 2581 CA MET C 217 94.405 33.312 122.968 1.00 26.49 ATOM 2582 CB MET C 217 93.450 34.270 123.668 1.00 25.10 ATOM 2583 CG MET C 217 93.780 35.714 123.453 1.00 26.08 ATOM 2584 SD MET C 217 92.719 36.763 124.435 1.00 28.69 ATOM 2585 CE MET C 217 91.386 36.979 123.321 1.00 29.90 ATOM 2586 C MET C 217 94.076 31.869 123.333 1.00 28.23 ATOM 2587 O MET C 217 93.113 31.271 122.843 1.00 28.32 ATOM 2588 N ASP C 218 94.910 31.300 124.190 1.00 29.55 ATOM 2589 CA ASP C 218 94.711 29.935 124.632 1.00 28.10 ATOM 2590 CB ASP C 218 96.044 29.248 124.890 1.00 26.11 ATOM 2591 CG ASP C 218 96.745 28.854 123.626 1.00 27.42 ATOM 2592 OD1 ASP C 218 96.054 28.374 122.698 1.00 25.60 ATOM 2593 OD2 ASP C 218 97.991 29.006 123.570 1.00 30.13 ATOM 2594 C ASP C 218 93.894 29.944 125.912 1.00 28.61 ATOM 2595 O ASP C 218 93.813 30.969 126.595 1.00 27.04 ATOM 2596 N SER C 219 93.297 28.793 126.224 1.00 29.67 ATOM 2597 CA SER C 219 92.480 28.607 127.425 1.00 29.41 ATOM 2598 CB SER C 219 93.314 27.972 128.534 1.00 29.13 ATOM 2599 OG SER C 219 92.485 27.653 129.642 1.00 30.01 ATOM 2600 C SER C 219 91.818 29.873 127.972 1.00 29.79 ATOM 2601 O SER C 219 92.176 30.372 129.041 1.00 27.97 ATOM 2602 N VAL C 220 90.829 30.374 127.239 1.00 31.22 ATOM 2603 CA VAL C 220 90.109 31.577 127.631 1.00 30.62 ATOM 2604 CB VAL C 220 89.239 32.075 126.481 1.00 27.62 ATOM 2605 CG1 VAL C 220 90.109 32.616 125.378 1.00 26.20 ATOM 2606 CG2 VAL C 220 88.413 30.946 125.956 1.00 29.75 ATOM 2607 C VAL C 220 89.235 31.393 128.870 1.00 31.94 ATOM 2608 O VAL C 220 88.472 30.434 128.994 1.00 32.79 ATOM 2609 N VAL C 221 89.353 32.334 129.791 1.00 32.13 ATOM 2610 CA VAL C 221 88.586 32.293 131.022 1.00 31.92 ATOM 2611 CB VAL C 221 89.533 32.287 132.267 1.00 31.72 ATOM 2612 CG1 VAL C 221 90.534 31.137 132.175 1.00 29.53 ATOM 2613 CG2 VAL C 221 90.269 33.608 132.365 1.00 31.11 ATOM 2614 C VAL C 221 87.682 33.537 131.046 1.00 32.11 ATOM 2615 O VAL C 221 87.858 34.446 130.229 1.00 31.15 ATOM 2616 N PRO C 222 86.707 33.597 131.982 1.00 31.23 ATOM 2617 CD PRO C 222 86.345 32.563 132.966 1.00 30.92 ATOM 2618 CA PRO C 222 85.784 34.731 132.105 1.00 30.47 ATOM 2619 CB PRO C 222 85.070 34.457 133.419 1.00 27.58 ATOM 2620 CG PRO C 222 84.953 33.014 133.399 1.00 29.80 ATOM 2621 C PRO C 222 86.424 36.114 132.096 1.00 31.43 ATOM 2622 O PRO C 222 85.848 37.055 131.548 1.00 30.86 ATOM 2623 N SER C 223 87.598 36.255 132.711 1.00 32.22 ATOM 2624 CA SER C 223 88.256 37.560 132.730 1.00 31.94 ATOM 2625 CB SER C 223 89.503 37.548 133.644 1.00 31.67 ATOM 2626 OG SER C 223 90.516 36.649 133.212 1.00 30.71 ATOM 2627 C SER C 223 88.619 38.009 131.305 1.00 32.23 ATOM 2628 O SER C 223 88.892 39.179 131.070 1.00 31.36 ATOM 2629 N ASP C 224 88.609 37.078 130.357 1.00 31.98 ATOM 2630 CA ASP C 224 88.912 37.412 128.978 1.00 32.72 ATOM 2631 CB ASP C 224 89.340 36.169 128.201 1.00 35.56 ATOM 2632 CG ASP C 224 90.740 35.736 128.537 1.00 37.51 ATOM 2633 OD1 ASP C 224 91.622 36.618 128.591 1.00 40.81 ATOM 2634 OD2 ASP C 224 90.964 34.525 128.736 1.00 37.64 ATOM 2635 C ASP C 224 87.691 38.002 128.312 1.00 32.18 ATOM 2636 O ASP C 224 87.799 38.675 127.298 1.00 32.48 ATOM 2637 N LYS C 225 86.521 37.725 128.872 1.00 31.98 ATOM 2638 CA LYS C 225 85.277 38.234 128.315 1.00 32.69 ATOM 2639 CB LYS C 225 84.128 38.037 129.314 1.00 33.13 ATOM 2640 CG LYS C 225 83.573 36.610 129.425 1.00 33.78 ATOM 2641 CD LYS C 225 82.107 36.644 129.872 1.00 33.61 ATOM 2642 CE LYS C 225 81.925 36.311 131.357 1.00 38.01 ATOM 2643 NZ LYS C 225 80.529 36.606 131.836 1.00 38.05 ATOM 2644 C LYS C 225 85.408 39.717 127.988 1.00 32.99 ATOM 2645 O LYS C 225 85.896 40.488 128.809 1.00 33.98 ATOM 26A6 H GLY C 226 84.979 40.124 126.798 1.00 32.15 ATOM 2647 CA GLY C 226 85.061 41.534 126.458 1.00 33.00 ATOM 2648 C GLY C 226 85.066 41.804 124.975 1.00 33.41 ATOM 2649 O GLY C 226 84.796 40.901 124.187 1.00 34.91 ATOM 2650 N ASN C 227 85.356 43.047 124.590 1.00 32.62 ATOM 2651 CA ASN C 227 85.419 43.406 123.176 1.00 31.01 ATOM 2652 CB ASN C 227 84.675 44.697 122.893 1.00 29.69 ATOM 2653 CG ASN C 227 83.219 44.595 123.210 1.00 28.50 ATOM 2654 OD1 ASN C 227 82.577 43.587 122.913 1.00 29.98 ATOM 2655 HD2 ASN C 227 82.675 45.642 123.808 1.00 25.67 ATOM 2656 C ASN C 227 86.855 43.576 122.730 1.00 31.54 ATOM 2657 O ASN C 227 87.668 44.181 123.411 1.00 33.57 ATOM 2658 H TYR C 228 87.173 43.027 121.576 1.00 31.42 ATOM 2659 CA TYR C 228 88.518 43.142 121.065 1.00 32.10 ATOM 2660 CB TYR C 228 89.162 41.765 120.962 1.00 31.62 ATOM 2661 CG TYR C 228 89.273 41.070 122.288 1.00 32.41 ATOM 2662 CD1 TYR C 228 88.138 40.585 122.954 1.00 32.91 ATOM 2663 CE1 TYR C 228 88.249 39.954 124.207 1.00 34.77 ATOM 2664 CD2 TYR C 228 90.516 40.912 122.899 1.00 34.65 ATOM 2665 CE2 TYR C 228 90.645 40.291 124.145 1.00 34.81 ATOM 2666 CZ TYR C 228 89.515 39.813 124.791 1.00 35.79 ATOM 2667 OH TYR C 228 89.674 39.179 126.001 1.00 36.37 ATOM 2668 C TYR C 228 88.426 43.807 119.707 1.00 32.91 ATOM 2669 O TYR C 228 87.634 43.397 118.852 1.00 31.39 ATOM 2670 N THR C 229 89.237 44.845 119.530 1.00 33.31 ATOM 2671 CA THR C 229 89.262 45.624 118.303 1.00 31.06 ATOM 2672 CB THR C 229 88.956 47.081 118.595 1.00 29.65 ATOM 2673 OG1 THR C 229 87.603 47.198 119.047 1.00 29.25 ATOM 2674 CG2 THR C 229 89.186 47.917 117.359 1.00 28.81 ATOM 2675 C THR C 229 90.608 45.585 117.622 1.00 29.85 ATOM 2676 O THR C 229 91.630 45.805 118.253 1.00 28.08 ATOM 2677 H CYS C 230 90.608 45.304 116.329 1.00 31.21 ATOM 2678 CA CYS C 230 91.852 45.282 115.586 1.00 31.56 ATOM 2679 C CYS C 230 91.929 46.617 114.874 1.00 31.07 ATOM 2680 O CYS C 230 90.911 47.161 114.443 1.00 30.73 ATOM 2681 CB CYS C 230 91.872 44.139 114.569 1.00 31.93 ATOM 2682 SG CYS C 230 90.535 44.169 113.337 1.00 29.76 ATOM 2683 N ILE C 231 93.135 47.156 114.784 1.00 31.08 ATOM 2684 CA ILE C 231 93.350 48.429 114.116 1.00 31.36 ATOM 2685 CB ILE C 231 93.746 49.525 115.108 1.00 29.07 ATOM 2686 CG2 ILE C 231 94.013 50.819 114.386 1.00 26.48 ATOM 2687 CG1 ILE C 231 92.615 49.733 116.096 1.00 29.41 ATOM 2688 CD1 ILE C 231 92.982 50.640 117.222 1.00 32.64 ATOM 2689 C ILE C 231 94.459 48.265 113.097 1.00 33.74 ATOM 2690 O ILE C 231 95.646 48.143 113.450 1.00 34.89 ATOM 2691 H VAL C 232 94.055 48.227 111.831 1.00 34.68 ATOM 2692 CA VAL C 232 94.992 48.101 110.726 1.00 35.66 ATOM 2693 CB VAL C 232 94.437 47.244 109.614 1.00 34.43 ATOM 2694 CG1 VAL C 232 95.526 46.993 108.601 1.00 35.90 ATOM 2695 CG2 VAL C 232 93.887 45.966 110.174 1.00 31.80 ATOM 2696 C VAL C 232 95.174 49.498 110.184 1.00 37.27 ATOM 2697 O VAL C 232 94.204 50.168 109.831 1.00 37.78 ATOM 2698 N GLU C 233 96.413 49.945 110.094 1.00 39.96 ATOM 2699 CA GLU C 233 96.627 51.299 109.626 1.00 41.82 ATOM 2700 CB GLU C 233 96.523 52.239 110.825 1.00 42.88 ATOM 2701 CG GLU C 233 96.386 53.679 110.443 1.00 48.56 ATOM 2702 CD GLU C 233 96.259 54.578 111.642 1.00 51.10 ATOM 2703 OE1 GLU C 233 96.017 54.054 112.756 1.00 52.31 ATOM 2704 OE2 GLU C 233 96.393 55.810 111.457 1.00 53.25 ATOM 2705 C GLU C 233 97.930 51.572 108.876 1.00 40.67 ATOM 2706 O GLU C 233 98.935 50.889 109.076 1.00 40.71 ATOM 2707 N ASN C 234 97.879 52.567 107.994 1.00 39.72 ATOM 2708 CA ASN C 234 99.038 53.019 107.234 1.00 39.29 ATOM 2709 CB ASN C 234 99.203 52.272 105.884 1.00 36.35 ATOM 2710 CG ASN C 234 98.347 52.840 104.748 1.00 35.20 ATOM 2711 OD1 ASN C 234 97.750 53.905 104.859 1.00 33.07 ATOM 2712 ND2 ASN C 234 98.308 52.115 103.631 1.00 32.78 ATOM 2713 C ASN C 234 98.869 54.523 107.039 1.00 40.78 ATOM 2714 O ASN C 234 97.893 55.102 107.524 1.00 40.10 ATOM 2715 N GLU C 235 99.811 55.157 106.346 1.00 42.64 ATOM 2716 CA GLU C 235 99.763 56.606 106.133 1.00 42.97 ATOM 2717 CB GLU C 235 100.978 57.068 105.324 1.00 43.47 ATOM 2718 C GLU C 235 98.504 57.169 105.475 1.00 43.42 ATOM 2719 O GLU C 235 98.195 58.340 105.654 1.00 43.34 ATOM 2720 N TYR C 236 97.765 56.358 104.726 1.00 43.63 ATOM 2721 CA TYR C 236 96.581 56.882 104.050 1.00 43.35 ATOM 2722 CB TYR C 236 96.621 56.480 102.576 1.00 46.25 ATOM 2723 CG TYR C 236 97.982 56.709 101.961 1.00 49.41 ATOM 2724 CD1 TYR C 236 98.907 55.671 101.869 1.00 52.22 ATOM 2725 CE1 TYR C 236 100.179 55.882 101.350 1.00 54.00 ATOM 2726 CD2 TYR C 236 98.367 57.975 101.515 1.00 51.14 ATOM 2727 CE2 TYR C 236 99.643 58.202 100.994 1.00 52.30 ATOM 2728 CZ TYR C 236 100.543 57.152 100.917 1.00 54.30 ATOM 2729 OH TYR C 236 101.814 57.362 100.425 1.00 54.97 ATOM 2730 C TYR C 236 95.221 56.534 104.650 1.00 40.94 ATOM 2731 O TYR C 236 94.185 56.933 104.119 1.00 38.63 ATOM 2732 N GLY C 237 95.223 55.805 105.759 1.00 39.11 ATOM 2733 CA GLY C 237 93.969 55.451 106.390 1.00 37.11 ATOM 2734 C GLY C 237 94.078 54.300 107.367 1.00 36.57 ATOM 2735 O GLY C 237 95.119 53.650 107.478 1.00 36.30 ATOM 2736 N SER C 238 92.991 54.060 108.093 1.00 34.87 ATOM 2737 CA SER C 238 92.943 52.974 109.054 1.00 33.24 ATOM 2738 CB SER C 238 93.251 53.476 110.455 1.00 33.21 ATOM 2739 OG SER C 238 92.087 54.057 111.007 1.00 35.23 ATOM 2740 C SER C 238 91.552 52.375 109.074 1.00 31.13 ATOM 2741 O SER C 238 90.561 53.055 108.830 1.00 28.33 ATOM 2742 N ILE C 239 91.490 51.091 109.376 1.00 30.79 ATOM 2743 CA ILE C 239 90.224 50.401 109.467 1.00 30.00 ATOM 2744 CB ILE C 239 89.998 49.504 108.250 1.00 26.28 ATOM 2745 CG2 ILE C 239 89.705 50.375 107.026 1.00 25.43 ATOM 2746 CG1 ILE C 239 91.213 48.613 108.015 1.00 18.70 ATOM 2747 CD1 ILE C 239 90.999 47.657 106.886 1.00 13.24 ATOM 2748 C ILE C 239 90.284 49.581 110.735 1.00 31.43 ATOM 2749 O ILE C 239 91.370 49.232 111.196 1.00 33.06 ATOM 2750 N ASN C 240 89.122 49.296 111.309 1.00 31.88 ATOM 2751 CA ASN C 240 89.041 48.532 112.542 1.00 31.51 ATOM 2752 CB ASN C 240 88.890 49.482 113.707 1.00 31.92 ATOM 2753 CG ASN C 240 87.635 50.313 113.602 1.00 33.22 ATOM 2754 OD1 ASN C 240 87.546 51.386 114.171 1.00 36.26 ATOM 2755 ND2 ASN C 240 86.650 49.812 112.879 1.00 35.73 ATOM 2756 C ASN C 240 87.845 47.603 112.516 1.00 32.00 ATOM 2757 O ASN C 240 86.911 47.795 111.743 1.00 31.13 ATOM 2758 N HIS C 241 87.879 46.594 113.372 1.00 33.09 ATOM 2759 CA HIS C 241 86.787 45.644 113.468 1.00 32.20 ATOM 276O CB HIS C 241 86.966 44.490 112.495 1.00 30.92 ATOM 2761 CG HIS C 241 85.779 43.585 112.436 1.00 31.46 ATOM 2762 CD2 HIS C 241 85.618 42.298 112.820 1.00 31.42 ATOM 2763 ND1 HIS C 241 84.557 43.998 111.949 1.00 28.62 ATOM 2764 CE1 HIS C 241 83.697 43.000 112.033 1.00 31.53 ATOM 2765 NE2 HIS C 241 84.314 41.957 112.559 1.00 31.80 ATOM 2766 C HIS C 241 86.795 45.107 114.874 1.00 31.49 ATOM 2767 O HIS C 241 87.848 44.785 115.406 1.00 32.43 ATOM 2768 N THR C 242 85.622 45.014 115.479 1.00 31.45 ATOM 2769 CA THR C 242 85.524 44.527 116.846 1.00 30.81 ATOM 2770 CB THR C 242 84.785 45.552 117.735 1.00 28.87 ATOM 2771 OG1 THR C 242 85.412 46.832 117.606 1.00 27.00 ATOM 2772 CG2 THR C 242 84.819 45.127 119.192 1.00 27.19 ATOM 2773 C THR C 242 84.806 43.180 116.943 1.00 31.09 ATOM 2774 O THR C 242 83.851 42.911 116.214 1.00 32.42 ATOM 2775 N TYR C 243 85.289 42.326 117.833 1.00 30.68 ATOM 2776 CA TYR C 243 84.679 41.025 118.049 1.00 30.08 ATOM 2777 CB TYR C 243 85.686 39.910 117.798 1.00 27.63 ATOM 2778 CG TYR C 243 86.089 39.769 116.356 1.00 26.41 ATOM 2779 CD1 TYR C 243 87.388 40.043 115.951 1.00 26.64 ATOM 2780 CE1 TYR C 243 87.776 39.888 114.621 1.00 25.57 ATOM 2781 CD2 TYR C 243 85.176 39.337 115.392 1.00 25.87 ATOM 2782 CE2 TYR C 243 85.553 39.179 114.064 1.00 23.60 ATOM 2783 CZ TYR C 243 86.856 39.458 113.687 1.00 24.34 ATOM 2784 OH TYR C 243 87.247 39.325 112.372 1.00 26.49 ATOM 2785 C TYR C 243 84.232 40.988 119.497 1.00 31.15 ATOM 2786 O TYR C 243 84.794 41.674 120.350 1.00 33.46 ATOM 2787 N GLN C 244 83.210 40.208 119.786 1.00 30.47 ATOM 2788 CA GLN C 244 82.761 40.129 121.150 1.00 31.36 ATOM 2789 CB GLN C 244 81.272 40.406 121.229 1.00 35.16 ATOM 2790 CG GLN C 244 80.774 40.695 122.627 1.00 42.83 ATOM 2791 CD GLN C 244 79.267 40.912 122.649 1.00 49.87 ATOM 2792 OE1 GLN C 244 78.681 41.359 121.649 1.00 51.89 ATOM 2793 NE2 GLN C 244 78.630 40.611 123.786 1.00 50.55 ATOM 2794 C GLN C 244 83.049 38.728 121.622 1.00 30.33 ATOM 2795 O GLN C 244 82.662 37.760 120.966 1.00 29.04 ATOM 2796 N LEU C 245 83.760 38.617 122.740 1.00 28.79 ATOM 2797 CA LEU C 245 84.066 37.312 123.296 1.00 28.04 ATOM 2798 CB LEU C 245 85.542 37.191 123.673 1.00 26.24 ATOM 2799 CG LEU C 245 85.901 35.821 124.266 1.00 25.15 ATOM 2800 CD1 LEU C 245 85.824 34.789 123.168 1.00 24.09 ATOM 2801 CD2 LEU C 245 87.290 35.826 124.892 1.00 25.19 ATOM 2802 C LEU C 245 83.220 37.063 124.531 1.00 28.41 ATOM 2803 O LEU C 245 83.077 37.919 125.405 1.00 27.19 ATOM 2804 N ASP C 246 82.634 35.882 124.581 1.00 30.12 ATOM 2805 CA ASP C 246 81.841 35.511 125.725 1.00 32.19 ATOM 2806 CB ASP C 246 80.360 35.611 125.400 1.00 32.80 ATOM 2807 CG ASP C 246 79.522 35.787 126.639 1.00 35.79 ATOM 2808 OD1 ASP C 246 78.374 36.272 126.521 1.00 37.26 ATOM 2809 OD2 ASP C 246 80.024 35.437 127.733 1.00 34.78 ATOM 2810 C ASP C 246 82.235 34.087 126.091 1.00 33.34 ATOM 2811 O ASP C 246 82.141 33.174 125.259 1.00 32.58 ATOM 2812 N VAL C 247 82.721 33.910 127.321 1.00 33.68 ATOM 2813 CA VAL C 247 83.135 32.590 127.788 1.00 32.59 ATOM 2814 CB VAL C 247 84.548 32.619 128.391 1.00 32.83 ATOM 2815 CG1 VAL C 247 84.938 31.224 128.835 1.00 32.26 ATOM 2816 CG2 VAL C 247 85.545 33.148 127.367 1.00 31.39 ATOM 2817 C VAL C 247 82.163 32.034 128.817 1.00 32.34 ATOM 2818 O VAL C 247 81.802 32.716 129.780 1.00 31.84 ATOM 2819 N VAL C 248 81.733 30.795 128.597 1.00 32.98 ATOM 2820 CA VAL C 248 80.793 30.136 129.498 1.00 33.49 ATOM 2821 CB VAL C 248 79.570 29.572 128.717 1.00 33.49 ATOM 2822 CG1 VAL C 248 78.692 28.737 129.622 1.00 33.78 ATOM 2823 CG2 VAL C 248 78.752 30.704 128.162 1.00 36.10 ATOM 2824 C VAL C 248 81.458 28.998 130.262 1.00 33.28 ATOM 2825 O VAL C 248 82.100 28.134 129.666 1.00 33.59 ATOM 2826 N GLU C 249 81.324 29.013 131.584 1.00 33.31 ATOM 2827 CA GLU C 249 81.876 27.943 132.412 1.00 34.53 ATOM 2828 CB GLU C 249 82.331 28.482 133.770 1.00 34.33 ATOM 2829 CG GLU C 249 83.429 29.528 133.694 1.00 37.57 ATOM 2830 CD GLU C 249 83.898 30.034 135.071 1.00 38.93 ATOM 2831 OE1 GLU C 249 83.103 30.664 135.805 1.00 38.35 ATOM 2832 OE2 GLU C 249 85.077 29.807 135.417 1.00 40.90 ATOM 2833 C GLU C 249 80.740 26.947 132.609 1.00 34.31 ATOM 2834 O GLU C 249 79.685 27.308 133.124 1.00 37.50 ATOM 2835 N ARG C 250 80.952 25.708 132.187 1.00 33.96 ATOM 2836 CA ARG C 250 79.945 24.657 132.297 1.00 35.77 ATOM 2837 CB ARG C 250 80.162 23.628 131.165 1.00 34.20 ATOM 2838 CG ARG C 250 80.369 24.218 129.755 1.00 30.74 ATOM 2839 CD ARG C 250 79.167 25.049 129.300 1.00 28.69 ATOM 2840 NE ARG C 250 77.936 24.261 129.347 1.00 29.35 ATOM 2841 CZ ARG C 250 77.572 23.362 128.433 1.00 29.10 ATOM 2842 NH1 ARG C 250 78.331 23.134 127.366 1.00 28.71 ATOM 2843 NH2 ARG C 250 76.470 22.648 128.615 1.00 26.65 ATOM 2844 C ARG C 250 80.054 23.962 133.658 1.00 36.77 ATOM 2845 O ARG C 250 80.513 24.537 134.629 1.00 38.20 ATOM 2846 N SER C 251 79.778 22.667 133.676 1.00 37.38 ATOM 2847 CA SER C 251 79.798 21.906 134.923 1.00 37.80 ATOM 2848 CB SER C 251 78.832 22.507 135.964 1.00 37.79 ATOM 2849 OG SER C 251 79.340 23.672 136.592 1.00 37.54 ATOM 2850 C SER C 251 79.318 20.502 134.627 1.00 37.89 ATOM 2851 O SER C 251 78.154 20.183 134.867 1.00 38.84 ATOM 2852 N PRO C 252 80.198 19.648 134.096 1.00 37.82 ATOM 2853 CD PRO C 252 81.504 19.973 133.497 1.00 38.36 ATOM 2854 CA PRO C 252 79.799 18.277 133.785 1.00 37.98 ATOM 2855 CB PRO C 252 80.842 17.841 132.759 1.00 38.53 ATOM 2856 CG PRO C 252 82.055 18.608 133.169 1.00 38.58 ATOM 2857 C PRO C 252 79.719 17.357 134.998 1.00 38.19 ATOM 2858 O PRO C 252 80.529 16.450 135.177 1.00 37.38 ATOM 2859 N HIS C 253 78.726 17.613 135.838 1.00 39.36 ATOM 2860 CA HIS C 253 78.491 16.799 137.023 1.00 40.22 ATOM 2861 CB HIS C 253 79.254 17.347 138.247 1.00 41.83 ATOM 2862 CG HIS C 253 78.984 18.791 138.548 1.00 44.50 ATOM 2863 CD2 HIS C 253 79.828 19.820 138.801 1.00 45.38 ATOM 2864 ND1 HIS C 253 77.709 19.313 138.636 1.00 45.96 ATOM 2865 CE1 HIS C 253 77.783 20.602 138.926 1.00 46.89 ATOM 2866 NE2 HIS C 253 79.056 20.935 139.032 1.00 45.49 ATOM 2867 C HIS C 253 76.993 16.749 137.306 1.00 38.23 ATOM 2868 O HIS C 253 76.241 17.606 136.836 1.00 37.80 ATOM 2869 N ARG C 254 76.572 15.733 138.059 1.00 36.30 ATOM 2870 CA ARG C 254 75.168 15.556 138.421 1.00 34.25 ATOM 2871 CB ARG C 254 74.997 14.301 139.288 1.00 37.38 ATOM 2872 CG ARG C 254 75.649 14.336 140.668 1.00 39.79 ATOM 2873 CD ARG C 254 75.434 12.983 141.340 1.00 44.46 ATOM 2874 NE ARG C 254 75.468 13.019 142.806 1.00 50.17 ATOM 2875 CZ ARG C 254 76.573 13.142 143.541 1.00 53.52 ATOM 2876 NH1 ARG C 254 77.768 13.245 142.953 1.00 54.83 ATOM 2877 NH2 ARG C 254 76.483 13.154 144.871 1.00 52.76 ATOM 2878 C ARG C 254 74.654 16.786 139.158 1.00 30.25 ATOM 2879 O ARG C 254 75.437 17.596 139.622 1.00 28.91 ATOM 2880 N PRO C 255 73.323 16.940 139.276 1.00 29.24 ATOM 2881 CD PRO C 255 72.241 16.051 138.809 1.00 28.68 ATOM 2882 CA PRO C 255 72.769 18.117 139.970 1.00 28.11 ATOM 2883 CB PRO C 255 71.252 17.913 139.873 1.00 27.02 ATOM 2884 CG PRO C 255 71.093 17.022 138.647 1.00 27.40 ATOM 2885 C PRO C 255 73.237 18.283 141.416 1.00 27.39 ATOM 2886 O PRO C 255 73.644 17.323 142.068 1.00 27.72 ATOM 2887 N ILE C 256 73.187 19.515 141.902 1.00 27.12 ATOM 2888 CA ILE C 256 73.600 19.844 143.262 1.00 28.10 ATOM 2889 CB ILE C 256 74.789 20.863 143.273 1.00 28.02 ATOM 2890 CG2 ILE C 256 75.094 21.336 144.685 1.00 27.93 ATOM 2891 CG1 ILE C 256 76.019 20.237 142.642 1.00 27.41 ATOM 2892 CD1 ILE C 256 75.860 20.080 141.138 1.00 30.37 ATOM 2893 C ILE C 256 72.422 20.506 143.977 1.00 29.88 ATOM 2894 O ILE C 256 71.857 21.484 143.472 1.00 31.33 ATOM 2895 N LEU C 257 72.046 19.979 145.141 1.00 28.88 ATOM 2896 CA LEU C 257 70.948 20.565 145.906 1.00 28.81 ATOM 2897 CB LEU C 257 70.072 19.490 146.560 1.00 28.93 ATOM 2898 CG LEU C 257 69.503 18.267 145.841 1.00 29.79 ATOM 2899 CD1 LEU C 257 68.145 17.994 146.496 1.00 28.42 ATOM 2900 CD2 LEU C 257 69.358 18.471 144.328 1.00 28.81 ATOM 2901 C LEU C 257 71.543 21.420 147.022 1.00 28.68 ATOM 2902 O LEU C 257 72.554 21.050 147.619 1.00 26.80 ATOM 2903 N GLN C 258 70.930 22.563 147.316 1.00 29.62 ATOM 2904 CA GLN C 258 71.464 23.397 148.394 1.00 30.80 ATOM 2905 CB GLN C 258 70.655 24.690 148.565 1.00 26.27 ATOM 2906 C GLN C 258 71.387 22.572 149.675 1.00 31.63 ATOM 2907 O GLN C 258 70.370 21.923 149.955 1.00 33.97 ATOM 2908 N ALA C 259 72.475 22.566 150.434 1.00 31.33 ATOM 2909 CA ALA C 259 72.504 21.838 151.690 1.00 29.04 ATOM 2910 CB ALA C 259 73.877 21.924 152.309 1.00 26.39 ATOM 2911 C ALA C 259 71.488 22.494 152.615 1.00 29.26 ATOM 2912 O ALA C 259 71.310 23.715 152.578 1.00 28.97 ATOM 2913 N GLY C 260 70.814 21.687 153.430 1.00 28.01 ATOM 2914 CA GLY C 260 69.857 22.238 154.364 1.00 27.52 ATOM 2915 C GLY C 260 68.420 22.312 153.887 1.00 29.28 ATOM 2916 O GLY C 260 67.536 22.690 154.665 1.00 29.52 ATOM 2917 N LEU C 261 68.176 21.975 152.621 1.00 28.79 ATOM 2918 CA LEU C 261 66.821 21.992 152.083 1.00 27.73 ATOM 2919 CB LEU C 261 66.566 23.241 151.250 1.00 27.45 ATOM 2920 CG LEU C 261 66.738 24.596 151.931 1.00 25.25 ATOM 2921 CD1 LEU C 261 66.114 25.630 151.015 1.00 25.20 ATOM 2922 CD2 LEU C 261 66.070 24.621 153.307 1.00 20.64 ATOM 2923 C LEU C 261 66.552 20.767 151.232 1.00 28.46 ATOM 2924 O LEU C 261 67.408 20.334 150.456 1.00 29.87 ATOM 2925 N PRO C 262 65.348 20.191 151.361 1.00 28.64 ATOM 2926 CD PRO C 262 64.953 18.948 150.677 1.00 26.13 ATOM 2927 CA PRO C 262 64.280 20.653 152.254 1.00 28.75 ATOM 2928 CB PRO C 262 63.106 19.760 151.866 1.00 28.38 ATOM 2929 CG PRO C 262 63.782 18.489 151.513 1.00 27.61 ATOM 2930 C PRO C 262 64.689 20.467 153.702 1.00 28.93 ATOM 2931 O PRO C 262 65.559 19.653 154.003 1.00 31.23 ATOM 2932 N ALA C 263 64.063 21.215 154.599 1.00 29.04 ATOM 2933 CA ALA C 263 64.390 21.115 156.018 1.00 28.73 ATOM 2934 CB ALA C 263 64.586 22.507 156.600 1.00 28.57 ATOM 2935 C ALA C 263 63.294 20.393 156.778 1.00 28.84 ATOM 2936 O ALA C 263 62.130 20.427 156.390 1.00 28.55 ATOM 2937 N ASN C 264 63.665 19.728 157.859 1.00 29.84 ATOM 2938 CA ASN C 264 62.667 19.044 158.655 1.00 32.61 ATOM 2939 CB ASN C 264 63.339 18.304 159.818 1.00 32.86 ATOM 2940 CG ASN C 264 64.203 17.129 159.346 1.00 33.45 ATOM 2941 OD1 ASN C 264 63.767 16.300 158.540 1.00 33.24 ATOM 2942 ND2 ASN C 264 65.424 17.052 159.854 1.00 34.09 ATOM 2943 C ASN C 264 61.676 20.097 159.161 1.00 33.97 ATOM 2944 O ASN C 264 62.068 21.234 159.457 1.00 35.75 ATOM 2945 N LYS C 265 60.397 19.723 159.232 1.00 33.81 ATOM 2946 CA LYS C 265 59.340 20.626 159.683 1.00 32.75 ATOM 2947 CB LYS C 265 58.442 21.021 158.513 1.00 30.60 ATOM 2948 CG LYS C 265 59.151 21.251 157.207 1.00 28.61 ATOM 2949 CD LYS C 265 59.994 22.491 157.247 1.00 28.14 ATOM 2950 CE LYS C 265 59.395 23.532 156.356 1.00 29.00 ATOM 2951 HZ LYS C 265 59.110 22.963 155.024 1.00 29.54 ATOM 2952 C LYS C 265 58.452 19.952 160.715 1.00 33.94 ATOM 2953 O LYS C 265 58.007 18.829 160.506 1.00 35.83 ATOM 2954 N THR C 266 58.202 20.618 161.831 1.00 34.46 ATOM 2955 CA THR C 266 57.283 20.074 162.824 1.00 34.80 ATOM 2956 CB THR C 266 57.904 19.999 164.246 1.00 33.05 ATOM 2957 OG1 THR C 266 58.856 18.924 164.309 1.00 29.77 ATOM 2958 CG2 THR C 266 56.822 19.768 165.280 1.00 30.67 ATOM 2959 C THR C 266 56.116 21.060 162.809 1.00 36.69 ATOM 2960 O THR C 266 56.316 22.268 162.924 1.00 36.47 ATOM 2961 N VAL C 267 54.903 20.557 162.627 1.00 38.51 ATOM 2962 CA VAL C 267 53.744 21.435 162.585 1.00 41.41 ATOM 2963 CB VAL C 267 53.387 21.793 161.122 1.00 40.72 ATOM 2964 CG1 VAL C 267 54.591 22.437 160.440 1.00 40.16 ATOM 2965 CG2 VAL C 267 52.947 20.546 160.366 1.00 40.17 ATOM 2966 C VAL C 267 52.521 20.840 163.287 1.00 43.88 ATOM 2967 O VAL C 267 52.533 19.676 163.711 1.00 44.81 ATOM 2968 N ALA C 268 51.475 21.654 163.420 1.00 45.61 ATOM 2969 CA ALA C 268 50.246 21.229 164.075 1.00 46.72 ATOM 2970 CB ALA C 268 49.595 22.410 164.763 1.00 47.07 ATOM 2971 C ALA C 268 49.296 20.635 163.054 1.00 47.68 ATOM 2972 O ALA C 268 49.272 21.056 161.898 1.00 47.58 ATOM 2973 N LEU C 269 48.520 19.647 163.481 1.00 48.97 ATOM 2974 CA LEU C 269 47.563 19.008 162.593 1.00 49.91 ATOM 2975 CB LEU C 269 46.675 18.044 163.390 1.00 51.98 ATOM 2976 CG LEU C 269 45.568 17.292 162.645 1.00 54.75 ATOM 2977 CD1 LEU C 269 45.328 15.925 163.300 1.00 55.71 ATOM 2978 CD2 LEU C 269 44.290 18.139 162.639 1.00 55.58 ATOM 2979 C LEU C 269 46.721 20.087 161.923 1.00 48.50 ATOM 2980 O LEU C 269 46.225 20.987 162.584 1.00 48.65 ATOM 2981 N GLY C 270 46.592 20.016 160.607 1.00 48.14 ATOM 2982 CA GLY C 270 45.795 20.999 159.901 1.00 48.37 ATOM 2983 C GLY C 270 46.556 22.163 159.297 1.00 47.96 ATOM 2984 O GLY C 270 45.988 22.941 158.525 1.00 48.79 ATOM 2985 N SER C 271 47.834 22.285 159.632 1.00 47.43 ATOM 2986 CA SER C 271 48.664 23.371 159.109 1.00 47.85 ATOM 2987 CB SER C 271 50.043 23.337 159.769 1.00 45.66 ATOM 2988 OG SER C 271 49.938 23.210 161.171 1.00 44.73 ATOM 2989 C SER C 271 48.858 23.296 157.593 1.00 48.34 ATOM 2990 O SER C 271 48.412 22.363 156.936 1.00 48.78 ATOM 2991 N ASN C 272 49.541 24.291 157.050 1.00 48.71 ATOM 2992 CA ASN C 272 49.832 24.335 155.628 1.00 50.82 ATOM 2993 CB ASN C 272 49.206 25.563 154.969 1.00 53.33 ATOM 2994 CG ASN C 272 47.752 25.369 154.639 1.00 55.48 ATOM 2995 OD1 ASN C 272 47.377 24.398 153.983 1.00 57.95 ATOM 2996 ND2 ASN C 272 46.919 26.303 155.078 1.00 57.55 ATOM 2997 C ASN C 272 51.337 24.437 155.474 1.00 50.91 ATOM 2998 O ASN C 272 51.885 25.539 155.492 1.00 52.42 ATOM 2999 N VAL C 273 52.011 23.304 155.320 1.00 48.89 ATOM 3000 CA VAL C 273 53.459 23.323 155.167 1.00 46.82 ATOM 3001 CB VAL C 273 54.099 22.146 155.931 1.00 47.39 ATOM 3002 CG1 VAL C 273 53.438 20.863 155.529 1.00 48.39 ATOM 3003 CG2 VAL C 273 55.587 22.079 155.654 1.00 48.76 ATOM 3004 C VAL C 273 53.874 23.265 153.702 1.00 44.84 ATOM 3005 O VAL C 273 53.117 22.783 152.858 1.00 45.60 ATOM 3006 N GLU C 274 55.060 23.794 153.402 1.00 42.50 ATOM 3007 CA GLU C 274 55.591 23.756 152.042 1.00 41.08 ATOM 3008 CB GLU C 274 55.197 25.008 151.260 1.00 42.81 ATOM 3009 CG GLU C 274 55.946 26.261 151.641 1.00 48.27 ATOM 3010 CD GLU C 274 55.372 27.499 150.969 1.00 50.91 ATOM 3011 OE1 GLU C 274 54.191 27.820 151.232 1.00 52.00 ATOM 3012 OE2 GLU C 274 56.093 28.149 150.179 1.00 52.04 ATOM 3013 C GLU C 274 57.112 23.606 152.093 1.00 38.22 ATOM 3014 O GLU C 274 57.798 24.370 152.764 1.00 35.80 ATOM 3015 N PHE C 275 57.623 22.597 151.391 1.00 35.82 ATOM 3016 CA PHE C 275 59.056 22.303 151.356 1.00 32.70 ATOM 3017 CB PHE C 275 59.286 20.793 151.208 1.00 27.90 ATOM 3018 CG PHE C 275 59.061 20.007 152.468 1.00 21.37 ATOM 3019 CD1 PHE C 275 60.002 20.013 153.479 1.00 19.05 ATOM 3020 CD2 PHE C 275 57.906 19.257 152.638 1.00 18.11 ATOM 3021 CE1 PHE C 275 59.792 19.283 154.643 1.00 18.55 ATOM 3022 CE2 PHE C 275 57.693 18.532 153.790 1.00 14.62 ATOM 3023 CZ PHE C 275 58.631 18.540 154.794 1.00 15.13 ATOM 3024 C PHE C 275 59.759 22.996 150.209 1.00 32.68 ATOM 3025 O PHE C 275 59.141 23.364 149.218 1.00 33.88 ATOM 3026 N MET C 276 61.065 23.157 150.340 1.00 32.88 ATOM 3027 CA MET C 276 61.841 23.775 149.285 1.00 33.50 ATOM 3028 CB MET C 276 62.421 25.098 149.737 1.00 36.46 ATOM 3029 CG MET C 276 61.437 26.185 150.011 1.00 40.85 ATOM 3030 SD MET C 276 62.424 27.650 150.433 1.00 48.53 ATOM 3031 CE MET C 276 62.803 28.305 148.751 1.00 46.73 ATOM 3032 C MET C 276 62.922 2.884 148.870 1.00 32.74 ATOM 3033 O MET C 276 63.441 22.022 149.619 1.00 32.54 ATOM 3034 N CYS C 277 63.481 23.120 147.668 1.00 31.31 ATOM 3035 CA CYS C 277 64.604 22.364 147.154 1.00 31.22 ATOM 3036 C CYS C 277 65.294 23.247 146.119 1.00 30.72 ATOM 3037 O CYS C 277 64.716 23.566 145.078 1.00 32.01 ATOM 3038 CB CYS C 277 64.109 21.078 146.521 1.00 30.12 ATOM 3039 SG CYS C 277 65.424 19.895 146.128 1.00 31.69 ATOM 3040 N LYS C 278 66.521 23.663 146.409 1.00 28.06 ATOM 3041 CA LYS C 278 67.227 24.529 145.488 1.00 25.72 ATOM 3042 CB LYS C 278 67.877 25.677 146.277 1.00 16.91 ATOM 3043 C LYS C 278 68.234 23.684 144.690 1.00 25.74 ATOM 3044 O LYS C 278 69.202 23.148 145.236 1.00 27.31 ATOM 3045 N VAL C 279 67.981 23.552 143.392 1.00 26.14 ATOM 3046 CA VAL C 279 68.839 22.742 142.518 1.00 26.68 ATOM 3047 CB VAL C 279 67.980 21.824 141.568 1.00 24.83 ATOM 3048 CG1 VAL C 279 68.870 20.894 140.757 1.00 22.99 ATOM 3049 CG2 VAL C 279 67.001 21.015 142.373 1.00 24.61 ATOM 3050 C VAL C 279 69.777 23.563 141.644 1.00 27.32 ATOM 3051 O VAL C 279 69.516 24.726 141.342 1.00 27.26 ATOM 3052 N TYR C 280 70.881 22.940 141.252 1.00 28.89 ATOM 3053 CA TYR C 280 71.851 23.568 140.370 1.00 29.97 ATOM 3054 CB TYR C 280 73.067 24.114 141.133 1.00 31.04 ATOM 3055 CG TYR C 280 74.121 24.607 140.172 1.00 32.86 ATOM 3056 CD1 TYR C 280 73.934 25.798 139.464 1.00 34.02 ATOM 3057 CE1 TYR C 280 74.795 26.177 138.430 1.00 33.55 ATOM 3058 CD2 TYR C 280 75.215 23.806 139.834 1.00 34.24 ATOM 3059 CE2 TYR C 280 76.081 24.170 138.799 1.00 36.13 ATOM 3060 CZ TYR C 280 75.856 25.359 138.098 1.00 36.27 ATOM 3061 OH TYR C 280 76.661 25.705 137.038 1.00 38.38 ATOM 3062 C TYR C 280 72.316 22.510 139.389 1.00 30.13 ATOM 3063 O TYR C 280 72.720 21.423 139.783 1.00 31.45 ATOM 3064 N SER C 281 72.264 22.829 138.109 1.00 31.21 ATOM 3065 CA SER C 281 72.697 21.882 137.099 1.00 31.69 ATOM 3066 CB SER C 281 71.584 20.857 136.851 1.00 31.08 ATOM 3067 OG SER C 281 71.973 19.883 135.902 1.00 30.86 ATOM 3068 C SER C 281 72.988 22.660 135.827 1.00 32.60 ATOM 3069 O SER C 281 72.254 23.597 135.493 1.00 31.43 ATOM 3070 N ASP C 282 74.073 22.305 135.140 1.00 34.32 ATOM 3071 CA ASP C 282 74.388 22.971 133.887 1.00 33.65 ATOM 3072 CB ASP C 282 75.809 22.650 133.424 1.00 37.97 ATOM 3073 CG ASP C 282 76.115 23.218 132.050 1.00 41.38 ATOM 3074 OD1 ASP C 282 77.316 23.423 131.752 1.00 41.95 ATOM 3075 OD2 ASP C 282 75.159 23.450 131.268 1.00 42.76 ATOM 3076 C ASP C 282 73.341 22.389 132.946 1.00 32.33 ATOM 3077 O ASP C 282 72.436 23.100 132.516 1.00 32.71 ATOM 3078 N PRO C 283 73.425 21.083 132.633 1.00 30.93 ATOM 3079 CD PRO C 283 74.459 20.080 132.962 1.00 30.14 ATOM 3080 CA PRO C 283 72.403 20.521 131.735 1.00 29.60 ATOM 3081 CB PRO C 283 72.932 19.120 131.434 1.00 29.84 ATOM 3082 CG PRO C 283 73.752 18.782 132.662 1.00 30.68 ATOM 3083 C PRO C 283 71.070 20.487 132.474 1.00 29.59 ATOM 3084 O PRO C 283 71.050 20.319 133.691 1.00 30.32 ATOM 3085 N GLN C 284 69.959 20.638 131.757 1.00 30.43 ATOM 3086 CA GLN C 284 68.641 20.647 132.406 1.00 29.42 ATOM 3087 CB GLN C 284 67.488 20.630 131.383 1.00 29.76 ATOM 3088 CG GLN C 284 67.422 21.820 130.459 1.00 30.05 ATOM 3089 CD GLN C 284 67.326 23.142 131.189 1.00 30.62 ATOM 3090 OE1 GLN C 284 67.695 24.177 130.648 1.00 33.73 ATOM 3091 NE2 GLN C 284 66.821 23.120 132.411 1.00 31.19 ATOM 3092 C GLN C 284 68.421 19.486 133.363 1.00 28.08 ATOM 3093 O GLN C 284 68.585 18.315 133.008 1.00 26.14 ATOM 3094 N PRO C 285 68.046 19.798 134.599 1.00 27.57 ATOM 3095 CD PRO C 285 68.156 21.115 135.249 1.00 27.54 ATOM 3096 CA PRO C 285 67.802 18.754 135.589 1.00 28.78 ATOM 3097 CB PRO C 285 68.239 19.411 136.883 1.00 28.36 ATOM 3098 CG PRO C 285 67.739 20.807 136.684 1.00 28.33 ATOM 3099 C PRO C 285 66.324 18.340 135.635 1.00 29.46 ATOM 3100 O PRO C 285 65.411 19.147 135.404 1.00 29.73 ATOM 3101 N HIS C 286 66.092 17.068 135.918 1.00 30.11 ATOM 3102 CA HIS C 286 64.733 16.581 136.036 1.00 30.34 ATOM 3103 CB HIS C 286 64.560 15.233 135.345 1.00 33.50 ATOM 3104 CG HIS C 286 63.137 14.776 135.305 1.00 37.45 ATOM 3105 CD2 HIS C 286 62.003 15.439 134.980 1.00 37.57 ATOM 3106 ND1 HIS C 286 62.749 13.500 135.654 1.00 37.58 ATOM 3107 CE1 HIS C 286 61.438 13.398 135.548 1.00 37.31 ATOM 3108 NE2 HIS C 286 60.962 14.560 135.140 1.00 38.77 ATOM 3109 C HIS C 286 64.476 16.425 137.525 1.00 28.51 ATOM 3110 O HIS C 286 65.063 15.555 138.170 1.00 28.43 ATOM 3111 N ILE C 287 63.616 17.286 138.064 1.00 27.36 ATOM 3112 CA ILE C 287 63.275 17.272 139.483 1.00 24.48 ATOM 3113 CB ILE C 287 63.139 18.705 140.019 1.00 22.01 ATOM 3114 CG2 ILE C 287 62.670 18.695 141.476 1.00 18.21 ATOM 3115 CG1 ILE C 287 64.475 19.418 139.841 1.00 17.88 ATOM 3116 CD1 ILE C 287 64.419 20.889 140.118 1.00 20.45 ATOM 3117 C ILE C 287 61.986 16.506 139.743 1.00 24.82 ATOM 3118 O ILE C 287 61.117 16.418 138.877 1.00 25.02 ATOM 3119 N GLN C 288 61.869 15.960 140.948 1.00 24.37 ATOM 3120 CA GLN C 288 60.704 15.183 141.314 1.00 23.98 ATOM 3121 CB GLN C 288 60.864 13.780 140.735 1.00 23.04 ATOM 3122 CG GLN C 288 59.666 12.871 140.893 1.00 24.04 ATOM 3123 CD GLN C 288 59.859 11.546 140.180 1.00 23.43 ATOM 3124 OE1 GLN C 288 59.223 11.266 139.155 1.00 21.63 ATOM 3125 NE2 GLN C 288 60.755 10.724 140.713 1.00 23.17 ATOM 3126 C GLN C 288 60.575 15.130 142.824 1.00 22.93 ATOM 3127 O GLN C 288 61.572 15.129 143.523 1.00 24.35 ATOM 3128 N TRP C 289 59.348 15.117 143.331 1.00 23.58 ATOM 3129 CA TRP C 289 59.142 15.036 144.775 1.00 25.79 ATOM 3130 CB TRP C 289 58.254 16.175 145.295 1.00 25.56 ATOM 3131 CG TRP C 289 58.933 17.506 145.344 1.00 25.50 ATOM 3132 CD2 TRP C 289 59.645 18.069 146.455 1.00 24.57 ATOM 3133 CE2 TRP C 289 60.132 19.331 146.042 1.00 24.75 ATOM 3134 CE3 TRP C 289 59.921 17.630 147.761 1.00 24.41 ATOM 3135 CD1 TRP C 289 59.015 18.421 144.331 1.00 25.66 ATOM 3136 NE1 TRP C 289 59.731 19.520 144.743 1.00 25.92 ATOM 3137 CZ2 TRP C 289 60.881 20.161 146.883 1.00 22.40 ATOM 3138 CZ3 TRP C 289 60.665 18.451 148.600 1.00 21.27 ATOM 3139 CH2 TRP C 289 61.137 19.706 148.152 1.00 24.99 ATOM 3140 C TRP C 289 58.502 13.709 145.125 1.00 25.97 ATOM 3141 O TRP C 289 57.590 13.261 144.437 1.00 27.01 ATOM 3142 N LEU C 290 58.983 13.089 146.198 1.00 26.09 ATOM 3143 CA LEU C 290 58.471 11.801 146.643 1.00 27.29 ATOM 3144 CB LEU C 290 59.505 10.698 146.424 1.00 29.58 ATOM 3145 CG LEU C 290 59.621 10.020 145.068 1.00 31.88 ATOM 3146 CD1 LEU C 290 59.875 11.031 143.947 1.00 33.27 ATOM 3147 CD2 LEU C 290 60.752 9.027 145.170 1.00 33.26 ATOM 3148 C LEU C 290 58.156 11.790 148.111 1.00 27.39 ATOM 3149 O LEU C 290 58.697 12.586 148.875 1.00 25.52 ATOM 3150 N LYS C 291 57.264 10.885 148.498 1.00 28.19 ATOM 3151 CA LYS C 291 56.981 10.704 149.907 1.00 29.65 ATOM 3152 CB LYS C 291 55.547 10.994 150.298 1.00 29.20 ATOM 3153 CG LYS C 291 55.458 10.873 151.802 1.00 28.12 ATOM 3154 CD LYS C 291 54.082 10.971 152.347 1.00 31.10 ATOM 3155 CE LYS C 291 54.147 10.840 153.863 1.00 34.01 ATOM 3156 NZ LYS C 291 52.799 10.966 154.488 1.00 38.80 ATOM 3157 C LYS C 291 57.260 9.245 150.201 1.00 30.38 ATOM 3158 O LYS C 291 56.877 8.369 149.429 1.00 30.70 ATOM 3159 N HIS C 292 57.934 8.984 151.311 1.00 31.17 ATOM 3160 CA HIS C 292 58.255 7.617 151.683 1.00 35.38 ATOM 3161 CB HIS C 292 59.533 7.606 152.500 1.00 33.90 ATOM 3162 CG HIS C 292 60.738 7.971 151.698 1.00 33.72 ATOM 3163 CD2 HIS C 292 61.298 9.173 151.428 1.00 33.65 ATOM 3164 ND1 HIS C 292 61.463 7.042 150.986 1.00 32.94 ATOM 3165 CE1 HIS C 292 62.418 7.656 150.311 1.00 32.86 ATOM 3166 NE2 HIS C 292 62.340 8.950 150.562 1.00 33.51 ATOM 3167 C HIS C 292 57.110 6.976 152.436 1.00 38.27 ATOM 3168 O HIS C 292 56.590 7.535 153.402 1.00 39.32 ATOM 3169 N ILE C 293 56.740 5.784 151.992 1.00 40.65 ATOM 3170 CA ILE C 293 55.616 5.069 152.565 1.00 43.55 ATOM 3171 CB ILE C 293 54.598 4.875 151.447 1.00 43.18 ATOM 3172 CG2 ILE C 293 53.368 4.172 151.951 1.00 44.52 ATOM 3173 CG1 ILE C 293 54.277 6.252 150.870 1.00 43.20 ATOM 3174 CD1 ILE C 293 53.296 6.236 149.748 1.00 48.45 ATOM 3175 C ILE C 293 55.914 3.737 153.279 1.00 45.41 ATOM 3176 O ILE C 293 56.903 3.058 152.976 1.00 45.28 ATOM 3177 N GLU C 294 55.068 3.391 154.252 1.00 47.39 ATOM 3178 CA GLU C 294 55.204 2.140 155.008 1.00 50.70 ATOM 3179 CB GLU C 294 55.286 2.436 156.512 1.00 48.39 ATOM 3180 CG GLU C 294 53.959 1.310 154.706 1.00 53.03 ATOM 3181 O GLU C 294 52.850 1.754 154.971 1.00 54.66 ATOM 3182 N VAL C 295 54.138 0.104 154.172 1.00 56.24 ATOM 3183 CA VAL C 295 53.010 −0.777 153.810 1.00 59.45 ATOM 3184 CB VAL C 295 53.401 −1.659 152.576 1.00 58.62 ATOM 3185 CG1 VAL C 295 52.315 −2.666 152.255 1.00 58.90 ATOM 3186 CG2 VAL C 295 53.639 −0.773 151.363 1.00 56.91 ATOM 3187 C VAL C 295 52.538 −1.684 154.972 1.00 61.72 ATOM 3188 O VAL C 295 51.394 −2.158 155.024 1.00 61.54 ATOM 3189 N ASN C 296 53.456 −1.910 155.894 1.00 63.81 ATOM 3190 CA ASN C 296 53.269 −2.698 157.106 1.00 65.79 ATOM 3191 CB ASN C 296 53.574 −4.182 156.835 1.00 66.07 ATOM 3192 CG ASN C 296 54.812 −4.374 155.927 1.00 68.22 ATOM 3193 OD1 ASN C 296 55.165 −3.493 155.123 1.00 67.63 ATOM 3194 ND2 ASN C 296 55.463 −5.543 156.041 1.00 69.60 ATOM 3195 C ASN C 296 54.325 −2.053 157.992 1.00 66.21 ATOM 3196 O ASN C 296 54.159 −0.911 158.405 1.00 66.39 ATOM 3197 N GLY C 297 55.423 −2.736 158.269 1.00 66.33 ATOM 3198 CA GLY C 297 56.433 −2.093 159.083 1.00 65.88 ATOM 3199 C GLY C 297 57.435 −1.460 158.144 1.00 65.04 ATOM 3200 O GLY C 297 57.835 −0.300 158.298 1.00 66.23 ATOM 3201 N SER C 298 57.778 −2.241 157.125 1.00 63.11 ATOM 3202 CA SER C 298 58.756 −1.883 156.112 1.00 60.17 ATOM 3203 CB SER C 298 58.975 −3.063 155.157 1.00 60.95 ATOM 3204 OG SER C 298 57.808 −3.351 154.398 1.00 61.30 ATOM 3205 C SER C 298 58.442 −0.636 155.314 1.00 57.83 ATOM 3206 O SER C 298 57.289 −0.362 154.962 1.00 55.90 ATOM 3207 N LYS C 299 59.506 0.125 155.073 1.00 55.35 ATOM 3208 CA LYS C 299 59.459 1.354 154.298 1.00 54.04 ATOM 3209 CB LYS C 299 60.202 2.486 155.025 1.00 55.85 ATOM 3210 CG LYS C 299 59.887 2.568 156.509 1.00 58.61 ATOM 3211 CD LYS C 299 59.571 3.993 156.978 1.00 61.21 ATOM 3212 CE LYS C 299 59.026 3.968 158.416 1.00 62.47 ATOM 3213 HZ LYS C 299 58.761 5.317 158.980 1.00 62.32 ATOM 3214 C LYS C 299 60.198 0.963 153.025 1.00 51.29 ATOM 3215 O LYS C 299 60.307 1.742 152.074 1.00 52.29 ATOM 3216 N ILE C 300 60.708 −0.265 153.042 1.00 46.86 ATOM 3217 CA ILE C 300 61.421 −0.842 151.915 1.00 43.84 ATOM 3218 CB ILE C 300 62.868 −1.185 152.268 1.00 43.48 ATOM 3219 CG2 ILE C 300 63.514 −1.946 151.117 1.00 42.81 ATOM 3220 CG1 ILE C 300 63.652 0.094 152.533 1.00 43.78 ATOM 3221 CD1 ILE C 300 65.137 −0.146 152.707 1.00 45.12 ATOM 3222 C ILE C 300 60.725 −2.125 151.483 1.00 40.85 ATOM 3223 O ILE C 300 60.277 −2.900 152.316 1.00 40.80 ATOM 3224 H GLY C 301 60.653 −2.352 150.178 1.00 38.10 ATOM 3225 CA GLY C 301 59.983 −3.534 149.683 1.00 36.41 ATOM 3226 C GLY C 301 60.841 −4.689 149.202 1.00 37.19 ATOM 3227 O GLY C 301 62.071 −4.647 149.266 1.00 35.86 ATOM 3228 N PRO C 302 60.186 −5.752 148.701 1.00 37.20 ATOM 3229 CD PRO C 302 58.725 −5.710 148.469 1.00 36.58 ATOM 3230 CA PRO C 302 60.758 −6.993 148.171 1.00 35.86 ATOM 3231 CB PRO C 302 59.667 −7.492 147.240 1.00 37.20 ATOM 3232 CG PRO C 302 58.415 −7.102 147.979 1.00 36.35 ATOM 3233 C PRO C 302 62.065 −6.784 147.433 1.00 36.22 ATOM 3234 O PRO C 302 63.050 −7.480 147.677 1.00 37.38 ATOM 3235 N ASP C 303 62.053 −5.819 146.522 1.00 36.04 ATOM 3236 CA ASP C 303 63.214 −5.484 145.705 1.00 35.56 ATOM 3237 CB ASP C 303 62.766 −4.668 144.496 1.00 36.91 ATOM 3238 CG ASP C 303 62.023 −3.418 144.892 1.00 40.20 ATOM 3239 OD1 ASP C 303 61.054 −3.523 145.685 1.00 42.73 ATOM 3240 OD2 ASP C 303 62.403 −2.330 144.410 1.00 40.82 ATOM 3241 C ASP C 303 64.294 −4.712 146.450 1.00 34.79 ATOM 3242 O ASP C 303 65.356 −4.451 145.897 1.00 36.36 ATOM 3243 N ASN C 304 64.018 −4.352 147.701 1.00 33.31 ATOM 3244 CA ASN C 304 64.945 −3.589 148.552 1.00 30.86 ATOM 3245 CB ASN C 304 66.364 −4.182 148.510 1.00 29.77 ATOM 3246 CG ASN C 304 67.167 −3.841 149.758 1.00 28.46 ATOM 3247 OD1 ASN C 304 66.684 −4.013 150.879 1.00 28.50 ATOM 3248 ND2 ASN C 304 68.391 −3.362 149.572 1.00 27.02 ATOM 3249 C ASN C 304 64.993 −2.090 148.219 1.00 28.19 ATOM 3250 O ASN C 304 65.943 −1.382 148.570 1.00 26.02 ATOM 3251 N LEU C 305 63.960 −1.627 147.525 1.00 26.97 ATOM 3252 CA LEU C 305 63.822 −0.221 147.184 1.00 26.40 ATOM 3253 CB LEU C 305 63.367 −0.049 145.746 1.00 25.25 ATOM 3254 CG LEU C 305 64.444 −0.319 144.700 1.00 26.05 ATOM 3255 CD1 LEU C 305 63.876 −0.007 143.342 1.00 23.07 ATOM 3256 CD2 LEU C 305 65.682 0.533 144.969 1.00 24.19 ATOM 3257 C LEU C 305 62.744 0.305 148.108 1.00 26.14 ATOM 3258 O LEU C 305 61.854 −0.439 148.503 1.00 26.57 ATOM 3259 N PRO C 306 62.819 1.590 148.481 1.00 26.10 ATOM 3260 CD PRO C 306 63.836 2.588 148.101 1.00 25.28 ATOM 3261 CA PRO C 306 61.816 2.179 149.370 1.00 25.56 ATOM 3262 CB PRO C 306 62.455 3.501 149.762 1.00 24.30 ATOM 3263 CG PRO C 306 63.188 3.888 148.525 1.00 23.16 ATOM 3264 C PRO C 306 60.492 2.376 148.640 1.00 25.91 ATOM 3265 O PRO C 306 60.492 2.692 147.452 1.00 25.20 ATOM 3266 N TYR C 307 59.371 2.159 149.334 1.00 27.62 ATOM 3267 CA TYR C 307 58.062 2.369 148.715 1.00 28.20 ATOM 3268 CB TYR C 307 56.905 1.803 149.536 1.00 26.18 ATOM 3269 CG TYR C 307 56.993 0.348 149.908 1.00 27.94 ATOM 3270 CD1 TYR C 307 57.401 −0.026 151.188 1.00 28.66 ATOM 3271 CE1 TYR C 307 57.417 −1.348 151.585 1.00 29.63 ATOM 3272 CD2 TYR C 307 56.609 −0.658 149.011 1.00 28.66 ATOM 3273 CE2 TYR C 307 56.626 −2.010 149.395 1.00 30.48 ATOM 3274 CZ TYR C 307 57.031 −2.344 150.697 1.00 31.89 ATOM 3275 OH TYR C 307 57.041 −3.660 151.140 1.00 33.12 ATOM 3276 C TYR C 307 57.921 3.872 148.712 1.00 29.73 ATOM 3277 O TYR C 307 58.328 4.547 149.669 1.00 33.14. ATOM 3278 N VAL C 308 57.357 4.413 147.647 1.00 29.62 ATOM 3279 CA VAL C 308 57.198 5.854 147.574 1.00 30.67 ATOM 3280 CB VAL C 308 58.365 6.549 146.792 1.00 29.93 ATOM 3281 CG1 VAL C 308 59.674 6.405 147.548 1.00 27.84 ATOM 3282 CG2 VAL C 308 58.475 5.970 145.385 1.00 28.19 ATOM 3283 C VAL C 308 55.914 6.270 146.900 1.00 30.97 ATOM 3284 O VAL C 308 55.169 5.455 146.369 1.00 31.26 ATOM 3285 N GLN C 309 55.669 7.568 146.936 1.00 31.96 ATOM 3286 CA GLN C 309 54.507 8.143 146.301 1.00 32.13 ATOM 3287 CB GLN C 309 53.478 8.551 147.343 1.00 35.21 ATOM 3288 CG GLN C 309 52.068 8.678 146.790 1.00 39.73 ATOM 3289 CD GLN C 309 51.135 9.417 147.740 1.00 43.61 ATOM 3290 OE1 GLN C 309 51.085 9.130 148.951 1.00 43.88 ATOM 3291 NE2 GLN C 309 50.383 10.373 147.196 1.00 44.33 ATOM 3292 C GLN C 309 55.014 9.369 145.551 1.00 30.79 ATOM 3293 O GLN C 309 55.503 10.327 146.164 1.00 30.26 ATOM 3294 N ILE C 310 54.921 9.321 144.223 1.00 29.07 ATOM 3295 CA ILE C 310 55.371 10.426 143.383 1.00 27.14 ATOM 3296 CB ILE C 310 55.444 9.999 141.891 1.00 28.09 ATOM 3297 CG2 ILE C 310 55.996 11.139 141.033 1.00 26.15 ATOM 3298 CG1 ILE C 310 56.311 8.737 141.749 1.00 29.18 ATOM 3299 CD1 ILE C 310 57.788 8.919 142.119 1.00 28.63 ATOM 3300 C ILE C 310 54.390 11.576 143.537 1.00 25.01 ATOM 3301 O ILE C 310 53.251 11.490 143.105 1.00 25.36 ATOM 3302 N LEU C 311 54.841 12.653 144.157 1.00 24.70 ATOM 3303 CA LEU C 311 53.990 13.814 144.384 1.00 25.69 ATOM 3304 CB LEU C 311 54.337 14.445 145.727 1.00 25.71 ATOM 3305 CG LEU C 311 54.135 13.504 146.904 1.00 26.24 ATOM 3306 CD1 LEU C 311 54.581 14.187 148.192 1.00 24.44 ATOM 3307 CD2 LEU C 311 52.662 13.085 146.951 1.00 24.28 ATOM 3308 C LEU C 311 54.055 14.897 143.320 1.00 25.46 ATOM 3309 O LEU C 311 53.068 15.573 143.059 1.00 24.77 ATOM 3310 N LYS C 312 55.221 15.064 142.713 1.00 28.01 ATOM 3311 CA LYS C 312 55.423 16.101 141.708 1.00 28.31 ATOM 3312 CB LYS C 312 55.815 17.390 142.416 1.00 26.66 ATOM 3313 CG LYS C 312 55.503 18.663 141.688 1.00 27.67 ATOM 3314 CD LYS C 312 55.802 19.812 142.648 1.00 31.49 ATOM 3315 CE LYS C 312 55.176 21.138 142.240 1.00 32.20 ATOM 3316 NZ LYS C 312 55.054 22.009 143.455 1.00 34.04 ATOM 3317 C LYS C 312 56.543 15.666 140.777 1.00 29.40 ATOM 3318 O LYS C 312 57.539 15.082 141.212 1.00 29.77 ATOM 3319 N THR C 313 56.384 15.957 139.494 1.00 31.02 ATOM 3320 CA THR C 313 57.379 15.571 138.498 1.00 30.41 ATOM 3321 CB THR C 313 56.977 14.268 137.775 1.00 28.36 ATOM 3322 OG1 THR C 313 56.976 13.177 138.699 1.00 28.72 ATOM 3323 CG2 THR C 313 57.938 13.963 136.667 1.00 28.33 ATOM 3324 C THR C 313 57.455 16.660 137.455 1.00 31.24 ATOM 3325 O THR C 313 56.443 17.004 136.836 1.00 32.10 ATOM 3326 N ALA C 314 58.652 17.193 137.252 1.00 31.41 ATOM 3327 CA ALA C 314 58.833 18.251 136.280 1.00 31.45 ATOM 3328 CB ALA C 314 60.237 18.823 136.386 1.00 33.93 ATOM 3329 C ALA C 314 58.562 17.751 134.867 1.00 31.70 ATOM 3330 O ALA C 314 58.722 16.564 134.553 1.00 29.10 ATOM 3331 N GLY C 315 58.139 18.685 134.024 1.00 32.86 ATOM 3332 CA GLY C 315 57.841 18.382 132.637 1.00 32.44 ATOM 3333 C GLY C 315 56.946 19.480 132.105 1.00 33.40 ATOM 3334 O GLY C 315 56.619 20.441 132.825 1.00 31.86 ATOM 3335 N VAL C 316 56.540 19.335 130.852 1.00 34.05 ATOM 3336 CA VAL C 316 55.671 20.308 130.209 1.00 35.92 ATOM 3337 CB VAL C 316 55.232 19.778 128.842 1.00 36.34 ATOM 3338 CG1 VAL C 316 54.425 20.823 128.120 1.00 39.31 ATOM 3339 CG2 VAL C 316 56.454 19.377 128.030 1.00 35.78 ATOM 3340 C VAL C 316 54.428 20.655 131.046 1.00 37.44 ATOM 3341 O VAL C 316 53.952 21.797 131.030 1.00 37.25 ATOM 3342 N ASN C 317 53.912 19.675 131.781 1.00 39.86 ATOM 3343 CA ASN C 317 52.724 19.890 132.605 1.00 42.60 ATOM 3344 CB ASN C 317 52.032 18.554 132.889 1.00 47.26 ATOM 3345 CG ASN C 317 51.391 17.949 131.647 1.00 51.28 ATOM 3346 OD1 ASN C 317 51.088 16.742 131.617 1.00 54.31 ATOM 3347 ND2 ASN C 317 51.169 18.780 130.617 1.00 48.94 ATOM 3348 C ASN C 317 53.043 20.581 133.917 1.00 41.85 ATOM 3349 O ASN C 317 52.172 21.186 134.542 1.00 43.36 ATOM 3350 N THR C 318 54.296 20.500 134.329 1.00 41.46 ATOM 3351 CA THR C 318 54.697 21.103 135.580 1.00 41.12 ATOM 3352 CB THR C 318 54.752 20.038 136.666 1.00 40.65 ATOM 3353 OG1 THR C 318 53.820 18.998 136.341 1.00 38.74 ATOM 3354 CG2 THR C 318 54.396 20.636 138.009 1.00 40.04 ATOM 3355 C THR C 318 56.074 21.665 135.354 1.00 41.10 ATOM 3356 O THR C 318 57.071 20.983 135.577 1.00 42.97 ATOM 3357 N THR C 319 56.115 22.907 134.893 1.00 40.14 ATOM 3358 CA THR C 319 57.358 23.602 134.593 1.00 39.06 ATOM 3359 CB THR C 319 57.024 24.935 133.912 1.00 39.04 ATOM 3360 OG1 THR C 319 56.341 24.643 132.692 1.00 38.77 ATOM 3361 CG2 THR C 319 58.280 25.752 133.604 1.00 40.60 ATOM 3362 C THR C 319 58.257 23.829 135.806 1.00 38.67 ATOM 3363 O THR C 319 57.785 23.867 136.950 1.00 38.34 ATOM 3364 N ASP C 320 59.558 23.966 135.543 1.00 38.76 ATOM 3365 CA ASP C 320 60.549 24.192 136.591 1.00 38.55 ATOM 3366 CB ASP C 320 61.916 24.518 135.966 1.00 39.25 ATOM 3367 CG ASP C 320 62.509 23.331 135.169 1.00 42.22 ATOM 3368 OD1 ASP C 320 62.255 22.158 135.537 1.00 40.72 ATOM 3369 OD2 ASP C 320 63.249 23.566 134.182 1.00 43.42 ATOM 3370 C ASP C 320 60.091 25.301 137.541 1.00 39.21 ATOM 3371 O ASP C 320 60.411 25.297 138.725 1.00 39.71 ATOM 3372 N LYS C 321 59.316 26.235 137.019 1.00 40.34 ATOM 3373 CA LYS C 321 58.786 27.326 137.816 1.00 42.35 ATOM 3374 CB LYS C 321 57.611 27.978 137.065 1.00 45.75 ATOM 3375 CG LYS C 321 57.946 28.373 135.620 1.00 48.28 ATOM 3376 CD LYS C 321 56.750 28.912 134.826 1.00 47.90 ATOM 3377 CE LYS C 321 57.182 29.250 133.386 1.00 48.35 ATOM 3378 NZ LYS C 321 56.043 29.601 132.490 1.00 47.69 ATOM 3379 C LYS C 321 58.299 26.824 139.177 1.00 42.50 ATOM 3380 O LYS C 321 58.761 27.269 140.226 1.00 42.89 ATOM 3381 N GLU C 322 57.367 25.880 139.154 1.00 43.54 ATOM 3382 CA GLU C 322 56.795 25.348 140.392 1.00 44.10 ATOM 3383 CB GLU C 322 55.336 25.006 140.161 1.00 48.31 ATOM 3384 CG GLU C 322 55.136 24.231 138.883 1.00 53.89 ATOM 3385 CD GLU C 322 54.083 24.874 138.017 1.00 59.22 ATOM 3386 OE1 GLU C 322 52.923 24.926 138.477 1.00 62.81 ATOM 3387 OE2 GLU C 322 54.405 25.337 136.894 1.00 62.06 ATOM 3388 C GLU C 322 57.474 24.127 140.995 1.00 41.62 ATOM 3389 O GLU C 322 57.074 23.672 142.058 1.00 40.29 ATOM 3390 N MET C 323 58.504 23.608 140.336 1.00 40.18 ATOM 3391 CA MET C 323 59.192 22.413 140.820 1.00 39.72 ATOM 3392 CB MET C 323 59.988 21.774 139.680 1.00 39.74 ATOM 3393 CG MET C 323 59.121 21.110 138.625 1.00 39.00 ATOM 3394 SD MET C 323 57.926 20.007 139.397 1.00 39.79 ATOM 3395 CE MET C 323 59.044 18.760 140.122 1.00 39.54 ATOM 3396 C MET C 323 60.103 22.524 142.041 1.00 39.88 ATOM 3397 O MET C 323 60.452 21.507 142.639 1.00 38.86 ATOM 3398 N GLU C 324 60.482 23.738 142.421 1.00 40.42 ATOM 3399 C GLU C 324 61.373 23.914 143.557 1.00 41.47 ATOM 3400 CB GLU C 324 62.209 25.174 143.346 1.00 45.26 ATOM 3401 CG GLU C 324 63.055 25.135 142.076 1.00 50.92 ATOM 3402 CD GLU C 324 64.212 26.137 142.092 1.00 54.85 ATOM 3403 OE1 GLU C 324 63.950 27.366 142.190 1.00 54.81 ATOM 3404 OE2 GLU C 324 65.383 25.685 142.006 1.00 55.29 ATOM 3405 C GLU C 324 60.697 23.960 144.929 1.00 40.67 ATOM 3406 O GLU C 324 61.368 23.958 145.966 1.00 41.14 ATOM 3407 N VAL C 325 59.373 23.993 144.953 1.00 39.72 ATOM 3408 CA VAL C 325 58.682 24.040 146.232 1.00 38.08 ATOM 3409 CB VAL C 325 58.220 25.487 146.546 1.00 36.29 ATOM 3410 CG1 VAL C 325 57.039 25.857 145.672 1.00 36.51 ATOM 3411 CG2 VAL C 325 57.893 25.633 148.015 1.00 36.14 ATOM 3412 C VAL C 325 57.500 23.072 146.254 1.00 38.56 ATOM 3413 O VAL C 325 56.651 23.074 145.357 1.00 38.82 ATOM 3414 N LEU C 326 57.471 22.216 147.269 1.00 38.14 ATOM 3415 CA LEU C 326 56.389 21.255 147.400 1.00 37.67 ATOM 3416 CB LEU C 326 56.896 19.891 147.879 1.00 35.37 ATOM 3417 CG LEU C 326 55.745 18.891 148.008 1.00 31.23 ATOM 3418 CD1 LEU C 326 55.376 18.418 146.637 1.00 28.32 ATOM 3419 CD2 LEU C 326 56.132 17.727 148.891 1.00 31.14 ATOM 3420 C LEU C 326 55.396 21.796 148.403 1.00 37.92 ATOM 3421 O LEU C 326 55.751 22.088 149.544 1.00 36.88 ATOM 3422 N HIS C 327 54.148 21.917 147.969 1.00 39.27 ATOM 3423 CA HIS C 327 53.085 22.430 148.820 1.00 41.32 ATOM 3424 CE HIS C 327 52.188 23.363 148.021 1.00 41.71 ATOM 3425 CG HIS C 327 52.802 24.693 147.740 1.00 43.39 ATOM 3426 CD2 HIS C 327 53.144 25.288 146.573 1.00 43.33 ATOM 3427 ND1 HIS C 327 53.132 25.582 148.740 1.00 42.70 ATOM 3428 CE1 HIS C 327 53.653 26.669 148.200 1.00 43.09 ATOM 3429 NE2 HIS C 327 53.673 26.517 146.888 1.00 43.55 ATOM 3430 C HIS C 327 52.207 21.363 149.452 1.00 42.33 ATOM 3431 O HIS C 327 51.644 20.517 148.761 1.00 42.42 ATOM 3432 N LEU C 328 52.083 21.412 150.769 1.00 43.08 ATOM 3433 CA LEU C 328 51.236 20.473 151.471 1.00 45.11 ATOM 3434 CB LEU C 328 52.029 19.708 152.528 1.00 42.60 ATOM 3435 CG LEU C 328 53.090 18.732 152.010 1.00 42.77 ATOM 3436 CD1 LEU C 328 53.743 18.001 153.175 1.00 42.02 ATOM 3437 CD2 LEU C 328 52.450 17.730 151.064 1.00 41.50 ATOM 3438 C LEU C 328 50.160 21.315 152.127 1.00 48.64 ATOM 3439 O LEU C 328 50.415 21.977 153.134 1.00 49.49 ATOM 3440 N ARG C 329 48.963 21.302 151.540 1.00 51.46 ATOM 3441 CA ARG C 329 47.839 22.076 152.056 1.00 53.13 ATOM 3442 CE ARG C 329 46.903 22.470 150.913 1.00 53.63 ATOM 3443 C ARG C 329 47.057 21.332 153.132 1.00 54.77 ATOM 3444 O ARG C 329 46.577 20.220 152.916 1.00 55.60 ATOM 3445 N ASN C 330 46.942 21.963 154.296 1.00 56.97 ATOM 3446 CA ASN C 330 46.218 21.399 155.429 1.00 59.20 ATOM 3447 CE ASN C 330 44.717 21.477 155.161 1.00 60.58 ATOM 3448 CG ASN C 330 43.897 21.255 156.407 1.00 62.83 ATOM 3449 OD1 ASN C 330 44.112 20.292 157.148 1.00 63.10 ATOM 3450 ND2 ASN C 330 42.940 22.146 156.646 1.00 64.41 ATOM 3451 C ASN C 330 46.636 19.948 155.658 1.00 59.55 ATOM 3452 O ASN C 330 46.059 19.029 155.085 1.00 60.48 ATOM 3453 N VAL C 331 47.636 19.747 156.504 1.00 60.31 ATOM 3454 CA VAL C 331 48.146 18.409 156.771 1.00 60.52 ATOM 3455 CE VAL C 331 49.606 18.486 157.308 1.00 59.96 ATOM 3456 CG1 VAL C 331 50.527 19.031 156.223 1.00 58.15 ATOM 3457 CG2 VAL C 331 49.672 19.380 158.535 1.00 58.53 ATOM 3458 C VAL C 331 47.288 17.590 157.732 1.00 60.66 ATOM 3459 O VAL C 331 46.274 18.061 158.239 1.00 60.55 ATOM 3460 N SER C 332 47.709 16.354 157.960 1.00 61.41 ATOM 3461 CA SER C 332 47.022 15.436 158.852 1.00 62.88 ATOM 3462 CE SER C 332 45.915 14.709 158.101 1.00 64.75 ATOM 3463 OG SER C 332 46.449 14.058 156.962 1.00 66.80 ATOM 3464 C SER C 332 48.066 14.440 159.312 1.00 62.96 ATOM 3465 O SER C 332 49.115 14.323 158.692 1.00 63.04 ATOM 3466 N PHE C 333 47.790 13.724 160.394 1.00 64.54 ATOM 3467 CA PHE C 333 48.748 12.747 160.900 1.00 65.91 ATOM 3468 CB PHE C 333 48.126 11.899 162.011 1.00 68.96 ATOM 3469 CG PHE C 333 48.270 12.489 163.390 1.00 72.38 ATOM 3470 CD1 PHE C 333 48.503 11.654 164.493 1.00 73.39 ATOM 3471 CD2 PHE C 333 48.151 13.864 163.595 1.00 73.19 ATOM 3472 CE1 PHE C 333 48.613 12.178 165.782 1.00 74.33 ATOM 3473 CE2 PHE C 333 48.259 14.402 164.879 1.00 74.97 ATOM 3474 CZ PHE C 333 48.493 13.554 165.978 1.00 75.37 ATOM 3475 C PHE C 333 49.239 11.828 159.786 1.00 65.14 ATOM 3476 O PHE C 333 50.341 11.279 159.855 1.00 64.30 ATOM 3477 N GLU C 334 48.405 11.675 158.764 1.00 64.25 ATOM 3478 CA GLU C 334 48.708 10.831 157.615 1.00 63.39 ATOM 3479 CB GLU C 334 47.497 10.792 156.677 1.00 66.69 ATOM 3480 CG GLU C 334 46.149 11.068 157.374 1.00 70.10 ATOM 3481 CD GLU C 334 45.096 11.684 156.439 1.00 72.14 ATOM 3482 OE1 GLU C 334 43.985 12.006 156.924 1.00 72.03 ATOM 3483 OE2 GLU C 334 45.378 11.849 155.225 1.00 72.85 ATOM 3484 C GLU C 334 49.905 11.399 156.856 1.00 60.52 ATOM 3485 O GLU C 334 50.863 10.686 156.557 1.00 60.51 ATOM 3486 N ASP C 335 49.832 12.690 156.549 1.00 56.90 ATOM 3487 CA ASP C 335 50.882 13.388 155.811 1.00 53.14 ATOM 3488 CB ASP C 335 50.476 14.842 155.564 1.00 53.78 ATOM 3489 CG ASP C 335 49.223 14.968 154.723 1.00 54.03 ATOM 3490 OD1 ASP C 335 49.229 14.518 153.555 1.00 53.72 ATOM 3491 OD2 ASP C 335 48.231 15.530 155.235 1.00 55.24 ATOM 3492 C ASP C 335 52.261 13.376 156.476 1.00 50.25 ATOM 3493 O ASP C 335 53.261 13.720 155.846 1.00 49.76 ATOM 3494 N ALA C 336 52.327 13.006 157.748 1.00 45.93 ATOM 3495 CA ALA C 336 53.617 12.972 158.418 1.00 43.25 ATOM 3496 CB ALA C 336 53.462 12.516 159.863 1.00 44.14 ATOM 3497 C ALA C 336 54.498 12.002 157.656 1.00 41.41 ATOM 3498 O ALA C 336 54.009 11.154 156.921 1.00 41.75 ATOM 3499 N GLY C 337 55.803 12.120 157.825 1.00 39.43 ATOM 3500 CA GLY C 337 56.689 11.221 157.115 1.00 36.79 ATOM 3501 C GLY C 337 57.793 11.926 156.354 1.00 34.67 ATOM 3502 O GLY C 337 57.866 13.150 156.308 1.00 35.77 ATOM 3503 N GLU C 338 58.652 11.131 155.740 1.00 32.73 ATOM 3504 CA GLU C 338 59.788 11.632 154.982 1.00 30.27 ATOM 3505 CB GLU C 338 60.866 10.562 154.953 1.00 29.00 ATOM 3506 CG GLU C 338 62.067 10.917 154.143 1.00 30.51 ATOM 3507 CD GLU C 338 63.198 9.949 154.375 1.00 31.47 ATOM 3508 OD1 GLU C 338 62.982 8.743 154.134 1.00 29.99 ATOM 3509 OE2 GLU C 338 64.292 10.400 154.807 1.00 32.90 ATOM 3510 C GLU C 338 59.469 12.047 153.551 1.00 28.43 ATOM 3511 O GLU C 338 58.915 11.276 152.772 1.00 28.10 ATOM 3512 N TYR C 339 59.830 13.274 153.206 1.00 27.27 ATOM 3513 CA TYR C 339 59.613 13.768 151.857 1.00 25.56 ATOM 3514 CB TYR C 339 58.848 15.080 151.888 1.00 22.41 ATOM 3515 CG TYR C 339 57.407 14.869 152.267 1.00 20.77 ATOM 3516 CD1 TYR C 339 57.039 14.638 153.594 1.00 19.97 ATOM 3517 CE1 TYR C 339 55.719 14.387 153.937 1.00 19.82 ATOM 3518 CD2 TYR C 339 56.416 14.844 151.294 1.00 18.89 ATOM 3519 CE2 TYR C 339 55.104 14.593 151.623 1.00 19.97 ATOM 3520 CZ TYR C 339 54.755 14.363 152.945 1.00 20.30 ATOM 3521 OH TYR C 339 53.435 14.097 153.260 1.00 23.03 ATOM 3522 C TYR C 339 60.978 13.940 151.219 1.00 25.76 ATOM 3523 O TYR C 339 61.920 14.404 151.863 1.00 25.02 ATOM 3524 N THR C 340 61.077 13.560 149.950 1.00 25.99 ATOM 3525 CA THR C 340 62.345 13.606 149.241 1.00 26.36 ATOM 3526 CB THR C 340 62.814 12.168 148.890 1.00 24.39 ATOM 3527 OG1 THR C 340 63.094 11.447 150.095 1.00 23.87 ATOM 3528 CG2 THR C 340 64.059 12.204 148.046 1.00 24.52 ATOM 3529 C THR C 340 62.325 14.409 147.957 1.00 27.11 ATOM 3530 O THR C 340 61.365 14.350 147.189 1.00 27.36 ATOM 3531 N CYS C 341 63.403 15.152 147.731 1.00 26.79 ATOM 3532 CA CYS C 341 63.548 15.940 146.521 1.00 27.05 ATOM 3533 C CYS C 341 64.636 15.325 145.654 1.00 28.59 ATOM 3534 O CYS C 341 65.806 15.303 146.046 1.00 29.17 ATOM 3535 CB CYS C 341 63.946 17.365 146.853 1.00 25.54 ATOM 3536 SG CYS C 341 64.337 18.352 145.373 1.00 25.46 ATOM 3537 N LEU C 342 64.251 14.834 144.479 1.00 28.86 ATOM 3538 CA LEU C 342 65.187 14.216 143.538 1.00 29.91 ATOM 3539 CB LEU C 342 64.633 12.917 142.982 1.00 33.91 ATOM 3540 CG LEU C 342 64.729 11.650 143.789 1.00 38.17 ATOM 3541 CD1 LEU C 342 63.609 11.576 144.833 1.00 40.39 ATOM 3542 CD2 LEU C 342 64.614 10.515 142.788 1.00 43.03 ATOM 3543 C LEU C 342 65.477 15.076 142.333 1.00 27.85 ATOM 3544 O LEU C 342 64.571 15.662 141.750 1.00 27.94 ATOM 3545 N ALA C 343 66.733 15.092 141.921 1.00 25.07 ATOM 3546 CA ALA C 343 67.132 15.866 140.763 1.00 23.93 ATOM 3547 CE ALA C 343 67.638 17.236 141.218 1.00 22.00 ATOM 3548 C ALA C 343 68.224 15.112 140.007 1.00 23.67 ATOM 3549 O ALA C 343 69.215 14.672 140.604 1.00 22.52 ATOM 3550 N GLY C 344 68.050 14.958 138.700 1.00 21.73 ATOM 3551 CA GLY C 344 69.064 14.259 137.949 1.00 22.16 ATOM 3552 C GLY C 344 69.211 14.686 136.509 1.00 23.40 ATOM 3553 O GLY C 344 68.280 15.217 135.901 1.00 24.16 ATOM 3554 N ASN C 345 70.405 14.481 135.966 1.00 22.89 ATOM 3555 CA ASN C 345 70.649 14.786 134.572 1.00 23.31 ATOM 3556 CE ASN C 345 71.592 15.980 134.382 1.00 22.34 ATOM 3557 CG ASN C 345 72.844 15.920 135.254 1.00 21.82 ATOM 3558 OD1 ASN C 345 73.463 14.860 135.432 1.00 18.42 ATOM 3559 ND2 ASN C 345 73.243 17.090 135.776 1.00 13.77 ATOM 3560 C ASN C 345 71.251 13.538 133.996 1.00 26.08 ATOM 3561 O ASN C 345 71.276 12.506 134.669 1.00 26.21 ATOM 3562 N SER C 346 71.729 13.608 132.760 1.00 29.18 ATOM 3563 CA SER C 346 72.317 12.428 132.130 1.00 32.72 ATOM 3564 CE SER C 346 72.628 12.718 130.670 1.00 32.48 ATOM 3565 OG SER C 346 73.540 13.802 130.580 1.00 39.08 ATOM 3566 C SER C 346 73.598 11.990 132.846 1.00 33.36 ATOM 3567 O SER C 346 73.995 10.818 132.777 1.00 33.41 ATOM 3568 N ILE C 347 74.236 12.928 133.543 1.00 32.93 ATOM 3569 CA ILE C 347 75.474 12.619 134.246 1.00 32.67 ATOM 3570 CE ILE C 347 76.216 13.890 134.647 1.00 32.54 ATOM 3571 CG2 ILE C 347 77.521 13.533 135.317 1.00 30.57 ATOM 3572 CG1 ILE C 347 76.495 14.738 133.414 1.00 30.88 ATOM 3573 CD1 ILE C 347 77.034 16.100 133.747 1.00 30.35 ATOM 3574 C ILE C 347 75.252 11.790 135.499 1.00 33.46 ATOM 3575 O ILE C 347 75.934 10.788 135.716 1.00 34.67 ATOM 3576 N GLY C 348 74.309 12.207 136.334 1.00 34.14 ATOM 3577 CA GLY C 348 74.046 11.458 137.549 1.00 33.61 ATOM 3578 C GLY C 348 72.761 11.867 138.239 1.00 34.30 ATOM 3579 O GLY C 348 71.953 12.617 137.678 1.00 35.47 ATOM 3580 N LEU C 349 72.592 11.389 139.471 1.00 33.67 ATOM 3581 CA LEU C 349 71.409 11.672 140.269 1.00 31.92 ATOM 3582 CB LEU C 349 70.572 10.399 140.360 1.00 34.71 ATOM 3583 CG LEU C 349 69.175 10.536 140.962 1.00 38.25 ATOM 3584 CD1 LEU C 349 68.296 11.357 140.007 1.00 39.99 ATOM 3585 CD2 LEU C 349 68.586 9.156 141.191 1.00 37.78 ATOM 3586 C LEU C 349 71.721 12.182 141.687 1.00 30.62 ATOM 3587 O LEU C 349 72.719 11.795 142.298 1.00 29.04 ATOM 3588 N SER C 350 70.856 13.051 142.207 1.00 28.72 ATOM 3589 CA SER C 350 71.022 13.587 143.551 1.00 27.43 ATOM 3590 CB SER C 350 71.590 15.001 143.515 1.00 26.34 ATOM 3591 OG SER C 350 72.889 15.011 142.967 1.00 26.24 ATOM 3592 C SER C 350 69.667 13.636 144.204 1.00 28.04 ATOM 3593 O SER C 350 68.654 13.578 143.515 1.00 29.41 ATOM 3594 N HIS C 351 69.643 13.742 145.529 1.00 28.26 ATOM 3595 CA HIS C 351 68.386 13.832 146.258 1.00 28.95 ATOM 3596 CB HIS C 351 67.598 12.518 146.162 1.00 30.19 ATOM 3597 CG HIS C 351 68.160 11.405 146.995 1.00 33.01 ATOM 3598 CD2 HIS C 351 67.678 10.794 148.107 1.00 33.21 ATOM 3599 ND1 HIS C 351 69.373 10.805 146.725 1.00 31.59 ATOM 3600 CE1 HIS C 351 69.615 9.876 147.632 1.00 31.13 ATOM 3601 NE2 HIS C 351 68.602 9.849 148.481 1.00 33.01 ATOM 3602 C HIS C 351 68.632 14.167 147.716 1.00 29.78 ATOM 3603 O HIS C 351 69.599 13.698 148.302 1.00 31.58 ATOM 3604 N HIS C 352 67.764 15.001 148.284 1.00 29.61 ATOM 3605 CA HIS C 352 67.833 15.388 149.692 1.00 28.24 ATOM 3606 CB HIS C 352 68.020 16.900 149.845 1.00 26.76 ATOM 3607 CG HIS C 352 69.436 17.358 149.705 1.00 27.38 ATOM 3608 CD2 HIS C 352 70.582 16.670 149.488 1.00 27.13 ATOM 3609 ND1 HIS C 352 69.797 18.687 149.786 1.00 27.93 ATOM 3610 CE1 HIS C 352 71.103 18.798 149.625 1.00 27.53 ATOM 3611 NE2 HIS C 352 71.603 17.589 149.442 1.00 28.55 ATOM 3612 C HIS C 352 66.495 14.998 150.292 1.00 28.26 ATOM 3613 O HIS C 352 65.473 15.043 149.613 1.00 30.53 ATOM 3614 N SER C 353 66.479 14.605 151.552 1.00 28.24 ATOM 3615 CA SER C 353 65.214 14.244 152.157 1.00 29.01 ATOM 3616 CB SER C 353 65.188 12.761 152.490 1.00 26.29 ATOM 3617 OG SER C 353 65.387 12.004 151.310 1.00 26.32 ATOM 3618 C SER C 353 64.995 15.083 153.398 1.00 30.55 ATOM 3619 O SER C 353 65.937 15.663 153.932 1.00 33.17 ATOM 3620 N ALA C 354 63.742 15.188 153.824 1.00 31.52 ATOM 3621 CA ALA C 354 63.391 15.954 155.017 1.00 31.06 ATOM 3622 CB ALA C 354 62.994 17.374 154.657 1.00 30.66 ATOM 3623 C ALA C 354 62.240 15.247 155.702 1.00 31.47 ATOM 3624 O ALA C 354 61.521 14.447 155.082 1.00 29.46 ATOM 3625 N TRP C 355 62.069 15.523 156.988 1.00 32.19 ATOM 3626 CA TRP C 355 60.998 14.873 157.705 1.00 33.04 ATOM 3627 CB TRP C 355 61.538 14.043 158.856 1.00 36.34 ATOM 3628 CG TRP C 355 60.566 12.984 159.209 1.00 43.15 ATOM 3629 CD2 TRP C 355 60.660 11.598 158.868 1.00 46.13 ATOM 3630 CE2 TRP C 355 59.454 10.978 159.295 1.00 47.17 ATOM 3631 CE3 TRP C 355 61.646 10.818 158.240 1.00 47.31 ATOM 3632 CD1 TRP C 355 59.343 13.148 159.821 1.00 44.54 ATOM 3633 NE1 TRP C 355 58.672 11.946 159.872 1.00 46.02 ATOM 3634 CZ2 TRP C 355 59.208 9.609 159.113 1.00 47.00 ATOM 3635 CZ3 TRP C 355 61.403 9.456 158.060 1.00 48.50 ATOM 3636 CR2 TRP C 355 60.189 8.866 158.496 1.00 48.25 ATOM 3637 C TRP C 355 59.919 15.802 158.214 1.00 32.05 ATOM 3638 O TRP C 355 60.198 16.828 158.835 1.00 30.83 ATOM 3639 N LEU C 356 58.678 15.420 157.933 1.00 31.07 ATOM 3640 CA LEU C 356 57.524 16.183 158.352 1.00 30.97 ATOM 3641 CB LEU C 356 56.477 16.209 157.234 1.00 30.59 ATOM 3642 CG LEU C 356 55.497 17.398 157.177 1.00 30.85 ATOM 3643 CD1 LEU C 356 54.086 16.904 157.372 1.00 28.31 ATOM 3644 CD2 LEU C 356 55.863 18.464 158.228 1.00 29.07 ATOM 3645 C LEU C 356 56.946 15.542 159.599 1.00 31.35 ATOM 3646 O LEU C 356 56.465 14.413 159.556 1.00 32.90 ATOM 3647 N THR C 357 57.024 16.263 160.712 1.00 32.76 ATOM 3648 CA THR C 357 56.493 15.808 162.001 1.00 33.59 ATOM 3649 CB THR C 357 57.483 16.103 163.156 1.00 31.42 ATOM 3650 OG1 THR C 357 58.639 15.274 163.031 1.00 30.47 ATOM 3651 CG2 THR C 357 56.825 15.868 164.498 1.00 29.75 ATOM 3652 C THR C 357 55.199 16.580 162.280 1.00 35.63 ATOM 3653 O THR C 357 55.219 17.811 162.359 1.00 36.00 ATOM 3654 N VAL C 358 54.077 15.876 162.414 1.00 38.93 ATOM 3655 CA VAL C 358 52.801 16.548 162.697 1.00 41.15 ATOM 3656 CB VAL C 358 51.677 16.122 161.714 1.00 41.26 ATOM 3657 CG1 VAL C 358 50.328 16.600 162.225 1.00 41.80 ATOM 3658 CG2 VAL C 358 51.917 16.742 160.352 1.00 41.94 ATOM 3659 C VAL C 358 52.313 16.314 164.126 1.00 41.85 ATOM 3660 O VAL C 358 52.489 15.227 164.688 1.00 43.32 ATOM 3661 N LEU C 359 51.715 17.347 164.715 1.00 41.83 ATOM 3662 CA LEU C 359 51.192 17.256 166.074 1.00 41.63 ATOM 3663 CB LEU C 359 52.240 17.766 167.075 1.00 41.22 ATOM 3664 CG LEU C 359 53.580 17.017 167.141 1.00 41.29 ATOM 3665 CD1 LEU C 359 54.507 17.658 168.177 1.00 37.31 ATOM 3666 CD2 LEU C 359 53.319 15.552 167.480 1.00 41.10 ATOM 3667 C LEU C 359 49.889 18.051 166.202 1.00 40.98 ATOM 3668 O LEU C 359 49.037 17.618 167.011 1.00 42.00 ATOM 3669 CB MET D 149 110.758 21.323 85.925 1.00 69.15 ATOM 3670 CG MET D 149 112.000 21.050 86.762 1.00 74.74 ATOM 3671 SD MET D 149 113.256 20.101 85.852 1.00 81.81 ATOM 3672 CE MET D 149 114.238 21.463 85.114 1.00 78.77 ATOM 3673 C MET D 149 109.620 19.185 86.605 1.00 62.44 ATOM 3674 O MET D 149 109.529 19.656 87.741 1.00 62.89 ATOM 3675 N MET D 149 108.883 20.439 84.573 1.00 63.06 ATOM 3676 CA MET D 149 110.054 20.057 85.419 1.00 64.74 ATOM 3677 N PRO D 150 109.353 17.894 86.353 1.00 59.72 ATOM 3678 CD PRO D 150 109.422 17.240 85.034 1.00 59.01 ATOM 3679 CA PRO D 150 108.924 16.941 87.384 1.00 57.62 ATOM 3680 CB PRO D 150 109.001 15.600 86.662 1.00 57.11 ATOM 3681 CG PRO D 150 108.634 15.970 85.264 1.00 57.93 ATOM 3682 C PRO D 150 109.754 16.957 88.670 1.00 55.83 ATOM 3683 O PRO D 150 110.977 16.787 88.631 1.00 54.45 ATOM 3684 N VAL D 151 109.079 17.171 89.803 1.00 54.22 ATOM 3685 CA VAL D 151 109.734 17.182 91.120 1.00 51.14 ATOM 3686 CB VAL D 151 109.991 18.614 91.675 1.00 49.72 ATOM 3687 CG1 VAL D 151 110.768 18.530 92.980 1.00 47.94 ATOM 3688 CG2 VAL D 151 110.778 19.431 90.685 1.00 51.03 ATOM 3689 C VAL D 151 108.679 16.454 92.144 1.00 49.31 ATOM 3690 O VAL D 151 107.679 16.711 92.263 1.00 49.40 ATOM 3691 N ALA D 152 109.507 15.539 92.874 1.00 47.24 ATOM 3692 CA ALA D 152 108.819 14.787 93.911 1.00 45.53 ATOM 3693 CB ALA D 152 109.658 13.586 94.330 1.00 46.23 ATOM 3694 C ALA D 152 108.599 15.726 95.100 1.00 44.08 ATOM 3695 O ALA D 152 109.352 16.683 95.303 1.00 43.55 ATOM 3696 N PRO D 153 107.565 15.463 95.904 1.00 42.50 ATOM 3697 CD PRO D 153 106.685 14.282 95.917 1.00 42.56 ATOM 3698 CA PRO D 153 107.308 16.332 97.053 1.00 41.65 ATOM 3699 CB PRO D 153 106.100 15.670 97.721 1.00 42.90 ATOM 3700 CG PRO D 153 106.266 14.218 97.360 1.00 44.02 ATOM 3701 C PRO D 153 108.499 16.481 98.001 1.00 40.45 ATOM 3702 O PRO D 153 109.251 15.530 98.237 1.00 39.50 ATOM 3703 N TYR D 154 108.668 17.685 98.535 1.00 38.89 ATOM 3704 CA TYR D 154 109.754 17.955 99.470 1.00 37.97 ATOM 3705 CB TYR D 154 110.957 18.508 98.727 1.00 36.16 ATOM 3706 CG TYR D 154 110.743 19.903 98.186 1.00 34.50 ATOM 3707 CD1 TYR D 154 110.255 20.109 96.900 1.00 34.15 ATOM 3708 CE1 TYR D 154 110.089 21.393 96.395 1.00 33.84 ATOM 3709 CD2 TYR D 154 111.050 21.019 98.959 1.00 34.16 ATOM 3710 CE2 TYR D 154 110.885 22.303 98.464 1.00 34.12 ATOM 3711 CZ TYR D 154 110.409 22.481 97.183 1.00 33.84 ATOM 3712 OH TYR D 154 110.276 23.751 96.689 1.00 35.14 ATOM 3713 C TYR D 154 109.298 18.972 100.524 1.00 38.33 ATOM 3714 O TYR D 154 108.449 19.830 100.243 1.00 39.41 ATOM 3715 N TRP D 155 109.863 18.892 101.727 1.00 36.71 ATOM 3716 CA TRP D 155 109.455 19.823 102.771 1.00 37.08 ATOM 3717 CB TRP D 155 109.894 19.355 104.170 1.00 35.10 ATOM 3718 CG TRP D 155 109.428 17.970 104.597 1.00 32.90 ATOM 3719 CD2 TRP D 155 108.072 17.482 104.711 1.00 33.50 ATOM 3720 CE2 TRP D 155 108.147 16.139 105.165 1.00 31.19 ATOM 3721 CE3 TRP D 155 106.809 18.045 104.473 1.00 35.19 ATOM 3722 CD1 TRP D 155 110.226 16.936 104.974 1.00 32.49 ATOM 3723 NE1 TRP D 155 109.467 15.835 105.316 1.00 32.97 ATOM 3724 CZ2 TRP D 155 107.014 15.352 105.386 1.00 31.24 ATOM 3725 CZ3 TRP D 155 105.668 17.253 104.696 1.00 33.46 ATOM 3726 CR2 TRP D 155 105.786 15.922 105.148 1.00 32.78 ATOM 3727 C TRP D 155 110.029 21.202 102.482 1.00 38.20 ATOM 3728 O TRP D 155 111.219 21.350 102.196 1.00 38.53 ATOM 3729 N THR D 156 109.161 22.202 102.554 1.00 38.98 ATOM 373O CA THR D 156 109.531 23.577 102.303 1.00 40.31 ATOM 3731 CB THR D 156 108.352 24.311 101.685 1.00 40.82 ATOM 3732 OG1 THR D 156 107.322 24.493 102.665 1.00 40.84 ATOM 3733 CG2 THR D 156 107.797 23.490 100.548 1.00 40.35 ATOM 3734 C THR D 156 109.948 24.276 103.593 1.00 42.90 ATOM 3735 O THR D 156 110.677 25.269 103.560 1.00 43.06 ATOM 3736 N SER D 157 109.495 23.753 104.730 1.00 45.45 ATOM 3737 CA SER D 157 109.833 24.357 106.019 1.00 46.78 ATOM 3738 CB SER D 157 108.702 25.283 106.472 1.00 45.14 ATOM 3739 OG SER D 157 108.311 26.138 105.413 1.00 44.01 ATOM 3740 C SER D 157 110.111 23.305 107.091 1.00 47.76 ATOM 3741 O SER D 157 109.389 23.205 108.083 1.00 49.26 ATOM 3742 N PRO D 158 111.175 22.510 106.905 1.00 48.01 ATOM 3743 CD PRO D 158 112.209 22.622 105.862 1.00 47.15 ATOM 3744 CA PRO D 158 111.529 21.470 107.873 1.00 48.12 ATOM 3745 CB PRO D 158 112.760 20.830 107.245 1.00 47.44 ATOM 3746 CG PRO D 158 113.392 21.978 106.534 1.00 47.27 ATOM 3747 C PRO D 158 111.810 22.047 109.259 1.00 48.98 ATOM 3748 O PRO D 158 111.803 21.324 110.257 1.00 49.86 ATOM 3749 N GLU D 159 112.060 23.351 109.313 1.00 49.77 ATOM 3750 CA GLU D 159 112.339 24.023 110.577 1.00 50.29 ATOM 3751 CB GLU D 159 112.846 25.442 110.313 1.00 51.25 ATOM 3752 C GLU D 159 111.081 24.060 111.448 1.00 50.73 ATOM 3753 O GLU D 159 111.168 24.038 112.674 1.00 52.21 ATOM 3754 N LYS D 160 109.916 24.095 110.803 1.00 50.21 ATOM 3755 CA LYS D 160 108.624 24.127 111.493 1.00 48.11 ATOM 3756 CB LYS D 160 107.612 24.890 110.625 1.00 47.76 ATOM 3757 C LYS D 160 108.088 22.714 111.803 1.00 46.25 ATOM 3758 O LYS D 160 106.895 22.534 112.065 1.00 45.85 ATOM 3759 N MET D 161 108.973 21.721 111.793 1.00 44.07 ATOM 3760 CA MET D 161 108.570 20.337 112.033 1.00 41.94 ATOM 3761 CB MET D 161 108.721 19.531 110.743 1.00 41.09 ATOM 3762 CG MET D 161 108.422 20.324 109.491 1.00 40.86 ATOM 3763 SD MET D 161 108.201 19.267 108.062 1.00 41.70 ATOM 3764 CE MET D 161 106.479 18.779 108.274 1.00 40.72 ATOM 3765 C MET D 161 109.376 19.656 113.128 1.00 40.13 ATOM 3766 O MET D 161 109.080 18.532 113.514 1.00 39.25 ATOM 3767 N GLU D 162 110.394 20.339 113.624 1.00 39.93 ATOM 3768 CA GLU D 162 111.249 19.777 114.656 1.00 39.97 ATOM 3769 CB GLU D 162 112.330 20.803 115.035 1.00 41.29 ATOM 3770 C GLU D 162 110.504 19.276 115.912 1.00 39.38 ATOM 3771 O GLU D 162 110.942 18.317 116.555 1.00 39.93 ATOM 3772 N LYS D 163 109.387 19.912 116.256 1.00 37.75 ATOM 3773 CA LYS D 163 108.601 19.519 117.430 1.00 37.57 ATOM 3774 CB LYS D 163 107.739 20.699 117.879 1.00 38.91 ATOM 3775 CG LYS D 163 106.685 20.375 118.924 1.00 39.14 ATOM 3776 CD LYS D 163 105.919 21.641 119.271 1.00 42.01 ATOM 3777 CE LYS D 163 104.685 21.381 120.110 1.00 42.34 ATOM 3778 NZ LYS D 163 103.984 22.666 120.386 1.00 43.85 ATOM 3779 C LYS D 163 107.699 18.325 117.135 1.00 36.24 ATOM 3780 O LYS D 163 106.522 18.499 116.832 1.00 36.01 ATOM 3781 N LYS D 164 108.248 17.118 117.231 1.00 35.31 ATOM 3782 CA LYS D 164 107.482 15.908 116.949 1.00 34.73 ATOM 3783 CB LYS D 164 108.429 14.703 116.845 1.00 33.14 ATOM 3784 C LYS D 164 106.363 15.627 117.971 1.00 34.05 ATOM 3785 O LYS D 164 105.279 15.178 117.597 1.00 33.86 ATOM 3786 N LEU D 165 106.616 15.901 119.251 1.00 33.62 ATOM 3787 CA LEU D 165 105.614 15.668 120.299 1.00 32.88 ATOM 3788 CB LEU D 165 106.266 15.047 121.539 1.00 30.62 ATOM 3789 CG LEU D 165 105.369 14.968 122.780 1.00 29.12 ATOM 3790 CD1 LEU D 165 104.041 14.358 122.395 1.00 30.41 ATOM 3791 CD2 LEU D 165 106.033 14.148 123.875 1.00 28.30 ATOM 3792 C LEU D 165 104.825 16.900 120.749 1.00 32.89 ATOM 3793 O LEU D 165 105.403 17.880 121.214 1.00 31.55 ATOM 3794 N HIS D 166 103.502 16.839 120.623 1.00 34.11 ATOM 3795 CA HIS D 166 102.642 17.944 121.062 1.00 35.36 ATOM 3796 CB HIS D 166 101.697 18.406 119.938 1.00 36.03 ATOM 3797 CG HIS D 166 102.383 19.122 118.815 1.00 38.56 ATOM 3798 CD2 HIS D 166 102.166 20.346 118.275 1.00 39.15 ATOM 3799 ND1 HIS D 166 103.415 18.563 118.090 1.00 40.14 ATOM 3800 CE1 HIS D 166 103.805 19.411 117.153 1.00 40.03 ATOM 3801 NE2 HIS D 166 103.063 20.500 117.243 1.00 39.63 ATOM 3802 C HIS D 166 101.815 17.512 122.278 1.00 34.38 ATOM 3803 O HIS D 166 100.854 16.751 122.151 1.00 33.62 ATOM 3804 N ALA D 167 102.216 17.987 123.453 1.00 34.17 ATOM 3805 CA ALA D 167 101.512 17.683 124.693 1.00 34.33 ATOM 3806 CB ALA D 167 102.494 17.263 125.773 1.00 34.70 ATOM 3807 C ALA D 167 100.773 18.953 125.102 1.00 34.92 ATOM 3808 O ALA D 167 101.349 20.053 125.139 1.00 34.52 ATOM 3809 N VAL D 168 99.490 18.807 125.404 1.00 34.73 ATOM 3810 CA VAL D 168 98.687 19.961 125.772 1.00 35.77 ATOM 3811 CB VAL D 168 98.071 20.638 124.516 1.00 37.28 ATOM 3812 CG1 VAL D 168 99.167 21.236 123.661 1.00 39.06 ATOM 3813 CG2 VAL D 168 97.266 19.618 123.708 1.00 35.97 ATOM 3814 C VAL D 168 97.542 19.679 126.734 1.00 35.05 ATOM 3815 O VAL D 168 97.092 18.541 126.890 1.00 34.17 ATOM 3816 N PRO D 169 97.055 20.733 127.401 1.00 35.28 ATOM 3817 CD PRO D 169 97.554 22.122 127.403 1.00 36.03 ATOM 3818 CA PRO D 169 95.949 20.572 128.340 1.00 35.43 ATOM 3819 CB PRO D 169 96.026 21.851 129.173 1.00 35.77 ATOM 3820 CG PRO D 169 96.490 22.857 128.188 1.00 35.98 ATOM 3821 C PRO D 169 94.661 20.467 127.525 1.00 34.49 ATOM 3822 O PRO D 169 94.466 21.221 126.569 1.00 34.25 ATOM 3823 N ALA D 170 93.796 19.523 127.886 1.00 34.06 ATOM 3824 CA ALA D 170 92.532 19.332 127.174 1.00 33.00 ATOM 3825 CB ALA D 170 91.619 18.416 127.956 1.00 33.00 ATOM 3826 C ALA D 170 91.824 20.651 126.924 1.00 32.26 ATOM 3827 O ALA D 170 91.941 21.578 127.719 1.00 32.40 ATOM 3828 N ALA D 171 91.093 20.713 125.813 1.00 32.29 ATOM 3829 CA ALA D 171 90.327 21.892 125.398 1.00 32.27 ATOM 383O CB ALA D 171 89.828 22.679 126.609 1.00 31.55 ATOM 3831 C ALA D 171 91.112 22.819 124.491 1.00 31.96 ATOM 3832 O ALA D 171 90.562 23.778 123.948 1.00 29.70 ATOM 3833 N LYS D 172 92.402 22.546 124.333 1.00 32.67 ATOM 3834 CA LYS D 172 93.217 23.384 123.473 1.00 33.52 ATOM 3835 CB LYS D 172 94.694 23.261 123.863 1.00 33.51 ATOM 3836 CG LYS D 172 95.611 24.093 122.988 1.00 34.75 ATOM 3837 CD LYS D 172 97.001 24.243 123.565 1.00 36.61 ATOM 3838 CE LYS D 172 97.944 24.853 122.526 1.00 37.04 ATOM 3839 NZ LYS D 172 97.361 26.069 121.884 1.00 37.00 ATOM 3840 C LYS D 172 93.019 23.029 121.987 1.00 34.04 ATOM 3841 O LYS D 172 92.652 21.896 121.647 1.00 33.27 ATOM 3842 N THR D 173 93.232 24.013 121.112 1.00 33.22 ATOM 3843 CA THR D 173 93.115 23.804 119.670 1.00 33.34 ATOM 3844 CB THR D 173 92.676 25.100 118.920 1.00 34.73 ATOM 3845 OG1 THR D 173 91.293 25.359 119.174 1.00 35.71 ATOM 3846 CG2 THR D 173 92.857 24.947 117.418 1.00 35.47 ATOM 3847 C THR D 173 94.484 23.379 119.161 1.00 32.51 ATOM 3848 O THR D 173 95.475 24.052 119.425 1.00 32.58 ATOM 3849 N VAL D 174 94.545 22.256 118.451 1.00 31.86 ATOM 3850 CA VAL D 174 95.814 21.779 117.920 1.00 31.60 ATOM 3851 CB VAL D 174 96.099 20.349 118.361 1.00 31.01 ATOM 3852 CG1 VAL D 174 97.430 19.890 117.769 1.00 32.36 ATOM 3853 CG2 VAL D 174 96.134 20.279 119.872 1.00 28.05 ATOM 3854 C VAL D 174 95.879 21.855 116.395 1.00 33.26 ATOM 3855 O VAL D 174 94.892 21.594 115.704 1.00 33.35 ATOM 3856 N LYS D 175 97.045 22.236 115.877 1.00 34.14 ATOM 3857 CA LYS D 175 97.235 22.345 114.433 1.00 34.10 ATOM 3858 CB LYS D 175 97.168 23.809 113.983 1.00 34.48 ATOM 3859 C LYS D 175 98.577 21.748 114.052 1.00 34.13 ATOM 3860 O LYS D 175 99.607 22.109 114.614 1.00 34.08 ATOM 3861 N PHE D 176 98.551 20.816 113.107 1.00 34.81 ATOM 3862 CA PHE D 176 99.764 20.157 112.639 1.00 36.16 ATOM 3863 CB PHE D 176 99.610 18.637 112.667 1.00 38.54 ATOM 3864 CG PHE D 176 99.406 18.067 114.038 1.00 42.17 ATOM 3865 CD1 PHE D 176 100.194 18.485 115.107 1.00 42.78 ATOM 3866 CD2 PHE D 176 98.451 17.074 114.256 1.00 42.56 ATOM 3867 CE1 PHE D 176 100.039 17.922 116.374 1.00 42.13 ATOM 3868 CE2 PHE D 176 98.290 16.506 115.519 1.00 42.31 ATOM 3869 CZ PHE D 176 99.087 16.932 116.577 1.00 42.63 ATOM 3870 C PHE D 176 100.070 20.590 111.214 1.00 36.23 ATOM 3871 O PHE D 176 99.227 20.441 110.322 1.00 34.78 ATOM 3872 N LYS D 177 101.283 21.101 111.005 1.00 35.54 ATOM 3873 CA LYS D 177 101.694 21.570 109.690 1.00 36.04 ATOM 3874 CB LYS D 177 102.157 23.032 109.801 1.00 34.13 ATOM 3875 C LYS D 177 102.784 20.706 109.033 1.00 36.18 ATOM 3876 O LYS D 177 103.714 20.248 109.698 1.00 35.87 ATOM 3877 N CYS D 178 102.637 20.474 107.728 1.00 37.01 ATOM 3878 CA CYS D 178 103.598 19.701 106.936 1.00 37.64 ATOM 3879 C CYS D 178 103.911 20.467 105.655 1.00 38.59 ATOM 3880 O CYS D 178 103.697 19.966 104.550 1.00 38.68 ATOM 3881 CB CYS D 178 103.031 18.330 106.578 1.00 36.26 ATOM 3882 SG CYS D 178 102.974 17.203 107.996 1.00 36.60 ATOM 3883 N PRO D 179 104.416 21.707 105.787 1.00 39.52 ATOM 3884 CD PRO D 179 104.675 22.481 107.015 1.00 39.06 ATOM 3885 CA PRO D 179 104.740 22.511 104.611 1.00 39.90 ATOM 3886 CB PRO D 179 105.401 23.747 105.217 1.00 38.21 ATOM 3887 CG PRO D 179 104.680 23.900 106.495 1.00 36.04 ATOM 3888 C PRO D 179 105.654 21.766 103.649 1.00 41.32 ATOM 3889 O PRO D 179 106.807 21.439 103.977 1.00 40.88 ATOM 3890 N SER D 180 105.119 21.485 102.466 1.00 42.71 ATOM 3891 CA SER D 180 105.875 20.790 101.437 1.00 44.82 ATOM 3892 CB SER D 180 105.529 19.292 101.413 1.00 45.46 ATOM 3893 OG SER D 180 104.130 19.082 101.432 1.00 48.11 ATOM 3894 C SER D 180 105.608 21.424 100.083 1.00 45.11 ATOM 3895 O SER D 180 104.881 22.425 99.988 1.00 45.08 ATOM 3896 N SER D 181 106.216 20.852 99.046 1.00 44.67 ATOM 3897 CA SER D 181 106.062 21.360 97.691 1.00 44.09 ATOM 3898 CB SER D 181 106.911 22.620 97.508 1.00 42.85 ATOM 3899 OG SER D 181 106.811 23.124 96.189 1.00 41.34 ATOM 3900 C SER D 181 106.499 20.317 96.680 1.00 44.51 ATOM 3901 O SER D 181 107.084 19.299 97.040 1.00 44.21 ATOM 3902 N GLY D 182 106.216 20.591 95.411 1.00 45.65 ATOM 3903 CA GLY D 182 106.592 19.692 94.336 1.00 45.68 ATOM 3904 C GLY D 182 105.741 19.934 93.103 1.00 46.72 ATOM 3905 O GLY D 182 104.697 20.588 93.180 1.00 47.72 ATOM 3906 N THR D 183 106.184 19.421 91.960 1.00 46.52 ATOM 3907 CA THR D 183 105.424 19.577 90.724 1.00 45.61 ATOM 3908 CB THR D 183 106.044 20.652 89.807 1.00 45.40 ATOM 3909 OG1 THR D 183 107.457 20.453 89.725 1.00 46.04 ATOM 3910 CG2 THR D 183 105.766 22.049 90.358 1.00 44.85 ATOM 3911 C THR D 183 105.339 18.251 89.978 1.00 44.73 ATOM 3912 O THR D 183 106.350 17.597 89.730 1.00 44.87 ATOM 3913 N PRO D 184 104.116 17.818 89.642 1.00 44.69 ATOM 3914 CD PRO D 184 103.857 16.493 89.049 1.00 43.56 ATOM 3915 CA PRO D 184 102.854 18.510 89.930 1.00 44.95 ATOM 3916 CB PRO D 184 101.829 17.645 89.213 1.00 43.90 ATOM 3917 CG PRO D 184 102.400 16.271 89.384 1.00 43.92 ATOM 3918 C PRO D 184 102.559 18.636 91.431 1.00 46.12 ATOM 3919 O PRO D 184 103.002 17.806 92.242 1.00 45.37 ATOM 3920 N GLN D 185 101.804 19.677 91.785 1.00 48.01 ATOM 3921 CA GLN D 185 101.439 19.942 93.179 1.00 48.94 ATOM 3922 CB GLN D 185 100.386 21.050 93.269 1.00 50.69 ATOM 3923 CG GLN D 185 100.407 21.749 94.605 1.00 55.14 ATOM 3924 CD GLN D 185 101.796 22.271 94.959 1.00 58.21 ATOM 3925 OE1 GLN D 185 102.026 22.757 96.067 1.00 61.45 ATOM 3926 NE2 GLN D 185 102.727 22.177 94.014 1.00 58.46 ATOM 3927 C GLN D 185 100.927 18.677 93.851 1.00 47.51 ATOM 3928 O GLN D 185 99.975 18.049 93.374 1.00 48.35 ATOM 3929 N PRO D 186 101.558 18.283 94.970 1.00 44.84 ATOM 3930 CD PRO D 186 102.748 18.894 95.593 1.00 43.75 ATOM 3931 CA PRO D 186 101.150 17.072 95.686 1.00 42.59 ATOM 3932 CB PRO D 186 102.346 16.799 96.590 1.00 42.85 ATOM 3933 CG PRO D 186 102.830 18.176 96.915 1.00 43.55 ATOM 3934 C PRO D 186 99.835 17.148 96.460 1.00 41.51 ATOM 3935 O PRO D 186 99.275 18.221 96.670 1.00 40.81 ATOM 3936 N THR D 187 99.337 15.984 96.862 1.00 41.66 ATOM 3937 CA THR D 187 98.108 15.901 97.638 1.00 40.35 ATOM 3938 CB THR D 187 97.232 14.753 97.203 1.00 39.73 ATOM 3939 OG1 THR D 187 98.044 13.590 97.003 1.00 40.03 ATOM 3940 CG2 THR D 187 96.502 15.108 95.941 1.00 40.19 ATOM 3941 C THR D 187 98.468 15.671 99.092 1.00 41.68 ATOM 3942 O THR D 187 99.486 15.041 99.408 1.00 42.57 ATOM 3943 N LEU D 188 97.612 16.174 99.973 1.00 41.12 ATOM 3944 CA LEU D 188 97.833 16.066 101.401 1.00 39.93 ATOM 3945 CB LEU D 188 97.967 17.475 101.992 1.00 39.49 ATOM 3946 CG LEU D 188 98.640 17.685 103.352 1.00 38.54 ATOM 3947 CD1 LEU D 188 97.695 18.466 104.252 1.00 36.15 ATOM 3948 CD2 LEU D 188 99.031 16.351 103.972 1.00 37.43 ATOM 3949 C LEU D 188 96.690 15.317 102.076 1.00 39.41 ATOM 3950 O LEU D 188 95.525 15.693 101.944 1.00 39.82 ATOM 3951 N ARG D 189 97.033 14.254 102.795 1.00 38.29 ATOM 3952 CA ARG D 189 96.050 13.463 103.515 1.00 37.44 ATOM 3953 CB ARG D 189 95.760 12.168 102.751 1.00 37.63 ATOM 3954 CG ARG D 189 96.969 11.294 102.500 1.00 40.60 ATOM 3955 CD ARG D 189 96.551 9.935 101.942 1.00 41.74 ATOM 3956 NE ARG D 189 97.654 8.970 101.942 1.00 42.49 ATOM 3957 CZ ARG D 189 97.512 7.668 101.714 1.00 41.00 ATOM 3958 C ARG D 189 96.630 13.156 104.891 1.00 36.92 ATOM 3959 O ARG D 189 97.844 13.071 105.035 1.00 37.76 ATOM 3960 N TRP D 190 95.771 13.004 105.899 1.00 37.03 ATOM 3961 CA TRP D 190 96.218 12.715 107.260 1.00 35.13 ATOM 3962 CB TRP D 190 95.732 13.797 108.214 1.00 34.41 ATOM 3963 CG TRP D 190 96.297 15.173 107.933 1.00 35.57 ATOM 3964 CD2 TRP D 190 97.500 15.735 108.479 1.00 35.94 ATOM 3965 CE2 TRP D 190 97.604 17.060 107.984 1.00 34.87 ATOM 3966 CE3 TRP D 190 98.502 15.247 109.338 1.00 36.28 ATOM 3967 CD1 TRP D 190 95.744 16.149 107.146 1.00 33.94 ATOM 3968 NE1 TRP D 190 96.520 17.283 107.178 1.00 32.39 ATOM 3969 CZ2 TRP D 190 98.673 17.911 108.323 1.00 36.31 ATOM 3970 CZ3 TRP D 190 99.568 16.093 109.678 1.00 37.87 ATOM 3971 CH2 TRP D 190 99.642 17.414 109.167 1.00 37.94 ATOM 3972 C TRP D 190 95.750 11.361 107.773 1.00 35.45 ATOM 3973 O TRP D 190 94.747 10.822 107.322 1.00 35.52 ATOM 3974 N LEU D 191 96.484 10.821 108.734 1.00 36.10 ATOM 3975 CA LEU D 191 96.161 9.520 109.307 1.00 37.96 ATOM 3976 CB LEU D 191 97.143 8.455 108.812 1.00 39.10 ATOM 3977 CG LEU D 191 97.237 8.046 107.349 1.00 39.59 ATOM 3978 CD1 LEU D 191 98.320 6.988 107.239 1.00 40.57 ATOM 3979 CD2 LEU D 191 95.915 7.493 106.856 1.00 39.59 ATOM 3980 C LEU D 191 96.252 9.520 110.824 1.00 38.40 ATOM 3981 O LEU D 191 97.307 9.861 111.376 1.00 39.40 ATOM 3982 N LYS D 192 95.168 9.144 111.504 1.00 36.74 ATOM 3983 CA LYS D 192 95.237 9.056 112.957 1.00 34.76 ATOM 3984 CB LYS D 192 93.912 9.326 113.658 1.00 33.63 ATOM 3985 CG LYS D 192 94.034 8.999 115.137 1.00 31.25 ATOM 3986 CD LYS D 192 92.711 8.816 115.826 1.00 32.21 ATOM 3987 CE LYS D 192 92.027 10.142 116.087 1.00 32.40 ATOM 3988 NZ LYS D 192 91.606 10.260 117.511 1.00 29.92 ATOM 3989 C LYS D 192 95.633 7.623 113.239 1.00 34.69 ATOM 3990 O LYS D 192 94.914 6.684 112.883 1.00 33.43 ATOM 3991 N ASN D 193 96.788 7.468 113.874 1.00 35.21 ATOM 3992 CA ASN D 193 97.338 6.165 114.216 1.00 35.69 ATOM 3993 CB ASN D 193 96.534 5.508 115.331 1.00 34.53 ATOM 3994 CG ASN D 193 96.728 6.204 116.643 1.00 34.30 ATOM 3995 OD1 ASN D 193 97.855 6.551 117.004 1.00 31.94 ATOM 3996 ND2 ASN D 193 95.636 6.419 117.372 1.00 34.92 ATOM 3997 C ASN D 193 97.445 5.224 113.033 1.00 36.74 ATOM 3998 O ASN D 193 97.162 4.029 113.144 1.00 35.50 ATOM 3999 N GLY D 194 97.855 5.777 111.897 1.00 38.21 ATOM 4000 CA GLY D 194 98.039 4.969 110.707 1.00 38.61 ATOM 4001 C GLY D 194 96.803 4.626 109.908 1.00 38.67 ATOM 4002 O GLY D 194 96.913 4.006 108.856 1.00 39.28 ATOM 4003 N LYS D 195 95.628 5.013 110.382 1.00 38.69 ATOM 4004 CA LYS D 195 94.417 4.703 109.639 1.00 37.44 ATOM 4005 CB LYS D 195 93.403 4.009 110.553 1.00 36.65 ATOM 4006 C LYS D 195 93.811 5.959 109.018 1.00 37.35 ATOM 4007 O LYS D 195 94.169 7.081 109.380 1.00 36.18 ATOM 4008 N GLIJ D 196 92.917 5.759 108.056 1.00 39.04 ATOM 4009 CA GLU D 196 92.237 6.860 107.394 1.00 40.62 ATOM 4010 CB GLU D 196 91.150 6.317 106.463 1.00 41.16 ATOM 4011 C GLU D 196 91.612 7.697 108.500 1.00 42.49 ATOM 4012 O GLU D 196 91.058 7.154 109.457 1.00 42.76 ATOM 4013 N PHE D 197 91.704 9.016 108.380 1.00 45.15 ATOM 4014 CA PHE D 197 91.161 9.905 109.404 1.00 47.11 ATOM 4015 CB PHE D 197 92.281 10.763 109.997 1.00 48.35 ATOM 4016 CG PHE D 197 91.847 11.619 111.151 1.00 50.43 ATOM 4017 CD1 PHE D 197 92.496 12.818 111.422 1.00 51.39 ATOM 4018 CD2 PHE D 197 90.812 11.214 111.995 1.00 51.03 ATOM 4019 CE1 PHE D 197 92.122 13.601 112.522 1.00 51.27 ATOM 4020 CE2 PHE D 197 90.433 11.988 113.095 1.00 49.59 ATOM 4021 CZ PHE D 197 91.087 13.181 113.358 1.00 49.70 ATOM 4022 C PHE D 197 90.082 10.824 108.856 1.00 48.38 ATOM 4023 O PHE D 197 90.387 11.911 108.379 1.00 49.86 ATOM 4024 N LYS D 198 88.826 10.396 108.925 1.00 49.00 ATOM 4025 CA LYS D 198 87.725 11.217 108.433 1.00 49.34 ATOM 4026 CB LYS D 198 86.570 10.307 107.993 1.00 49.48 ATOM 4027 C LYS D 198 87.268 12.189 109.537 1.00 49.85 ATOM 4028 O LYS D 198 87.350 11.874 110.719 1.00 50.32 ATOM 4029 N PRO D 199 86.785 13.385 109.161 1.00 50.70 ATOM 4030 CD PRO D 199 86.568 13.840 107.780 1.00 51.66 ATOM 4031 CA PRO D 199 86.321 14.400 110.116 1.00 51.18 ATOM 4032 CB PRO D 199 85.886 15.551 109.217 1.00 51.42 ATOM 4033 CG PRO D 199 85.464 14.847 107.961 1.00 52.15 ATOM 4034 C PRO D 199 85.218 13.976 111.074 1.00 51.82 ATOM 4035 O PRO D 199 85.035 14.603 112.125 1.00 52.82 ATOM 4036 N ASP D 200 84.472 12.929 110.728 1.00 52.67 ATOM 4037 CA ASP D 200 83.397 12.455 111.609 1.00 52.73 ATOM 4038 CB ASP D 200 82.415 11.550 110.879 1.00 54.01 ATOM 4039 CG ASP D 200 81.571 12.301 109.917 1.00 56.59 ATOM 4040 OD1 ASP D 200 82.109 12.649 108.841 1.00 58.29 ATOM 4041 OD2 ASP D 200 80.386 12.552 110.257 1.00 57.25 ATOM 4042 G ASP D 200 83.986 11.647 112.731 1.00 51.43 ATOM 4043 O ASP D 200 83.264 11.159 113.606 1.00 51.56 ATOM 4044 N HIS D 201 85.296 11.482 112.683 1.00 50.04 ATOM 4045 CA HIS D 201 85.995 10.714 113.697 1.00 50.04 ATOM 4046 CB HIS D 201 87.400 10.355 113.216 1.00 54.12 ATOM 4047 CG HIS D 201 87.430 9.254 112.200 1.00 59.01 ATOM 4048 CD2 HIS D 201 88.217 8.159 112.102 1.00 60.50 ATOM 4049 ND1 HIS D 201 86.591 9.220 111.103 1.00 61.62 ATOM 4050 CE1 HIS D 201 86.857 8.148 110.373 1.00 61.43 ATOM 4051 NE2 HIS D 201 87.836 7.485 110.957 1.00 61.73 ATOM 4052 G HIS D 201 86.092 11.457 115.036 1.00 48.25 ATOM 4053 O HIS D 201 86.576 10.892 116.025 1.00 49.24 ATOM 4054 N ARG D 202 85.647 12.717 115.090 1.00 44.11 ATOM 4055 CA ARG D 202 85.673 13.443 116.354 1.00 42.29 ATOM 4056 CB ARG D 202 87.067 14.035 116.596 1.00 38.00 ATOM 4057 CG ARG D 202 87.460 15.167 115.659 1.00 33.51 ATOM 4058 CD ARG D 202 88.948 15.528 115.748 1.00 27.20 ATOM 4059 NE ARG D 202 89.348 15.969 117.079 1.00 22.95 ATOM 4060 CZ ARG D 202 89.011 17.130 117.633 1.00 18.84 ATOM 4061 NH1 ARG D 202 88.259 18.008 116.987 1.00 15.62 ATOM 4062 NH2 ARG D 202 89.432 17.411 118.851 1.00 17.58 ATOM 4063 C ARG D 202 84.622 14.532 116.313 1.00 43.43 ATOM 4064 O ARG D 202 84.375 15.108 115.254 1.00 44.47 ATOM 4065 N ILE D 203 84.001 14.806 117.459 1.00 43.13 ATOM 4066 CA ILE D 203 82.970 15.840 117.525 1.00 44.86 ATOM 4067 CB ILE D 203 82.374 15.992 118.974 1.00 45.75 ATOM 4068 CG2 ILE D 203 81.579 14.742 119.350 1.00 44.96 ATOM 4069 CG1 ILE D 203 83.484 16.303 119.990 1.00 45.71 ATOM 4070 CD1 ILE D 203 84.635 15.309 120.011 1.00 46.02 ATOM 4071 C ILE D 203 83.552 17.180 117.058 1.00 45.25 ATOM 4072 O ILE D 203 84.687 17.528 117.393 1.00 44.55 ATOM 4073 N GLY D 204 82.776 17.921 116.269 1.00 45.78 ATOM 4074 CA GLY D 204 83.254 19.192 115.751 1.00 44.14 ATOM 4075 C GLY D 204 84.179 18.966 114.569 1.00 42.10 ATOM 4076 O GLY D 204 84.496 19.897 113.835 1.00 42.25 ATOM 4077 N GLY D 205 84.614 17.720 114.400 1.00 41.53 ATOM 4078 CA GLY D 205 85.494 17.359 113.300 1.00 42.52 ATOM 4079 C GLY D 205 86.826 18.076 113.305 1.00 43.08 ATOM 4080 O GLY D 205 87.429 18.274 114.367 1.00 43.80 ATOM 4081 N TYR D 206 87.284 18.468 112.118 1.00 42.12 ATOM 4082 CA TYR D 206 88.552 19.174 111.986 1.00 40.97 ATOM 4083 CB TYR D 206 89.701 18.194 112.168 1.00 43.57 ATOM 4084 CG TYR D 206 89.726 17.090 111.150 1.00 44.70 ATOM 4085 CD1 TYR D 206 89.353 15.795 111.490 1.00 46.53 ATOM 4086 CE1 TYR D 206 89.397 14.773 110.552 1.00 49.43 ATOM 4087 CD2 TYR D 206 90.138 17.341 109.845 1.00 47.44 ATOM 4088 CE2 TYR D 206 90.181 16.339 108.900 1.00 49.64 ATOM 4089 CZ TYR D 206 89.811 15.056 109.254 1.00 51.35 ATOM 4090 OH TYR D 206 89.844 14.073 108.292 1.00 53.81 ATOM 4091 C TYR D 206 88.682 19.858 110.629 1.00 40.00 ATOM 4092 O TYR D 206 88.095 19.410 109.645 1.00 39.98 ATOM 4093 N LYS D 207 89.458 20.936 110.577 1.00 39.38 ATOM 4094 CA LYS D 207 89.662 21.667 109.332 1.00 40.21 ATOM 4095 CB LYS D 207 89.458 23.173 109.563 1.00 38.02 ATOM 4096 C LYS D 207 91.054 21.400 108.736 1.00 41.63 ATOM 4097 O LYS D 207 92.067 21.362 109.454 1.00 41.52 ATOM 4098 N VAL D 208 91.090 21.206 107.418 1.00 42.22 ATOM 4099 CA VAL D 208 92.337 20.948 106.711 1.00 42.05 ATOM 4100 CB VAL D 208 92.261 19.614 105.919 1.00 41.48 ATOM 4101 CD1 VAL D 208 93.631 19.253 105.364 1.00 40.66 ATOM 4102 CG2 VAL D 208 91.745 18.505 106.816 1.00 40.29 ATOM 4103 C VAL D 208 92.626 22.081 105.736 1.00 42.09 ATOM 4104 O VAL D 208 92.114 22.079 104.626 1.00 43.46 ATOM 4105 N ARG D 209 93.429 23.053 106.151 1.00 42.59 ATOM 4106 CA ARG D 209 93.776 24.165 105.276 1.00 44.83 ATOM 4107 CB ARG D 209 94.227 25.362 106.117 1.00 44.83 ATOM 4108 C ARG D 209 94.904 23.678 104.354 1.00 45.93 ATOM 4109 O ARG D 209 96.055 23.561 104.783 1.00 46.40 ATOM 4110 N TYR D 210 94.562 23.382 103.097 1.00 46.61 ATOM 4111 CA TYR D 210 95.530 22.877 102.125 1.00 45.87 ATOM 4112 CB TYR D 210 94.814 22.377 100.882 1.00 45.46 ATOM 4113 CG TYR D 210 93.833 21.280 101.175 1.00 47.79 ATOM 4114 CD1 TYR D 210 92.470 21.552 101.287 1.00 48.81 ATOM 4115 CE1 TYR D 210 91.556 20.538 101.594 1.00 50.01 ATOM 4116 CD2 TYR D 210 94.268 19.966 101.376 1.00 48.67 ATOM 4117 CE2 TYR D 210 93.365 18.942 101.685 1.00 49.71 ATOM 4118 CZ TYR D 210 92.011 19.236 101.793 1.00 50.16 ATOM 4119 OH TYR D 210 91.117 18.233 102.101 1.00 51.87 ATOM 4120 C TYR D 210 96.573 23.899 101.725 1.00 44.94 ATOM 4121 O TYR D 210 97.716 23.545 101.414 1.00 44.92 ATOM 4122 N ALA D 211 96.178 25.168 101.728 1.00 43.47 ATOM 4123 CA ALA D 211 97.100 26.233 101.376 1.00 42.49 ATOM 4124 CB ALA D 211 96.368 27.551 101.316 1.00 41.51 ATOM 4125 C ALA D 211 98.206 26.301 102.415 1.00 42.14 ATOM 4126 O ALA D 211 99.284 26.815 102.153 1.00 42.30 ATOM 4127 N THR D 212 97.931 25.764 103.596 1.00 43.17 ATOM 4128 CA THR D 212 98.892 25.775 104.683 1.00 43.50 ATOM 4129 CB THR D 212 98.255 26.374 105.929 1.00 44.87 ATOM 4130 OG1 THR D 212 97.646 27.622 105.577 1.00 44.88 ATOM 4131 CG2 THR D 212 99.307 26.626 107.001 1.00 47.61 ATOM 4132 C THR D 212 99.459 24.392 104.994 1.00 42.04 ATOM 4133 O THR D 212 100.328 24.244 105.851 1.00 41.28 ATOM 4134 N TRP D 213 98.979 23.380 104.284 1.00 41.50 ATOM 4135 CA TRP D 213 99.477 22.030 104.499 1.00 41.66 ATOM 4136 CB TRP D 213 100.965 21.957 104.160 1.00 42.60 ATOM 4137 CG TRP D 213 101.248 22.323 102.770 1.00 44.75 ATOM 4138 CD2 TRP D 213 101.116 21.472 101.635 1.00 44.62 ATOM 4139 CE2 TRP D 213 101.425 22.245 100.498 1.00 45.13 ATOM 4140 CE3 TRP D 213 100.762 20.128 101.469 1.00 44.93 ATOM 4141 CD1 TRP D 213 101.623 23.548 102.299 1.00 45.15 ATOM 4142 NE1 TRP D 213 101.730 23.510 100.931 1.00 46.03 ATOM 4143 CZ2 TRP D 213 101.392 21.720 99.206 1.00 45.66 ATOM 4144 CZ3 TRP D 213 100.727 19.605 100.192 1.00 46.75 ATOM 4145 CH2 TRP D 213 101.042 20.402 99.071 1.00 46.85 ATOM 4146 C TRP D 213 99.309 21.671 105.953 1.00 40.31 ATOM 4147 O TRP D 213 100.199 21.085 106.565 1.00 40.74 ATOM 4148 N SER D 214 98.159 22.002 106.508 1.00 38.32 ATOM 4149 CA SER D 214 97.951 21.747 107.912 1.00 38.09 ATOM 4150 CB SER D 214 98.153 23.056 108.661 1.00 38.40 ATOM 4151 OG SER D 214 97.366 24.080 108.070 1.00 37.60 ATOM 4152 C SER D 214 96.591 21.177 108.268 1.00 37.89 ATOM 4153 O SER D 214 95.641 21.253 107.483 1.00 38.08 ATOM 4154 N ILE D 215 96.517 20.591 109.459 1.00 35.82 ATOM 4155 CA ILE D 215 95.268 20.055 109.961 1.00 34.85 ATOM 4156 CB ILE D 215 95.305 18.522 110.127 1.00 34.07 ATOM 4157 CG2 ILE D 215 96.448 18.109 111.040 1.00 33.74 ATOM 4158 CG1 ILE D 215 93.954 18.044 110.668 1.00 33.63 ATOM 4159 CD1 ILE D 215 93.741 16.544 110.588 1.00 31.56 ATOM 4160 C ILE D 215 95.051 20.732 111.306 1.00 34.51 ATOM 4161 O ILE D 215 95.996 20.944 112.068 1.00 34.28 ATOM 4162 N ILE D 216 93.804 21.086 111.588 1.00 33.79 ATOM 4163 CA ILE D 216 93.486 21.773 112.828 1.00 32.42 ATOM 4164 CB ILE D 216 93.075 23.230 112.515 1.00 32.82 ATOM 4165 CG2 ILE D 216 92.639 23.949 113.784 1.00 32.35 ATOM 4166 CG1 ILE D 216 94.249 23.947 111.848 1.00 31.96 ATOM 4167 CD1 ILE D 216 93.925 25.324 111.396 1.00 31.43 ATOM 4168 C ILE D 216 92.379 21.080 113.619 1.00 31.47 ATOM 4169 O ILE D 216 91.356 20.690 113.061 1.00 30.20 ATOM 4170 N MET D 217 92.601 20.932 114.921 1.00 30.40 ATOM 4171 CA MET D 217 91.639 20.307 115.808 1.00 31.05 ATOM 4172 CB MET D 217 92.220 19.030 116.405 1.00 31.90 ATOM 4173 CG MET D 217 92.655 18.028 115.372 1.00 34.20 ATOM 4174 SD MET D 217 92.974 16.395 116.081 1.00 39.57 ATOM 4175 CE MET D 217 94.743 16.222 115.824 1.00 33.97 ATOM 4176 C MET D 217 91.310 21.268 116.938 1.00 32.05 ATOM 4177 O MET D 217 92.201 21.789 117.604 1.00 30.41 ATOM 4178 N ASP D 218 90.019 21.482 117.150 1.00 34.51 ATOM 4179 CA ASP D 218 89.503 22.367 118.186 1.00 34.94 ATOM 4180 CB ASP D 218 88.201 22.968 117.642 1.00 35.60 ATOM 4181 CG ASP D 218 87.680 24.115 118.468 1.00 38.16 ATOM 4182 OD1 ASP D 218 87.193 23.858 119.592 1.00 40.42 ATOM 4183 OD2 ASP D 218 87.753 25.272 117.989 1.00 37.02 ATOM 4184 C ASP D 218 89.268 21.533 119.460 1.00 35.32 ATOM 4185 O ASP D 218 89.088 20.318 119.380 1.00 37.02 ATOM 4186 N SER D 219 89.294 22.181 120.623 1.00 35.62 ATOM 4187 CA SER D 219 89.073 21.525 121.916 1.00 36.41 ATOM 4188 CB SER D 219 87.616 21.757 122.361 1.00 37.09 ATOM 4189 OG SER D 219 87.424 21.434 123.736 1.00 40.88 ATOM 4190 C SER D 219 89.422 20.024 121.962 1.00 35.85 ATOM 4191 O SER D 219 88.535 19.165 122.012 1.00 35.43 ATOM 4192 N VAL D 220 90.721 19.729 121.951 1.00 35.38 ATOM 4193 CA VAL D 220 91.217 18.356 121.999 1.00 34.96 ATOM 4194 CB VAL D 220 92.725 18.305 121.745 1.00 34.89 ATOM 4195 CG1 VAL D 220 93.016 18.848 120.369 1.00 35.35 ATOM 4196 CG2 VAL D 220 93.471 19.095 122.824 1.00 34.72 ATOM 4197 C VAL D 220 90.940 17.663 123.329 1.00 34.86 ATOM 4198 O VAL D 220 91.165 18.204 124.403 1.00 35.98 ATOM 4199 N VAL D 221 90.470 16.437 123.227 1.00 34.78 ATOM 4200 CA VAL D 221 90.117 15.631 124.373 1.00 34.91 ATOM 4201 CB VAL D 221 88.632 15.251 124.235 1.00 34.42 ATOM 4202 CG1 VAL D 221 87.779 16.515 124.192 1.00 30.48 ATOM 4203 CG2 VAL D 221 88.423 14.475 122.935 1.00 30.80 ATOM 4204 C VAL D 221 91.000 14.374 124.353 1.00 35.97 ATOM 4205 O VAL D 221 91.607 14.056 123.332 1.00 37.52 ATOM 4206 N PRO D 222 91.068 13.637 125.469 1.00 35.56 ATOM 4207 CD PRO D 222 90.372 13.891 126.742 1.00 35.68 ATOM 4208 CA PRO D 222 91.883 12.419 125.555 1.00 34.78 ATOM 4209 CB PRO D 222 91.426 11.801 126.874 1.00 36.22 ATOM 4210 CG PRO D 222 91.150 13.011 127.712 1.00 36.43 ATOM 4211 C PRO D 222 91.714 11.458 124.383 1.00 33.09 ATOM 4212 O PRO D 222 92.682 10.842 123.935 1.00 33.47 ATOM 4213 N SER D 223 90.490 11.325 123.887 1.00 31.05 ATOM 4214 CA SER D 223 90.250 10.412 122.783 1.00 31.65 ATOM 4215 CB SER D 223 88.761 10.353 122.460 1.00 29.34 ATOM 4216 OG SER D 223 88.308 11.570 121.913 1.00 32.73 ATOM 4217 C SER D 223 91.041 10.824 121.545 1.00 32.52 ATOM 4218 O SER D 223 91.237 10.033 120.627 1.00 33.05 ATOM 4219 N ASP D 224 91.501 12.068 121.524 1.00 33.64 ATOM 4220 CA ASP D 224 92.276 12.556 120.394 1.00 33.83 ATOM 4221 CB ASP D 224 92.216 14.088 120.303 1.00 33.17 ATOM 4222 CG ASP D 224 90.866 14.593 119.820 1.00 33.79 ATOM 4223 OD1 ASP D 224 90.395 14.105 118.769 1.00 35.24 ATOM 4224 OD2 ASP D 224 90.278 15.478 120.482 1.00 32.14 ATOM 4225 C ASP D 224 93.723 12.116 120.515 1.00 34.68 ATOM 4226 O ASP D 224 94.450 12.112 119.531 1.00 35.14 ATOM 4227 N LYS D 225 94.146 11.753 121.722 1.00 35.77 ATOM 4228 CA LYS D 225 95.527 11.323 121.923 1.00 36.05 ATOM 4229 CB LYS D 225 95.731 10.715 123.315 1.00 39.64 ATOM 4230 CG LYS D 225 95.658 11.662 124.489 1.00 40.94 ATOM 4231 CD LYS D 225 96.158 10.947 125.731 1.00 42.47 ATOM 4232 CE LYS D 225 95.590 11.577 126.984 1.00 46.13 ATOM 4233 NZ LYS D 225 96.280 11.098 128.215 1.00 48.29 ATOM 4234 C LYS D 225 95.907 10.274 120.890 1.00 34.81 ATOM 4235 O LYS D 225 95.151 9.332 120.636 1.00 33.69 ATOM 4236 N GLY D 226 97.084 10.432 120.301 1.00 33.57 ATOM 4237 CA GLY D 226 97.522 9.469 119.309 1.00 34.57 ATOM 4238 C GLY D 226 98.568 10.003 118.352 1.00 34.49 ATOM 4239 O GLY D 226 99.121 11.087 118.561 1.00 34.89 ATOM 4240 N ASN D 227 98.840 9.231 117.303 1.00 33.54 ATOM 4241 CA ASN D 227 99.815 9.604 116.293 1.00 32.79 ATOM 4242 CB ASN D 227 100.679 8.401 115.923 1.00 32.45 ATOM 4243 CG ASN D 227 101.640 8.011 117.023 1.00 33.66 ATOM 4244 OD1 ASN D 227 102.419 8.841 117.511 1.00 34.74 ATOM 4245 ND2 ASN D 227 101.602 6.743 117.413 1.00 30.46 ATOM 4246 C ASN D 227 99.123 10.098 115.038 1.00 32.66 ATOM 4247 O ASN D 227 98.194 9.471 114.551 1.00 33.96 ATOM 4248 N TYR D 228 99.569 11.226 114.511 1.00 32.63 ATOM 4249 CA TYR D 228 98.977 11.735 113.289 1.00 32.20 ATOM 4250 CB TYR D 228 98.333 13.089 113.532 1.00 30.83 ATOM 4251 CG TYR D 228 97.209 12.983 114.498 1.00 28.79 ATOM 4252 CD1 TYR D 228 97.451 12.854 115.859 1.00 28.66 ATOM 4253 CE1 TYR D 228 96.417 12.689 116.748 1.00 30.07 ATOM 4254 CD2 TYR D 228 95.900 12.946 114.050 1.00 31.02 ATOM 4255 CE2 TYR D 228 94.851 12.782 114.929 1.00 31.42 ATOM 4256 CZ TYR D 228 95.115 12.656 116.273 1.00 31.27 ATOM 4257 OH TYR D 228 94.062 12.516 117.136 1.00 34.09 ATOM 4258 C TYR D 228 100.073 11.843 112.250 1.00 32.68 ATOM 4259 O TYR D 228 101.134 12.412 112.511 1.00 32.76 ATOM 4260 N THR D 229 99.815 11.278 111.075 1.00 32.13 ATOM 4261 CA THR D 229 100.785 11.305 109.992 1.00 30.62 ATOM 4262 CB THR D 229 101.199 9.891 109.600 1.00 30.56 ATOM 4263 OG1 THR D 229 101.602 9.176 110.770 1.00 31.01 ATOM 4264 CG2 THR D 229 102.357 9.934 108.629 1.00 31.89 ATOM 4265 C THR D 229 100.250 12.000 108.756 1.00 29.30 ATOM 4266 O THR D 229 99.148 11.716 108.309 1.00 28.58 ATOM 4267 N CYS D 230 101.028 12.928 108.217 1.00 30.51 ATOM 4268 CA CYS D 230 100.610 13.621 107.011 1.00 32.35 ATOM 4269 C CYS D 230 101.289 12.904 105.858 1.00 32.87 ATOM 4270 O CYS D 230 102.423 12.417 105.979 1.00 33.82 ATOM 4271 CB CYS D 230 101.026 15.088 107.029 1.00 32.58 ATOM 4272 SG CYS D 230 102.817 15.348 107.184 1.00 39.09 ATOM 4273 N ILE D 231 100.577 12.825 104.746 1.00 32.40 ATOM 4274 CA ILE D 231 101.081 12.154 103.574 1.00 32.93 ATOM 4275 CB ILE D 231 100.256 10.881 103.314 1.00 33.24 ATOM 4276 CG2 ILE D 231 100.826 10.114 102.137 1.00 31.63 ATOM 4277 CG1 ILE D 231 100.263 10.015 104.577 1.00 32.96 ATOM 4278 CD1 ILE D 231 99.708 8.642 104.375 1.00 34.35 ATOM 4279 C ILE D 231 100.958 13.100 102.401 1.00 33.48 ATOM 4280 O ILE D 231 99.849 13.355 101.922 1.00 33.16 ATOM 4281 N VAL D 232 102.094 13.645 101.971 1.00 33.93 ATOM 4282 CA VAL D 232 102.134 14.556 100.834 1.00 36.17 ATOM 4283 CB VAL D 232 103.091 15.718 101.072 1.00 34.31 ATOM 4284 CG1 VAL D 232 103.078 16.635 99.879 1.00 34.18 ATOM 4285 CG2 VAL D 232 102.691 16.462 102.324 1.00 34.98 ATOM 4286 C VAL D 232 102.647 13.721 99.678 1.00 39.40 ATOM 4287 O VAL D 232 103.707 13.092 99.775 1.00 39.92 ATOM 4288 N GLU D 233 101.907 13.709 98.579 1.00 42.11 ATOM 4289 CA GLU D 233 102.320 12.875 97.474 1.00 44.91 ATOM 4290 CB GLU D 233 101.752 11.482 97.710 1.00 46.98 ATOM 4291 CG GLU D 233 101.754 10.584 96.507 1.00 54.51 ATOM 4292 CD GLU D 233 101.552 9.132 96.892 1.00 59.37 ATOM 4293 OE1 GLU D 233 100.659 8.864 97.739 1.00 61.58 ATOM 4294 OE2 GLU D 233 102.288 8.267 96.348 1.00 59.83 ATOM 4295 C GLU D 233 101.941 13.363 96.090 1.00 45.68 ATOM 4296 O GLU D 233 100.961 14.096 95.926 1.00 45.02 ATOM 4297 N ASN D 234 102.747 12.958 95.105 1.00 45.84 ATOM 4298 CA ASN D 234 102.516 13.281 93.701 1.00 45.22 ATOM 4299 CB ASN D 234 103.183 14.614 93.314 1.00 45.24 ATOM 4300 CG ASN D 234 104.641 14.468 92.946 1.00 44.43 ATOM 4301 OD1 ASN D 234 105.256 13.422 93.165 1.00 44.59 ATOM 4302 ND2 ASN D 234 105.210 15.534 92.385 1.00 40.85 ATOM 4303 C ASN D 234 103.060 12.112 92.888 1.00 45.49 ATOM 4304 O ASN D 234 103.561 11.149 93.464 1.00 45.48 ATOM 4305 N GLU D 235 102.965 12.194 91.564 1.00 46.96 ATOM 4306 CA GLU D 235 103.410 11.110 90.687 1.00 47.27 ATOM 4307 CB GLU D 235 103.165 11.494 89.218 1.00 46.16 ATOM 4308 C GLU D 235 104.857 10.643 90.851 1.00 47.83 ATOM 4309 O GLU D 235 105.171 9.496 90.533 1.00 48.35 ATOM 4310 N TYR D 236 105.735 11.498 91.368 1.00 48.23 ATOM 4311 CA TYR D 236 107.139 11.110 91.492 1.00 48.07 ATOM 4312 CB TYR D 236 108.000 12.221 90.905 1.00 51.78 ATOM 4313 CG TYR D 236 107.449 12.674 89.579 1.00 56.38 ATOM 4314 CD1 TYR D 236 106.553 13.744 89.501 1.00 58.00 ATOM 4315 CE1 TYR D 236 105.976 14.112 88.286 1.00 60.31 ATOM 4316 CD2 TYR D 236 107.757 11.981 88.408 1.00 57.90 ATOM 4317 CE2 TYR D 236 107.184 12.337 87.190 1.00 60.14 ATOM 4318 CZ TYR D 236 106.298 13.401 87.135 1.00 61.38 ATOM 4319 OH TYR D 236 105.748 13.758 85.925 1.00 62.75 ATOM 4320 C TYR D 236 107.638 10.728 92.876 1.00 45.71 ATOM 4321 O TYR D 236 108.803 10.372 93.049 1.00 45.60 ATOM 4322 N GLY D 237 106.758 10.783 93.863 1.00 43.72 ATOM 4323 CA GLY D 237 107.177 10.429 95.202 1.00 42.52 ATOM 4324 C GLY D 237 106.233 10.922 96.275 1.00 42.32 ATOM 4325 O GLY D 237 105.280 11.661 95.996 1.00 42.37 ATOM 4326 N SER D 238 106.493 10.497 97.509 1.00 40.93 ATOM 4327 CA SER D 238 105.678 10.895 98.643 1.00 38.31 ATOM 4328 CB SER D 238 104.607 9.848 98.912 1.00 37.78 ATOM 4329 OG SER D 238 105.218 8.650 99.344 1.00 39.41 ATOM 4330 C SER D 238 106.559 11.027 99.871 1.00 37.41 ATOM 4331 O SER D 238 107.577 10.350 99.993 1.00 36.75 ATOM 4332 N ILE D 239 106.166 11.919 100.772 1.00 37.40 ATOM 4333 CA ILE D 239 106.885 12.138 102.028 1.00 37.41 ATOM 4334 CB ILE D 239 107.571 13.516 102.117 1.00 37.31 ATOM 4335 CG2 ILE D 239 109.017 13.429 101.703 1.00 36.88 ATOM 4336 CG1 ILE D 239 106.777 14.527 101.305 1.00 38.29 ATOM 4337 CD1 ILE D 239 107.409 15.895 101.252 1.00 42.39 ATOM 4338 C ILE D 239 105.828 12.151 103.098 1.00 38.18 ATOM 4339 O ILE D 239 104.672 12.502 102.825 1.00 38.68 ATOM 4340 N ASN D 240 106.220 11.777 104.311 1.00 38.07 ATOM 4341 CA ASN D 240 105.292 11.775 105.434 1.00 39.19 ATOM 4342 CB ASN D 240 104.696 10.375 105.660 1.00 41.17 ATOM 4343 CG ASN D 240 105.743 9.348 106.072 1.00 43.52 ATOM 4344 CD1 ASN D 240 106.601 9.622 106.912 1.00 47.31 ATOM 4345 ND2 ASN D 240 105.665 8.153 105.494 1.00 43.18 ATOM 4346 C ASN D 240 105.999 12.246 106.697 1.00 38.45 ATOM 4347 O ASN D 240 107.226 12.240 106.778 1.00 38.26 ATOM 4348 N HIS D 241 105.218 12.668 107.681 1.00 38.00 ATOM 4349 CA HIS D 241 105.777 13.125 108.945 1.00 37.35 ATOM 4350 CB HIS D 241 106.127 14.621 108.868 1.00 38.82 ATOM 4351 CG HIS D 241 106.784 15.166 110.104 1.00 40.90 ATOM 4352 CD2 HIS D 241 106.499 16.256 110.857 1.00 40.95 ATOM 4353 ND1 HIS D 241 107.897 14.588 110.680 1.00 41.06 ATOM 4354 CE1 HIS D 241 108.266 15.298 111.733 1.00 39.83 ATOM 4355 NE2 HIS D 241 107.434 16.315 111.861 1.00 40.11 ATOM 4356 C HIS D 241 104.713 12.873 109.996 1.00 36.27 ATOM 4357 O HIS D 241 103.531 13.167 109.784 1.00 36.50 ATOM 4358 N THR D 242 105.125 12.320 111.125 1.00 34.08 ATOM 4359 CA THR D 242 104.171 12.037 112.173 1.00 33.41 ATOM 4360 CB THR D 242 104.208 10.557 112.512 1.00 33.88 ATOM 4361 OG1 THR D 242 104.178 9.820 111.286 1.00 34.73 ATOM 4362 CG2 THR D 242 103.001 10.166 113.359 1.00 32.87 ATOM 4363 C THR D 242 104.390 12.880 113.422 1.00 32.39 ATOM 4364 O THR D 242 105.515 13.202 113.785 1.00 31.61 ATOM 4365 N TYR D 243 103.286 13.266 114.047 1.00 33.00 ATOM 4366 CA TYR D 243 103.308 14.064 115.267 1.00 33.46 ATOM 4367 CB TYR D 243 102.534 15.373 115.093 1.00 33.45 ATOM 4368 CG TYR D 243 103.207 16.364 114.190 1.00 32.79 ATOM 4369 CD1 TYR D 243 102.642 16.715 112.960 1.00 30.88 ATOM 4370 CE1 TYR D 243 103.287 17.616 112.106 1.00 31.50 ATOM 4371 CD2 TYR D 243 104.430 16.937 114.552 1.00 32.94 ATOM 4372 CE2 TYR D 243 105.086 17.842 113.706 1.00 33.56 ATOM 4373 CZ TYR D 243 104.511 18.175 112.482 1.00 32.47 ATOM 4374 OH TYR D 243 105.177 19.042 111.641 1.00 30.66 ATOM 4375 C TYR D 243 102.640 13.247 116.351 1.00 33.10 ATOM 4376 O TYR D 243 101.782 12.400 116.077 1.00 32.05 ATOM 4377 N GLN D 244 103.031 13.491 117.588 1.00 33.55 ATOM 4378 CA GLN D 244 102.424 12.745 118.661 1.00 35.12 ATOM 4379 CB GLN D 244 103.481 12.044 119.495 1.00 37.87 ATOM 4380 CG GLN D 244 102.937 10.835 120.198 1.00 43.93 ATOM 4381 CD GLN D 244 103.911 10.283 121.205 1.00 48.46 ATOM 4382 OE1 GLN D 244 105.119 10.215 120.943 1.00 51.99 ATOM 4383 NE2 GLN D 244 103.398 9.879 122.367 1.00 47.54 ATOM 4384 C GLN D 244 101.642 13.719 119.507 1.00 33.39 ATOM 4385 O GLN D 244 102.172 14.740 119.947 1.00 31.94 ATOM 4386 N LEU D 245 100.365 13.419 119.699 1.00 31.77 ATOM 4387 CA LEU D 245 99.535 14.285 120.504 1.00 32.20 ATOM 4388 CB LEU D 245 98.189 14.607 119.818 1.00 32.50 ATOM 4389 CG LEU D 245 97.244 15.496 120.658 1.00 32.01 ATOM 4390 CD1 LEU D 245 97.931 16.802 120.993 1.00 31.78 ATOM 4391 CD2 LEU D 245 95.952 15.779 119.922 1.00 33.00 ATOM 4392 C LEU D 245 99.279 13.635 121.842 1.00 31.58 ATOM 4393 O LEU D 245 98.968 12.447 121.932 1.00 30.22 ATOM 4394 N ASP D 246 99.432 14.437 122.883 1.00 32.78 ATOM 4395 CA ASP D 246 99.199 13.994 124.239 1.00 33.03 ATOM 4396 CB ASP D 246 100.521 13.828 124.963 1.00 34.24 ATOM 4397 CG ASP D 246 100.369 13.061 126.240 1.00 38.04 ATOM 4398 CD1 ASP D 246 101.348 12.968 127.014 1.00 40.39 ATOM 4399 CD2 ASP D 246 99.255 12.544 126.464 1.00 41.31 ATOM 4400 C ASP D 246 98.369 15.077 124.915 1.00 33.21 ATOM 4401 O ASP D 246 98.793 16.233 124.987 1.00 33.23 ATOM 4402 N VAL D 247 97.181 14.702 125.388 1.00 34.04 ATOM 4403 CA VAL D 247 96.259 15.634 126.053 1.00 34.00 ATOM 4404 CB VAL D 247 94.819 15.478 125.507 1.00 33.34 ATOM 4405 CG1 VAL D 247 93.957 16.651 125.942 1.00 31.80 ATOM 4406 CG2 VAL D 247 94.849 15.355 123.997 1.00 35.20 ATOM 4407 C VAL D 247 96.204 15.358 127.557 1.00 34.12 ATOM 4408 O VAL D 247 95.933 14.228 127.970 1.00 32.75 ATOM 4409 N VAL D 248 96.438 16.394 128.365 1.00 33.95 ATOM 4410 CA VAL D 248 96.414 16.264 129.822 1.00 34.42 ATOM 4411 CB VAL D 248 97.650 16.919 130.475 1.00 33.86 ATOM 4412 CG1 VAL D 248 97.646 16.649 131.954 1.00 33.01 ATOM 4413 CG2 VAL D 248 98.925 16.407 129.844 1.00 35.22 ATOM 4414 C VAL D 248 95.202 16.965 130.415 1.00 35.72 ATOM 4415 O VAL D 248 94.969 18.134 130.116 1.00 35.44 ATOM 4416 N GLU D 249 94.438 16.255 131.246 1.00 36.91 ATOM 4417 CA GLU D 249 93.272 16.836 131.917 1.00 38.36 ATOM 4418 CB GLU D 249 92.182 15.787 132.122 1.00 41.10 ATOM 4419 CG GLU D 249 91.599 15.230 130.847 1.00 46.18 ATOM 4420 CD GLU D 249 90.669 14.058 131.103 1.00 48.79 ATOM 4421 OE1 GLU D 249 91.133 13.032 131.662 1.00 50.76 ATOM 4422 OE2 GLU D 249 89.476 14.166 130.743 1.00 49.83 ATOM 4423 C GLU D 249 93.773 17.262 133.289 1.00 37.17 ATOM 4424 O GLU D 249 94.255 16.417 134.030 1.00 37.43 ATOM 4425 N ARG D 250 93.675 18.544 133.648 1.00 36.72 ATOM 4426 CA ARG D 250 94.156 18.956 134.986 1.00 35.30 ATOM 4427 CB ARG D 250 94.622 20.427 135.022 1.00 32.09 ATOM 4428 CG ARG D 250 95.801 20.729 134.091 1.00 31.09 ATOM 4429 CD ARG D 250 96.960 19.717 134.237 1.00 27.53 ATOM 4430 NE ARG D 250 97.736 19.907 135.466 1.00 27.19 ATOM 4431 CZ ARG D 250 98.601 20.901 135.671 1.00 23.34 ATOM 4432 NH1 ARG D 250 98.819 21.807 134.733 1.00 24.08 ATOM 4433 NH2 ARG D 250 99.236 21.005 136.824 1.00 20.42 ATOM 4434 C ARG D 250 93.146 18.699 136.123 1.00 35.26 ATOM 4435 O ARG D 250 92.000 18.335 135.877 1.00 36.33 ATOM 4436 N SER D 251 93.642 18.752 137.373 1.00 36.16 ATOM 4437 CA SER D 251 92.839 18.539 138.596 1.00 35.07 ATOM 4438 CB SER D 251 93.267 17.254 139.308 1.00 33.85 ATOM 4439 OG SER D 251 93.280 16.152 138.433 1.00 33.32 ATOM 4440 C SER D 251 93.050 19.708 139.564 1.00 35.84 ATOM 4441 O SER D 251 93.706 19.560 140.601 1.00 36.47 ATOM 4442 N PRO D 252 92.505 20.888 139.235 1.00 36.42 ATOM 4443 CD PRO D 252 91.828 21.237 137.975 1.00 37.05 ATOM 4444 CA PRO D 252 92.655 22.070 140.088 1.00 36.24 ATOM 4445 CB PRO D 252 92.319 23.219 139.147 1.00 34.89 ATOM 4446 CG PRO D 252 91.286 22.625 138.277 1.00 37.22 ATOM 4447 C PRO D 252 91.790 22.066 141.334 1.00 36.91 ATOM 4448 O PRO D 252 90.850 22.854 141.469 1.00 36.54 ATOM 4449 N HIS D 253 92.122 21.166 142.247 1.00 37.49 ATOM 4450 CA HIS D 253 91.406 21.063 143.501 1.00 39.08 ATOM 4451 CB HIS D 253 90.229 20.073 143.366 1.00 42.98 ATOM 4452 CG HIS D 253 90.599 18.724 142.823 1.00 46.99 ATOM 4453 CD2 HIS D 253 90.222 18.090 141.686 1.00 48.65 ATOM 4454 ND1 HIS D 253 91.398 17.830 143.511 1.00 50.87 ATOM 4455 CE1 HIS D 253 91.492 16.703 142.823 1.00 51.49 ATOM 4456 NE2 HIS D 253 90.786 16.835 141.712 1.00 50.65 ATOM 4457 C HIS D 253 92.372 20.652 144.608 1.00 36.52 ATOM 4458 O HIS D 253 93.441 20.112 144.323 1.00 36.08 ATOM 4459 N ARG D 254 92.005 20.933 145.857 1.00 34.39 ATOM 4460 CA ARG D 254 92.838 20.590 147.000 1.00 32.02 ATOM 4461 CB ARG D 254 92.187 21.070 148.290 1.00 35.17 ATOM 4462 CG ARG D 254 90.937 20.319 148.714 1.00 40.73 ATOM 4463 CD ARG D 254 90.271 21.102 149.827 1.00 45.75 ATOM 4464 NE ARG D 254 89.412 20.288 150.677 1.00 51.38 ATOM 4465 CZ ARG D 254 88.375 19.586 150.237 1.00 55.43 ATOM 4466 NH1 ARG D 254 88.071 19.590 148.942 1.00 58.96 ATOM 4467 NH2 ARG D 254 87.624 18.904 151.094 1.00 55.71 ATOM 4468 C ARG D 254 93.059 19.092 147.045 1.00 29.52 ATOM 4469 O ARG D 254 92.338 18.342 146.393 1.00 30.17 ATOM 4470 N PRO D 255 94.071 18.634 147.803 1.00 27.73 ATOM 4471 CD PRO D 255 95.023 19.467 148.565 1.00 24.12 ATOM 4472 CA PRO D 255 94.392 17.199 147.926 1.00 25.71 ATOM 4473 CB PRO D 255 95.511 17.190 148.968 1.00 24.99 ATOM 4474 CG PRO D 255 96.191 18.531 148.754 1.00 24.65 ATOM 4475 C PRO D 255 93.213 16.314 148.344 1.00 25.05 ATOM 4476 O PRO D 255 92.296 16.770 149.018 1.00 24.12 ATOM 4477 N ILE D 256 93.241 15.050 147.931 1.00 26.53 ATOM 4478 CA ILE D 256 92.190 14.096 148.284 1.00 27.73 ATOM 4479 CB ILE D 256 91.420 13.556 147.047 1.00 26.74 ATOM 4480 CG2 ILE D 256 90.767 12.231 147.382 1.00 26.27 ATOM 4481 CG1 ILE D 256 90.341 14.553 146.621 1.00 24.87 ATOM 4482 CD1 ILE D 256 90.850 15.688 145.775 1.00 25.75 ATOM 4483 C ILE D 256 92.842 12.921 148.981 1.00 28.99 ATOM 4484 O ILE D 256 93.811 12.348 148.471 1.00 30.56 ATOM 4485 N LEU D 257 92.313 12.564 150.145 1.00 28.90 ATOM 4486 CA LEU D 257 92.862 11.449 150.909 1.00 29.82 ATOM 4487 CB LEU D 257 92.973 11.863 152.389 1.00 30.22 ATOM 4488 CG LEU D 257 93.644 13.245 152.571 1.00 33.19 ATOM 4489 CD1 LEU D 257 93.479 13.776 153.996 1.00 31.95 ATOM 4490 CD2 LEU D 257 95.113 13.146 152.208 1.00 32.87 ATOM 4491 C LEU D 257 91.945 10.240 150.709 1.00 28.77 ATOM 4492 O LEU D 257 90.729 10.401 150.619 1.00 28.70 ATOM 4493 N GLN D 258 92.512 9.041 150.596 1.00 27.83 ATOM 4494 CA GLN D 258 91.664 7.863 150.411 1.00 29.70 ATOM 4495 CB GLN D 258 92.497 6.580 150.272 1.00 28.42 ATOM 4496 C GLN D 258 90.763 7.762 151.632 1.00 29.85 ATOM 4497 O GLN D 258 91.226 7.912 152.773 1.00 31.42 ATOM 4498 N ALA D 259 89.475 7.536 151.401 1.00 27.97 ATOM 4499 CA ALA D 259 88.554 7.423 152.510 1.00 26.07 ATOM 4500 CE ALA D 259 87.146 7.384 152.001 1.00 24.75 ATOM 4501 C ALA D 259 88.903 6.141 153.252 1.00 27.29 ATOM 4502 O ALA D 259 89.340 5.165 152.640 1.00 26.71 ATOM 4503 N GLY D 260 88.747 6.159 154.573 1.00 27.98 ATOM 4504 CA GLY D 260 89.047 4.982 155.365 1.00 28.73 ATOM 4505 C GLY D 260 90.465 4.897 155.903 1.00 30.14 ATOM 4506 O GLY D 260 90.777 3.963 156.640 1.00 31.06 ATOM 4507 N LEU D 261 91.311 5.866 155.549 1.00 30.20 ATOM 4508 CA LEU D 261 92.714 5.900 155.979 1.00 30.06 ATOM 4509 CB LEU D 261 93.619 5.501 154.809 1.00 28.40 ATOM 4510 CG LEU D 261 93.420 4.108 154.217 1.00 27.35 ATOM 4511 CD1 LEU D 261 94.115 3.975 152.871 1.00 26.70 ATOM 4512 CD2 LEU D 261 93.945 3.097 155.199 1.00 23.13 ATOM 4513 C LEU D 261 93.120 7.298 156.440 1.00 30.61 ATOM 4514 O LEU D 261 92.839 8.275 155.753 1.00 33.23 ATOM 4515 N PRO D 262 93.804 7.413 157.593 1.00 30.88 ATOM 4516 CD PRO D 262 94.125 8.712 158.211 1.00 30.49 ATOM 4517 CA PRO D 262 94.210 6.314 158.478 1.00 30.82 ATOM 4518 CB PRO D 262 95.108 7.007 159.500 1.00 30.09 ATOM 4519 CG PRO D 262 94.453 8.323 159.648 1.00 29.04 ATOM 4520 C PRO D 262 92.988 5.705 159.132 1.00 29.98 ATOM 4521 O PRO D 262 91.935 6.341 159.211 1.00 29.28 ATOM 4522 N ALA D 263 93.123 4.469 159.594 1.00 29.91 ATOM 4523 CA ALA D 263 92.001 3.809 160.255 1.00 30.35 ATOM 4524 CB ALA D 263 91.743 2.421 159.641 1.00 28.77 ATOM 4525 C ALA D 263 92.250 3.684 161.750 1.00 29.36 ATOM 4526 O ALA D 263 93.392 3.646 162.206 1.00 27.15 ATOM 4527 N ASN D 264 91.168 3.651 162.514 1.00 30.53 ATOM 4528 CA ASN D 264 91.289 3.495 163.945 1.00 31.88 ATOM 4529 CB ASN D 264 89.917 3.445 164.598 1.00 31.69 ATOM 4530 CG ASN D 264 89.206 4.744 164.501 1.00 33.36 ATOM 4531 OD1 ASN D 264 89.845 5.797 164.471 1.00 34.00 ATOM 4532 ND2 ASN D 264 87.873 4.700 164.463 1.00 36.85 ATOM 4533 C ASN D 264 92.024 2.190 164.215 1.00 32.38 ATOM 4534 O ASN D 264 91.845 1.204 163.499 1.00 30.61 ATOM 4535 N LYS D 265 92.852 2.195 165.253 1.00 33.51 ATOM 4536 CA LYS D 265 93.620 1.023 165.624 1.00 34.84 ATOM 4537 CB LYS D 265 95.106 1.209 165.275 1.00 36.12 ATOM 4538 CG LYS D 265 95.388 1.866 163.932 1.00 38.63 ATOM 4539 CD LYS D 265 94.975 1.003 162.761 1.00 39.25 ATOM 4540 CE LYS D 265 96.191 0.440 162.060 1.00 39.05 ATOM 4541 NZ LYS D 265 97.026 1.523 161.471 1.00 39.06 ATOM 4542 C LYS D 265 93.524 0.788 167.121 1.00 36.31 ATOM 4543 O LYS D 265 93.691 1.715 167.911 1.00 38.31 ATOM 4544 N THR D 266 93.240 0.447 167.515 1.00 37.04 ATOM 4545 CA THR D 266 93.210 0.790 168.926 1.00 37.70 ATOM 4546 CB THR D 266 91.882 1.444 169.345 1.00 36.73 ATOM 4547 OG1 THR D 266 90.837 0.468 169.294 1.00 37.40 ATOM 4548 CG2 THR D 266 91.977 1.990 170.769 1.00 37.09 ATOM 4549 C THR D 266 94.349 1.794 169.078 1.00 39.32 ATOM 4550 O THR D 266 94.422 2.774 168.350 1.00 38.85 ATOM 4551 N VAL D 267 95.269 1.530 169.995 1.00 42.44 ATOM 4552 CA VAL D 267 96.386 2.444 170.201 1.00 44.11 ATOM 4553 CB VAL D 267 97.636 1.990 169.439 1.00 43.44 ATOM 4554 CG1 VAL D 267 97.387 2.084 167.942 1.00 43.56 ATOM 4555 CG2 VAL D 267 97.994 0.577 169.845 1.00 43.00 ATOM 4556 C VAL D 267 96.760 2.599 171.669 1.00 45.67 ATOM 4557 O VAL D 267 96.228 1.895 172.545 1.00 44.80 ATOM 4558 N ALA D 268 97.676 3.535 171.921 1.00 46.81 ATOM 4559 CA ALA D 268 98.153 3.831 173.270 1.00 46.58 ATOM 4560 CB ALA D 268 98.563 5.288 173.373 1.00 44.62 ATOM 4561 C ALA D 268 99.335 2.942 173.602 1.00 46.29 ATOM 4562 O ALA D 268 100.121 2.592 172.722 1.00 44.98 ATOM 4563 N LEU D 269 99.452 2.578 174.876 1.00 47.03 ATOM 4564 CA LEU D 269 100.548 1.731 175.334 1.00 47.97 ATOM 4565 CB LEU D 269 100.533 1.626 176.869 1.00 47.45 ATOM 4566 CG LEU D 269 101.303 0.473 177.541 1.00 48.73 ATOM 4567 CD1 LEU D 269 101.066 0.503 179.041 1.00 47.47 ATOM 4568 CD2 LEU D 269 102.800 0.570 177.240 1.00 49.24 ATOM 4569 C LEU D 269 101.859 2.354 174.861 1.00 48.02 ATOM 4570 O LEU D 269 102.082 3.548 175.052 1.00 48.67 ATOM 4571 N GLY D 270 102.712 1.551 174.230 1.00 47.32 ATOM 4572 CA GLY D 270 103.989 2.060 173.761 1.00 47.45 ATOM 4573 C GLY D 270 104.044 2.496 172.307 1.00 47.67 ATOM 4574 O GLY D 270 105.125 2.778 171.784 1.00 47.93 ATOM 4575 N SER D 271 102.895 2.552 171.643 1.00 47.17 ATOM 4576 CA SER D 271 102.861 2.965 170.246 1.00 46.98 ATOM 4577 CB SER D 271 101.416 3.160 169.795 1.00 46.79 ATOM 4578 OG SER D 271 100.759 4.117 170.611 1.00 50.01 ATOM 4579 C SER D 271 103.562 1.964 169.327 1.00 47.46 ATOM 4580 O SER D 271 104.065 0.933 169.770 1.00 47.22 ATOM 4581 N ASN D 272 103.602 2.288 168.042 1.00 47.66 ATOM 4582 CA ASN D 272 104.220 1.425 167.045 1.00 48.16 ATOM 4583 CB ASN D 272 105.418 2.118 166.394 1.00 47.89 ATOM 4584 CG ASN D 272 106.677 1.978 167.204 1.00 48.55 ATOM 4585 001 ASN D 272 107.266 0.901 167.263 1.00 49.20 ATOM 4586 ND2 ASN D 272 107.099 3.063 167.841 1.00 49.75 ATOM 4587 C ASN D 272 103.179 1.127 165.986 1.00 48.54 ATOM 4588 O ASN D 272 103.003 1.902 165.049 1.00 51.19 ATOM 4589 N VAL D 273 102.484 0.008 166.133 1.00 47.34 ATOM 4590 CA VAL D 273 101.452 0.368 165.172 1.00 47.18 ATOM 4591 CB VAL D 273 100.245 1.014 165.909 1.00 48.44 ATOM 4592 CG1 VAL D 273 100.692 2.319 166.584 1.00 49.44 ATOM 4593 CG2 VAL D 273 99.093 1.269 164.936 1.00 47.73 ATOM 4594 C VAL D 273 101.989 1.355 164.121 1.00 45.31 ATOM 4595 O VAL D 273 102.945 2.090 164.377 1.00 45.17 ATOM 4596 N GLU D 274 101.385 1.353 162.934 1.00 42.57 ATOM 4597 CA GLU D 274 101.778 2.281 161.876 1.00 40.24 ATOM 4598 CB GLU D 274 102.807 1.650 160.942 1.00 41.03 ATOM 4599 CG GLU D 274 102.204 0.676 159.951 1.00 43.76 ATOM 4600 CD GLU D 274 103.232 0.089 159.019 1.00 44.63 ATOM 4601 OE1 GLU D 274 104.294 0.338 159.533 1.00 47.63 ATOM 4602 OE2 GLU D 274 102.979 0.046 157.789 1.00 42.57 ATOM 4603 C GLU D 274 100.533 2.673 161.081 1.00 37.93 ATOM 4604 O GLU D 274 99.781 1.815 160.617 1.00 36.45 ATOM 4605 N PHE D 275 100.317 3.976 160.934 1.00 36.52 ATOM 4606 CA PHE D 275 99.155 4.499 160.210 1.00 33.93 ATOM 4607 CB PHE D 275 98.654 5.787 160.860 1.00 32.58 ATOM 4608 CG PHE D 275 98.012 5.585 162.206 1.00 29.81 ATOM 4609 CD1 PHE D 275 96.732 5.052 162.307 1.00 28.52 ATOM 4610 C02 PHE D 275 98.682 5.950 163.373 1.00 26.90 ATOM 4611 CE1 PHE D 275 96.127 4.893 163.554 1.00 30.09 ATOM 4612 CE2 PHE D 275 98.088 5.794 164.619 1.00 26.27 ATOM 4613 CZ PHE D 275 96.811 5.267 164.713 1.00 28.01 ATOM 4614 C PHE D 275 99.465 4.779 158.758 1.00 33.21 ATOM 4615 O PHE D 275 100.619 4.954 158.380 1.00 32.57 ATOM 4616 N MET D 276 98.414 4.829 157.950 1.00 33.97 ATOM 4617 CA MET D 276 98.552 5.090 156.529 1.00 34.49 ATOM 4618 CB MET D 276 98.052 3.923 155.713 1.00 38.18 ATOM 4619 CG MET D 276 98.799 2.645 155.872 1.00 44.09 ATOM 4620 SD MET D 276 98.473 1.821 154.327 1.00 50.23 ATOM 4621 CE MET D 276 99.686 2.703 153.271 1.00 48.04 ATOM 4622 C MET D 276 97.724 6.274 156.107 1.00 34.32 ATOM 4623 O MET D 276 96.730 6.619 156.747 1.00 32.03 ATOM 4624 N CYS D 277 98.123 6.871 154.994 1.00 34.70 ATOM 4625 CA CYS D 277 97.408 8.007 154.442 1.00 34.96 ATOM 4626 C CYS D 277 97.704 8.032 152.943 1.00 33.55 ATOM 4627 O CYS D 277 98.843 8.224 152.529 1.00 34.70 ATOM 4628 CB CYS D 277 97.892 9.283 155.108 1.00 36.83 ATOM 4629 SG CYS D 277 96.863 10.744 154.794 1.00 39.87 ATOM 4630 N LYS D 278 96.682 7.820 152.130 1.00 31.82 ATOM 4631 CA LYS D 278 96.868 7.799 150.688 1.00 30.45 ATOM 4632 CB LYS D 278 96.086 6.611 150.107 1.00 33.60 ATOM 4633 CG LYS D 278 96.331 6.278 148.628 1.00 41.46 ATOM 4634 CD LYS D 278 95.614 7.246 147.632 1.00 43.28 ATOM 4635 CE LYS D 278 95.477 6.643 146.221 1.00 40.06 ATOM 4636 NZ LYS D 278 94.721 5.342 146.221 1.00 39.77 ATOM 4637 C LYS D 278 96.380 9.128 150.120 1.00 28.42 ATOM 4638 O LYS D 278 95.182 9.425 150.132 1.00 27.77 ATOM 4639 N VAL D 279 97.316 9.932 149.628 1.00 27.51 ATOM 4640 CA VAL D 279 96.987 11.240 149.078 1.00 26.96 ATOM 4641 CB VAL D 279 97.969 12.305 149.565 1.00 27.10 ATOM 4642 CG1 VAL D 279 97.531 13.683 149.075 1.00 28.38 ATOM 4643 CG2 VAL D 279 98.044 12.278 151.066 1.00 28.56 ATOM 4644 C VAL D 279 96.991 11.306 147.560 1.00 27.47 ATOM 4645 O VAL D 279 97.666 10.528 146.887 1.00 27.46 ATOM 4646 N TYR D 280 96.213 12.243 147.031 1.00 27.87 ATOM 4647 CA TYR D 280 96.140 12.481 145.590 1.00 27.91 ATOM 4648 CB TYR D 280 94.879 11.896 144.946 1.00 25.61 ATOM 4649 CG TYR D 280 94.783 12.292 143.492 1.00 20.03 ATOM 4650 CD1 TYR D 280 95.581 11.663 142.538 1.00 21.49 ATOM 4651 CE1 TYR D 280 95.641 12.113 141.214 1.00 20.60 ATOM 4652 CD2 TYR D 280 94.016 13.377 143.092 1.00 18.90 ATOM 4653 CE2 TYR D 280 94.064 13.843 141.766 1.00 22.69 ATOM 4654 CZ TYR D 280 94.894 13.206 140.834 1.00 23.31 ATOM 4655 OH TYR D 280 95.053 13.704 139.556 1.00 23.42 ATOM 4656 C TYR D 280 96.100 13.978 145.338 1.00 28.68 ATOM 4657 O TYR D 280 95.275 14.692 145.906 1.00 30.82 ATOM 4658 N SER D 281 96.921 4.462 144.493 1.00 28.17 ATOM 4659 CA SER D 281 96.984 15.870 144.171 1.00 28.04 ATOM 4660 CB SER D 281 97.625 16.709 145.275 1.00 28.85 ATOM 4661 OG SER D 281 97.563 18.093 144.954 1.00 27.99 ATOM 4662 C SER D 281 97.733 16.050 142.883 1.00 27.96 ATOM 4663 O SER D 281 98.740 15.372 142.645 1.00 26.52 ATOM 4664 N ASP D 282 97.211 16.942 142.040 1.00 28.40 ATOM 4665 CA ASP D 282 97.836 17.229 140.764 1.00 28.26 ATOM 4666 CB ASP D 282 96.869 18.031 139.871 1.00 26.72 ATOM 4667 CG ASP D 282 97.391 18.230 138.437 1.00 27.05 ATOM 4668 OD1 ASP D 282 96.605 18.670 137.565 1.00 23.35 ATOM 4669 OD2 ASP D 282 98.584 17.968 138.174 1.00 27.42 ATOM 4670 C ASP D 282 99.077 18.008 141.190 1.00 28.63 ATOM 4671 O ASP D 282 100.185 17.485 141.091 1.00 31.59 ATOM 4672 N PRO D 283 98.918 19.246 141.703 1.00 27.45 ATOM 4673 CD PRO D 283 97.721 20.080 141.912 1.00 27.15 ATOM 4674 CA PRO D 283 100.122 19.969 142.116 1.00 25.51 ATOM 4675 CB PRO D 283 99.612 21.377 142.350 1.00 22.95 ATOM 4676 CG PRO D 283 98.245 21.152 142.833 1.00 25.35 ATOM 4677 C PRO D 283 100.672 19.302 143.376 1.00 26.74 ATOM 4678 O PRO D 283 99.922 18.722 144.160 1.00 28.84 ATOM 4679 N GLN D 284 101.979 19.373 143.572 1.00 27.83 ATOM 4680 CA GLN D 284 102.595 18.719 144.719 1.00 27.59 ATOM 4681 CB GLN D 284 104.098 19.008 144.738 1.00 26.73 ATOM 4682 CG GLN D 284 104.824 18.393 143.540 1.00 26.87 ATOM 4683 CD GLN D 284 104.642 16.877 143.463 1.00 26.85 ATOM 4684 OE1 GLN D 284 104.782 16.273 142.400 1.00 29.56 ATOM 4685 NE2 GLN D 284 104.339 16.261 144.596 1.00 26.92 ATOM 4686 C GLN D 284 101.959 19.043 146.060 1.00 27.76 ATOM 4687 O GLN D 284 101.806 20.208 146.434 1.00 29.44 ATOM 4688 N PRO D 285 101.539 17.996 146.789 1.00 27.52 ATOM 4689 CD PRO D 285 101.201 16.657 146.273 1.00 26.12 ATOM 4690 CA PRO D 285 100.926 18.206 148.101 1.00 27.83 ATOM 4691 CB PRO D 285 99.948 17.034 148.196 1.00 26.21 ATOM 4692 CG PRO D 285 100.696 15.944 147.512 1.00 24.09 ATOM 4693 C PRO D 285 101.941 18.209 149.252 1.00 27.69 ATOM 4694 O PRO D 285 102.975 17.530 149.198 1.00 26.73 ATOM 4695 N HIS D 286 101.655 19.000 150.285 1.00 27.91 ATOM 4696 CA HIS D 286 102.515 19.025 151.450 1.00 25.77 ATOM 4697 CB HIS D 286 102.755 20.438 151.955 1.00 26.97 ATOM 4698 CG HIS D 286 103.809 20.511 153.016 1.00 27.05 ATOM 4699 CD2 HIS D 286 104.943 19.792 153.190 1.00 27.21 ATOM 4700 ND1 HIS D 286 103.740 21.386 154.080 1.00 25.97 ATOM 4701 CE1 HIS D 286 104.784 21.196 154.867 1.00 27.93 ATOM 4702 NE2 HIS D 286 105.529 20.234 154.350 1.00 27.84 ATOM 4703 C HIS D 286 101.779 18.234 152.510 1.00 25.23 ATOM 4704 O HIS D 286 100.719 18.645 152.981 1.00 24.71 ATOM 4705 N ILE D 287 102.342 17.087 152.867 1.00 26.15 ATOM 4706 CA ILE D 287 101.757 16.199 153.863 1.00 26.81 ATOM 4707 CB ILE D 287 101.949 14.728 153.477 1.00 26.82 ATOM 4708 CG2 ILE D 287 101.300 13.824 154.520 1.00 27.34 ATOM 4709 CG1 ILE D 287 101.340 14.471 152.107 1.00 24.98 ATOM 4710 CD1 ILE D 287 101.328 13.043 151.747 1.00 24.48 ATOM 4711 C ILE D 287 102.391 16.395 155.231 1.00 28.63 ATOM 4712 O ILE D 287 103.556 16.788 155.341 1.00 29.59 ATOM 4713 N GLN D 288 101.624 16.101 156.276 1.00 28.82 ATOM 4714 CA GLN D 288 102.121 16.250 157.630 1.00 28.67 ATOM 4715 CB GLN D 288 102.031 17.712 158.048 1.00 30.80 ATOM 4716 CG GLN D 288 102.553 17.995 159.436 1.00 34.16 ATOM 4717 CD GLN D 288 102.568 19.475 159.726 1.00 36.29 ATOM 4718 OE1 GLN D 288 103.584 20.032 160.156 1.00 36.96 ATOM 4719 NE2 GLN D 288 101.435 20.128 159.486 1.00 36.39 ATOM 4720 C GLN D 288 101.305 15.395 158.578 1.00 27.72 ATOM 4721 O GLN D 288 100.116 15.190 158.357 1.00 27.73 ATOM 4722 N TRP D 289 101.946 14.884 159.624 1.00 26.18 ATOM 4723 CA TRP D 289 101.247 14.077 160.608 1.00 25.04 ATOM 4724 CB TRP D 289 101.924 12.728 160.796 1.00 26.06 ATOM 4725 CG TRP D 289 101.747 11.809 159.652 1.00 24.37 ATOM 4726 CD2 TRP D 289 100.666 10.889 159.452 1.00 24.24 ATOM 4727 CE2 TRP D 289 100.911 10.219 158.236 1.00 23.33 ATOM 4728 CE3 TRP D 289 99.510 10.565 160.184 1.00 25.18 ATOM 4729 CD1 TRP D 289 102.572 11.674 158.588 1.00 23.31 ATOM 4730 NE1 TRP D 289 102.083 10.720 157.731 1.00 24.91 ATOM 4731 CZ2 TRP D 289 100.048 9.236 157.724 1.00 21.63 ATOM 4732 CZ3 TRP D 289 98.642 9.578 159.672 1.00 24.77 ATOM 4733 CH2 TRP D 289 98.925 8.930 158.452 1.00 22.51 ATOM 4734 C TRP D 289 101.202 14.802 161.940 1.00 25.00 ATOM 4735 O TRP D 289 102.193 15.374 162.373 1.00 26.08 ATOM 4736 N LEU D 290 100.042 14.762 162.586 1.00 25.25 ATOM 4737 CA LEU D 290 99.825 15.417 163.864 1.00 25.69 ATOM 4738 CB LEU D 290 98.788 16.514 163.722 1.00 25.43 ATOM 4739 CG LEU D 290 99.206 17.911 163.325 1.00 27.57 ATOM 4740 CD1 LEU D 290 100.063 17.843 162.068 1.00 31.13 ATOM 4741 CD2 LEU D 290 97.961 18.762 163.126 1.00 23.46 ATOM 4742 C LEU D 290 99.253 14.483 164.888 1.00 27.28 ATOM 4743 O LEU D 290 98.616 13.494 164.542 1.00 26.67 ATOM 4744 N LYS D 291 99.471 14.810 166.156 1.00 29.81 ATOM 4745 CA LYS D 291 98.848 14.057 167.233 1.00 32.14 ATOM 4746 CB LYS D 291 99.833 13.316 168.120 1.00 31.84 ATOM 4747 CG LYS D 291 99.077 12.575 169.210 1.00 33.10 ATOM 4748 CD LYS D 291 99.986 11.827 170.140 1.00 37.57 ATOM 4749 CE LYS D 291 99.193 11.164 171.249 1.00 37.27 ATOM 4750 NZ LYS D 291 100.141 10.473 172.162 1.00 38.20 ATOM 4751 C LYS D 291 98.120 15.096 168.072 1.00 33.93 ATOM 4752 O LYS D 291 98.684 16.153 168.387 1.00 33.14 ATOM 4753 N HIS D 292 96.866 14.804 168.413 1.00 35.56 ATOM 4754 CA HIS D 292 96.052 15.716 169.205 1.00 36.77 ATOM 4755 CB HIS D 292 94.576 15.433 168.953 1.00 37.96 ATOM 4756 CG HIS D 292 94.136 15.760 167.563 1.00 40.80 ATOM 4757 CD2 HIS D 292 93.785 14.962 166.526 1.00 42.12 ATOM 4758 ND1 HIS D 292 94.037 17.054 167.101 1.00 40.67 ATOM 4759 CE1 HIS D 292 93.641 17.040 165.840 1.00 41.85 ATOM 4760 NE2 HIS D 292 93.481 15.783 165.466 1.00 42.65 ATOM 4761 C HIS D 292 96.358 15.581 170.687 1.00 37.14 ATOM 4762 O HIS D 292 96.298 14.484 171.239 1.00 38.92 ATOM 4763 N VAL D 308 98.284 20.414 169.346 1.00 33.09 ATOM 4764 CA VAL D 308 98.821 19.295 168.570 1.00 33.71 ATOM 4765 CB VAL D 308 98.490 19.448 167.064 1.00 32.52 ATOM 4766 CD1 VAL D 308 97.010 19.502 166.862 1.00 29.95 ATOM 4767 CG2 VAL D 308 99.155 20.697 166.515 1.00 31.27 ATOM 4768 C VAL D 308 100.343 19.119 168.681 1.00 32.88 ATOM 4769 O VAL D 308 101.059 19.964 169.223 1.00 32.12 ATOM 4770 N GLN D 309 100.818 17.997 168.160 1.00 31.80 ATOM 4771 CA GLN D 309 102.234 17.703 168.150 1.00 30.85 ATOM 4772 CB GLN D 309 102.562 16.577 169.115 1.00 30.07 ATOM 4773 CG GLN D 309 103.829 15.882 168.709 1.00 32.83 ATOM 4774 CD GLN D 309 104.309 14.897 169.724 1.00 33.49 ATOM 4775 OE1 GLN D 309 103.538 14.072 170.224 1.00 35.52 ATOM 4776 NE2 GLN D 309 105.600 14.959 170.035 1.00 33.76 ATOM 4777 C GLN D 309 102.588 17.281 166.733 1.00 29.45 ATOM 4778 O GLN D 309 102.072 16.274 166.225 1.00 29.22 ATOM 4779 N ILE D 310 103.451 18.059 166.089 1.00 27.57 ATOM 4780 CA ILE D 310 103.862 17.752 164.721 1.00 25.83 ATOM 4781 CB ILE D 310 104.536 18.961 164.062 1.00 21.88 ATOM 4782 CG2 ILE D 310 104.713 18.710 162.584 1.00 21.49 ATOM 4783 CG1 ILE D 310 103.657 20.191 164.252 1.00 18.95 ATOM 4784 CD1 ILE D 310 102.170 19.948 163.940 1.00 17.06 ATOM 4785 C ILE D 310 104.805 16.563 164.740 1.00 24.75 ATOM 4786 O ILE D 310 105.919 16.654 165.236 1.00 25.81 ATOM 4787 N LEU D 311 104.342 15.442 164.207 1.00 23.85 ATOM 4788 CA LEU D 311 105.126 14.218 164.203 1.00 25.83 ATOM 4789 CB LEU D 311 104.192 13.019 164.353 1.00 25.27 ATOM 4790 CG LEU D 311 103.223 13.077 165.532 1.00 26.41 ATOM 4791 CD1 LEU D 311 102.098 12.051 165.348 1.00 21.64 ATOM 4792 CD2 LEU D 311 104.015 12.860 166.820 1.00 24.12 ATOM 4793 C LEU D 311 105.979 14.015 162.955 1.00 26.90 ATOM 4794 O LEU D 311 107.079 13.462 163.031 1.00 28.62 ATOM 4795 N LYS D 312 105.470 14.456 161.811 1.00 26.26 ATOM 4796 CA LYS D 312 106.174 14.270 160.558 1.00 26.36 ATOM 4797 CB LYS D 312 105.816 12.895 159.985 1.00 27.03 ATOM 4798 CG LYS D 312 106.793 12.339 158.963 1.00 26.95 ATOM 4799 CD LYS D 312 106.526 10.860 158.710 1.00 27.20 ATOM 4800 CE LYS D 312 107.679 10.201 157.954 1.00 27.96 ATOM 4801 NZ LYS D 312 107.554 8.713 157.955 1.00 26.09 ATOM 4802 C LYS D 312 105.751 15.358 159.596 1.00 26.99 ATOM 4803 O LYS D 312 104.595 15.780 159.596 1.00 26.20 ATOM 4804 N THR D 313 106.693 15.828 158.787 1.00 28.01 ATOM 4805 CA THR D 313 106.385 16.861 157.820 1.00 28.06 ATOM 4806 CB THR D 313 106.595 18.263 158.393 1.00 27.10 ATOM 4807 OG1 THR D 313 105.828 18.406 159.597 1.00 25.05 ATOM 4808 CG2 THR D 313 106.123 19.309 157.387 1.00 26.17 ATOM 4809 C THR D 313 107.246 16.677 156.592 1.00 29.26 ATOM 4810 O THR D 313 108.471 16.581 156.683 1.00 31.13 ATOM 4811 N ALA D 314 106.584 16.607 155.442 1.00 29.36 ATOM 4812 CA ALA D 314 107.257 16.420 154.166 1.00 29.34 ATOM 4813 CB ALA D 314 106.237 16.281 153.058 1.00 27.47 ATOM 4814 C ALA D 314 108.204 17.562 153.842 1.00 30.36 ATOM 4815 O ALA D 314 107.974 18.712 154.228 1.00 30.60 ATOM 4816 N GLY D 315 109.264 17.227 153.116 1.00 29.90 ATOM 4817 CA GLY D 315 110.252 18.211 152.727 1.00 29.95 ATOM 4818 C GLY D 315 111.524 17.495 152.343 1.00 30.80 ATOM 4819 O GLY D 315 111.577 16.265 152.353 1.00 31.54 ATOM 4820 N VAL D 316 112.555 18.254 152.004 1.00 30.69 ATOM 4821 CA VAL D 316 113.817 17.654 151.619 1.00 31.98 ATOM 4822 CB VAL D 316 114.869 18.739 151.357 1.00 32.20 ATOM 4823 CG1 VAL D 316 116.252 18.117 151.272 1.00 34.99 ATOM 4824 CG2 VAL D 316 114.548 19.455 150.058 1.00 33.78 ATOM 4825 C VAL D 316 114.355 16.654 152.655 1.00 32.59 ATOM 4826 O VAL D 316 115.014 15.681 152.301 1.00 33.55 ATOM 4827 N ASN D 317 114.071 16.891 153.929 1.00 32.95 ATOM 4828 CA ASN D 317 114.538 16.009 154.998 1.00 34.22 ATOM 4829 CB ASN D 317 114.477 16.711 156.355 1.00 34.35 ATOM 4830 CG ASN D 317 115.607 17.680 156.570 1.00 34.02 ATOM 4831 OD1 ASN D 317 115.668 18.340 157.608 1.00 34.37 ATOM 4832 ND2 ASN D 317 116.512 17.776 155.596 1.00 33.35 ATOM 4833 C ASN D 317 113.706 14.748 155.118 1.00 35.11 ATOM 4834 O ASN D 317 114.151 13.737 155.658 1.00 34.96 ATOM 4835 N THR D 318 112.476 14.815 154.647 1.00 36.25 ATOM 4836 CA THR D 318 111.599 13.670 154.729 1.00 35.45 ATOM 4837 CB THR D 318 110.737 13.758 155.994 1.00 35.52 ATOM 4838 OG1 THR D 318 111.563 13.517 157.140 1.00 33.24 ATOM 4839 CG2 THR D 318 109.633 12.743 155.963 1.00 36.91 ATOM 4840 C THR D 318 110.760 13.645 153.474 1.00 36.75 ATOM 4841 O THR D 318 109.685 14.233 153.403 1.00 38.77 ATOM 4842 N THR D 319 111.309 12.970 152.473 1.00 37.80 ATOM 4843 CA THR D 319 110.718 12.809 151.152 1.00 37.38 ATOM 4844 CB THR D 319 111.661 11.962 150.294 1.00 37.90 ATOM 4845 OG1 THR D 319 112.838 12.723 150.042 1.00 39.64 ATOM 4846 CG2 THR D 319 111.020 11.559 148.967 1.00 41.12 ATOM 4847 C THR D 319 109.347 12.154 151.164 1.00 36.69 ATOM 4848 O THR D 319 109.022 11.402 152.086 1.00 36.67 ATOM 4849 N ASP D 320 108.554 12.436 150.128 1.00 36.46 ATOM 4850 CA ASP D 320 107.216 11.859 149.997 1.00 35.83 ATOM 4851 CB ASP D 320 106.624 12.117 148.610 1.00 33.91 ATOM 4852 CG ASP D 320 106.286 13.570 148.373 1.00 34.35 ATOM 4853 OD1 ASP D 320 105.917 14.262 149.346 1.00 32.14 ATOM 4854 OD2 ASP D 320 106.374 14.015 147.205 1.00 34.66 ATOM 4855 C ASP D 320 107.271 10.359 150.206 1.00 35.84 ATOM 4856 O ASP D 320 106.323 9.759 150.695 1.00 36.05 ATOM 4857 N LYS D 321 108.385 9.752 149.821 1.00 37.45 ATOM 4858 CA LYS D 321 108.548 8.314 149.966 1.00 37.85 ATOM 4859 CB LYS D 321 110.014 7.931 149.794 1.00 39.71 ATOM 4860 CG LYS D 321 110.605 8.440 148.502 1.00 43.24 ATOM 4861 CD LYS D 321 112.123 8.263 148.471 1.00 47.56 ATOM 4862 CE LYS D 321 112.737 8.967 147.246 1.00 49.40 ATOM 4863 NZ LYS D 321 114.185 8.668 147.052 1.00 48.66 ATOM 4864 C LYS D 321 108.045 7.841 151.320 1.00 37.80 ATOM 4865 O LYS D 321 107.177 6.982 151.395 1.00 39.63 ATOM 4866 N GLU D 322 108.560 8.428 152.391 1.00 36.93 ATOM 4867 CA GLU D 322 108.173 8.021 153.732 1.00 36.01 ATOM 4868 CB GLU D 322 109.381 8.179 154.649 1.00 34.63 ATOM 4869 CG GLU D 322 109.979 9.585 154.627 1.00 32.89 ATOM 4870 CD GLU D 322 111.343 9.678 155.330 1.00 32.55 ATOM 4871 OE1 GLU D 322 111.467 9.187 156.479 1.00 28.33 ATOM 4872 OE2 GLU D 322 112.288 10.253 154.730 1.00 30.74 ATOM 4873 CG GLU D 322 106.983 8.747 154.345 1.00 36.20 ATOM 4874 O GLU D 322 106.546 8.393 155.433 1.00 36.13 ATOM 4875 N MET D 323 106.446 9.744 153.653 1.00 36.12 ATOM 4876 CA MET D 323 105.341 10.529 154.195 1.00 36.16 ATOM 4877 CB MET D 323 105.272 11.881 153.479 1.00 36.94 ATOM 4878 CG MET D 323 106.389 12.840 153.876 1.00 36.64 ATOM 4879 SD MET D 323 106.595 12.886 155.676 1.00 34.99 ATOM 4880 CE MET D 323 104.933 13.398 156.200 1.00 37.06 ATOM 4881 C MET D 323 103.940 9.935 154.259 1.00 36.22 ATOM 4882 O MET D 323 103.088 10.474 154.954 1.00 35.07 ATOM 4883 N GLU D 324 103.688 8.836 153.556 1.00 37.83 ATOM 4884 CA GLU D 324 102.352 8.250 153.574 1.00 37.78 ATOM 4885 CB GLU D 324 102.023 7.635 152.208 1.00 39.20 ATOM 4886 CG GLU D 324 101.867 8.691 151.115 1.00 45.52 ATOM 4887 CD GLU D 324 101.254 8.153 149.821 1.00 48.59 ATOM 4888 OE1 GLU D 324 101.736 7.109 149.325 1.00 52.60 ATOM 4889 OE2 GLU D 324 100.304 8.779 149.290 1.00 46.67 ATOM 4890 C GLU D 324 102.093 7.248 154.699 1.00 36.24 ATOM 4891 O GLU D 324 100.972 6.767 154.873 1.00 36.10 ATOM 4892 N VAL D 325 103.115 6.953 155.484 1.00 34.34 ATOM 4893 CA VAL D 325 102.945 6.021 156.582 1.00 35.57 ATOM 4894 CB VAL D 325 103.579 4.653 156.249 1.00 34.18 ATOM 4895 CG1 VAL D 325 105.095 4.781 156.198 1.00 32.54 ATOM 4896 CG2 VAL D 325 103.167 3.625 157.282 1.00 32.08 ATOM 4897 C VAL D 325 103.570 6.550 157.878 1.00 36.78 ATOM 4898 O VAL D 325 104.755 6.887 157.916 1.00 36.54 ATOM 4899 N LEU D 326 102.764 6.631 158.935 1.00 37.89 ATOM 4900 CA LEU D 326 103.243 7.097 160.235 1.00 38.72 ATOM 4901 CB LEU D 326 102.184 7.958 160.919 1.00 38.44 ATOM 4902 CG LEU D 326 102.598 8.517 162.283 1.00 38.99 ATOM 4903 CD1 LEU D 326 103.837 9.373 162.117 1.00 37.38 ATOM 4904 CD2 LEU D 326 101.465 9.344 162.883 1.00 38.01 ATOM 4905 C LEU D 326 103.564 5.890 161.114 1.00 39.59 ATOM 4906 O LEU D 326 102.700 5.069 161.401 1.00 38.62 ATOM 4907 N HIS D 327 104.814 5.794 161.540 1.00 41.75 ATOM 4908 CA HIS D 327 105.257 4.679 162.355 1.00 43.79 ATOM 4909 CB HIS D 327 106.648 4.249 161.914 1.00 46.71 ATOM 4910 CG HIS D 327 106.674 3.598 160.574 1.00 49.33 ATOM 4911 CD2 HIS D 327 107.068 4.062 159.365 1.00 50.34 ATOM 4912 ND1 HIS D 327 106.215 2.314 160.367 1.00 49.92 ATOM 4913 CE1 HIS D 327 106.324 2.015 159.085 1.00 51.65 ATOM 4914 NE2 HIS D 327 106.839 3.058 158.456 1.00 52.95 ATOM 4915 C HIS D 327 105.302 4.981 163.830 1.00 44.31 ATOM 4916 O HIS D 327 105.916 5.955 164.254 1.00 44.81 ATOM 4917 N LEU D 328 104.654 4.142 164.618 1.00 45.14 ATOM 4918 CA LEU D 328 104.688 4.322 166.055 1.00 47.78 ATOM 4919 CB LEU D 328 103.278 4.587 166.603 1.00 46.33 ATOM 4920 CG LEU D 328 102.642 5.872 166.044 1.00 43.57 ATOM 4921 CD1 LEU D 328 101.380 6.232 166.811 1.00 42.21 ATOM 4922 CD2 LEU D 328 103.631 7.000 166.136 1.00 39.43 ATOM 4923 C LEU D 328 105.310 3.046 166.615 1.00 50.07 ATOM 4924 O LEU D 328 104.682 1.987 166.642 1.00 51.11 ATOM 4925 N ARG D 329 106.571 3.164 167.022 1.00 52.33 ATOM 4926 CA ARG D 329 107.351 2.051 167.558 1.00 54.65 ATOM 4927 CB ARG D 329 108.842 2.324 167.336 1.00 54.25 ATOM 4928 C ARG D 329 107.095 1.820 169.043 1.00 56.39 ATOM 4929 O ARG D 329 107.316 2.716 169.857 1.00 57.26 ATOM 4930 N ASN D 330 106.649 0.612 169.389 1.00 58.57 ATOM 4931 CA ASN D 330 106.338 0.250 170.774 1.00 60.39 ATOM 4932 CB ASN D 330 107.607 0.066 171.560 1.00 63.16 ATOM 4933 CG ASN D 330 107.328 0.299 173.031 1.00 65.73 ATOM 4934 001 ASN D 330 107.248 0.648 173.819 1.00 66.78 ATOM 4935 ND2 ASN D 330 107.155 1.562 173.406 1.00 67.36 ATOM 4936 C ASN D 330 105.565 1.355 171.477 1.00 60.09 ATOM 4937 O AEN D 330 106.147 2.282 172.041 1.00 60.19 ATOM 4938 N VAL D 331 104.244 1.244 171.450 1.00 59.65 ATOM 4939 CA VAL D 331 103.397 2.257 172.053 1.00 59.89 ATOM 4940 CB VAL D 331 101.979 2.227 171.431 1.00 58.63 ATOM 4941 CG1 VAL D 331 102.057 2.593 169.967 1.00 57.29 ATOM 4942 CG2 VAL D 331 101.370 0.851 171.580 1.00 57.94 ATOM 4943 C VAL D 331 103.288 2.155 173.565 1.00 60.47 ATOM 4944 O VAL D 331 103.862 1.267 174.187 1.00 61.22 ATOM 4945 N SER D 332 102.548 3.092 174.144 1.00 61.44 ATOM 4946 CA SER D 332 102.321 3.156 175.583 1.00 62.61 ATOM 4947 CB SER D 332 103.424 3.969 176.269 1.00 62.34 ATOM 4948 OC SER D 332 103.348 5.346 175.927 1.00 60.01 ATOM 4949 C SER D 332 100.923 .868 175.766 1.00 63.67 ATOM 4950 O SER D 332 100.512 4.522 174.845 1.00 64.37 ATOM 4951 N PHE D 333 100.397 3.754 176.946 1.00 64.59 ATOM 4952 CA PHE D 333 99.122 4.413 177.199 1.00 65.42 ATOM 4953 CB PHE D 333 98.744 4.276 178.676 1.00 68.43 ATOM 4954 CG PHE D 333 98.278 2.896 179.054 1.00 72.42 ATOM 4955 CD1 PHE D 333 98.169 2.526 180.391 1.00 73.24 ATOM 4956 CD2 PHE D 333 97.933 1.966 178.069 1.00 74.01 ATOM 4957 CE1 PHE D 333 97.725 1.252 180.745 1.00 73.82 ATOM 4958 CE2 PHE D 333 97.488 0.691 178.413 1.00 74.79 ATOM 4959 CZ PHE D 333 97.384 0.334 179.754 1.00 74.53 ATOM 4960 C PHE D 333 99.180 5.882 176.809 1.00 64.25 ATOM 4961 O PHE D 333 98.161 6.494 176.488 1.00 63.25 ATOM 4962 N GLU D 334 100.386 6.436 176.830 1.00 63.41 ATOM 4963 CA GLU D 334 100.591 7.835 176.486 1.00 62.79 ATOM 4964 CB GLU D 334 102.032 8.235 176.794 1.00 65.85 ATOM 4965 CG GLU D 334 102.503 7.874 178.195 1.00 69.95 ATOM 4966 CD GLU D 334 104.013 8.031 178.345 1.00 73.26 ATOM 4967 OE1 GLU D 334 104.540 7.773 179.457 1.00 73.50 ATOM 4968 OE2 GLU D 334 104.669 8.410 177.342 1.00 73.62 ATOM 4969 C GLU D 334 100.293 8.067 175.002 1.00 59.92 ATOM 4970 O GLU D 334 99.578 9.003 174.643 1.00 59.28 ATOM 4971 N ASP D 335 100.839 7.198 174.154 1.00 55.93 ATOM 4972 CA ASP D 335 100.669 7.287 172.712 1.00 51.63 ATOM 4973 CB ASP D 335 101.515 6.217 172.037 1.00 49.63 ATOM 4974 CG ASP D 335 102.974 6.327 172.406 1.00 48.72 ATOM 4975 OD1 ASP D 335 103.514 7.444 172.311 1.00 46.64 ATOM 4976 OD2 ASP D 335 103.584 5.303 172.790 1.00 50.29 ATOM 4977 C ASP D 335 99.224 7.183 172.239 1.00 50.20 ATOM 4978 O ASP D 335 98.923 7.478 171.079 1.00 50.69 ATOM 4979 N ALA D 336 98.327 6.764 173.123 1.00 47.17 ATOM 4980 CA ALA D 336 96.924 6.659 172.750 1.00 44.10 ATOM 4981 CB ALA D 336 96.119 6.160 173.923 1.00 44.65 ATOM 4982 C ALA D 336 96.448 8.050 172.331 1.00 42.08 ATOM 4983 O ALA D 336 97.047 9.059 172.709 1.00 42.12 ATOM 4984 N GLY D 337 95.384 8.113 171.544 1.00 39.09 ATOM 4985 CA GLY D 337 94.900 9.406 171.116 1.00 36.28 ATOM 4986 C GLY D 337 94.650 9.494 169.627 1.00 35.30 ATOM 4987 O GLY D 337 94.873 8.550 168.874 1.00 37.23 ATOM 4988 N GLU D 338 94.199 10.661 169.203 1.00 34.06 ATOM 4989 CA GLU D 338 93.864 10.928 167.819 1.00 31.79 ATOM 4990 CB GLU D 338 92.743 11.964 167.823 1.00 32.76 ATOM 4991 CG GLU D 338 92.136 12.358 166.515 1.00 35.47 ATOM 4992 CD GLU D 338 90.919 13.237 166.746 1.00 38.92 ATOM 4993 OE1 GLU D 338 90.910 13.990 167.750 1.00 40.52 ATOM 4994 OE2 GLU D 338 89.972 13.183 165.937 1.00 40.80 ATOM 4995 C GLU D 338 95.058 11.401 166.987 1.00 30.61 ATOM 4996 O GLU D 338 95.751 12.362 167.336 1.00 28.27 ATOM 4997 N TYR D 339 95.301 10.701 165.886 1.00 29.87 ATOM 4998 CA TYR D 339 96.388 11.062 164.989 1.00 30.24 ATOM 4999 CB TYR D 339 97.305 9.865 164.711 1.00 30.60 ATOM 5000 CG TYR D 339 98.156 9.495 165.893 1.00 31.84 ATOM 5001 CD1 TYR D 339 97.613 8.807 166.984 1.00 33.22 ATOM 5002 CE1 TYR D 339 98.365 8.561 168.127 1.00 35.77 ATOM 5003 CD2 TYR D 339 99.478 9.917 165.970 1.00 33.47 ATOM 5004 CE2 TYR D 339 100.242 9.683 167.104 1.00 36.30 ATOM 5005 CZ TYR D 339 99.683 9.009 168.182 1.00 38.40 ATOM 5006 OH TYR D 339 100.439 8.829 169.323 1.00 41.10 ATOM 5007 C TYR D 339 95.747 11.557 163.711 1.00 29.89 ATOM 5008 O TYR D 339 94.753 10.998 163.249 1.00 28.60 ATOM 5009 N THR D 340 96.316 12.613 163.143 1.00 30.27 ATOM 5010 CA THR D 340 95.757 13.196 161.942 1.00 29.19 ATOM 5011 CB THR D 340 95.164 14.567 162.269 1.00 28.40 ATOM 5012 OG1 THR D 340 94.249 14.418 163.357 1.00 28.64 ATOM 5013 CG2 THR D 340 94.430 15.146 161.075 1.00 27.74 ATOM 5014 C THR D 340 96.747 13.328 160.799 1.00 29.78 ATOM 5015 O THR D 340 97.928 13.616 161.002 1.00 29.63 ATOM 5016 N CYS D 341 96.244 13.098 159.592 1.00 29.75 ATOM 5017 CA CYS D 341 97.052 13.222 158.397 1.00 31.36 ATOM 5018 C CYS D 341 96.573 14.424 157.580 1.00 30.34 ATOM 5019 O CYS D 341 95.439 14.427 157.095 1.00 31.13 ATOM 5020 CB CYS D 341 96.953 11.954 157.561 1.00 33.83 ATOM 5021 SG CYS D 341 97.798 12.118 155.958 1.00 38.30 ATOM 5022 N LEU D 342 97.429 15.440 157.443 1.00 28.14 ATOM 5023 CA LEU D 342 97.084 16.632 156.680 1.00 25.64 ATOM 5024 CB LEU D 342 97.421 17.909 157.433 1.00 29.80 ATOM 5025 CG LEU D 342 96.974 18.193 158.862 1.00 34.80 ATOM 5026 CD1 LEU D 342 96.751 19.704 158.943 1.00 34.66 ATOM 5027 CD2 LEU D 342 95.703 17.435 159.246 1.00 33.53 ATOM 5028 C LEU D 342 97.828 16.702 155.370 1.00 24.11 ATOM 5029 O LEU D 342 99.010 16.345 155.288 1.00 22.00 ATOM 5030 N ALA D 343 97.130 17.193 154.352 1.00 21.64 ATOM 5031 CA ALA D 343 97.711 17.364 153.031 1.00 20.61 ATOM 5032 CB ALA D 343 97.465 16.147 152.182 1.00 21.72 ATOM 5033 C ALA D 343 97.112 18.592 152.372 1.00 20.26 ATOM 5034 O ALA D 343 95.900 18.779 152.364 1.00 20.13 ATOM 5035 N GLY D 344 97.970 19.440 151.827 1.00 21.09 ATOM 5036 CA GLY D 344 97.473 20.634 151.181 1.00 22.38 ATOM 5037 C GLY D 344 98.345 21.160 150.060 1.00 23.80 ATOM 5038 O GLY D 344 99.540 20.857 149.971 1.00 23.92 ATOM 5039 N ASN D 345 97.720 21.919 149.167 1.00 23.54 ATOM 5040 CA ASN D 345 98.439 22.546 148.082 1.00 21.83 ATOM 5041 CB ASN D 345 98.150 21.895 146.733 1.00 21.01 ATOM 5042 CG ASN D 345 96.679 21.689 146.476 1.00 24.41 ATOM 5043 CD1 ASN D 345 95.861 22.605 146.636 1.00 26.37 ATOM 5044 ND2 ASN D 345 96.331 20.482 146.038 1.00 20.51 ATOM 5045 C ASN D 345 98.001 23.984 148.101 1.00 22.08 ATOM 5046 O ASN D 345 97.356 24.430 149.046 1.00 19.30 ATOM 5047 N SER D 346 98.356 24.727 147.075 1.00 24.23 ATOM 5048 CA SER D 346 97.991 26.123 147.061 1.00 27.91 ATOM 5049 CB SER D 346 98.779 26.857 145.969 1.00 30.80 ATOM 5050 OG SER D 346 98.859 26.091 144.773 1.00 37.69 ATOM 5051 C SER D 346 96.491 26.314 146.894 1.00 28.82 ATOM 5052 O SER D 346 95.952 27.355 147.250 1.00 29.53 ATOM 5053 N ILE D 347 95.806 25.299 146.381 1.00 30.08 ATOM 5054 CA ILE D 347 94.371 25.416 146.190 1.00 28.98 ATOM 5055 CB ILE D 347 93.870 24.403 145.169 1.00 26.99 ATOM 5056 CG2 ILE D 347 92.394 24.583 144.965 1.00 22.50 ATOM 5057 CG1 ILE D 347 94.606 24.621 143.851 1.00 26.44 ATOM 5058 CD1 ILE D 347 94.363 23.584 142.795 1.00 30.48 ATOM 5059 C ILE D 347 93.607 25.266 147.496 1.00 29.91 ATOM 5060 O ILE D 347 92.719 26.058 147.788 1.00 32.67 ATOM 5061 N GLY D 348 93.950 24.273 148.301 1.00 28.95 ATOM 5062 CA GLY D 348 93.239 24.114 149.554 1.00 30.13 ATOM 5063 C GLY D 348 93.890 23.115 150.483 1.00 30.97 ATOM 5064 O GLY D 348 95.017 22.680 150.241 1.00 31.52 ATOM 5065 N LEU D 349 93.179 22.749 151.545 1.00 30.91 ATOM 5066 CA LEU D 349 93.697 21.789 152.513 1.00 31.11 ATOM 5067 CB LEU D 349 94.104 22.517 153.796 1.00 31.40 ATOM 5068 CG LEU D 349 94.819 21.653 154.841 1.00 33.44 ATOM 5069 CD1 LEU D 349 96.170 21.198 154.305 1.00 31.52 ATOM 5070 CD2 LEU D 349 94.989 22.451 156.124 1.00 33.38 ATOM 5071 C LEU D 349 92.730 20.634 152.849 1.00 30.31 ATOM 5072 O LEU D 349 91.506 20.791 152.828 1.00 29.25 ATOM 5073 N SER D 350 93.297 19.470 153.151 1.00 29.32 ATOM 5074 CA SER D 350 92.513 18.290 153.495 1.00 29.59 ATOM 5075 CB SER D 350 92.461 17.312 152.325 1.00 28.63 ATOM 5076 OG SER D 350 91.629 17.795 151.287 1.00 32.28 ATOM 5077 C SER D 350 93.176 17.604 154.664 1.00 30.54 ATOM 5078 O SER D 350 94.345 17.856 154.943 1.00 30.95 ATOM 5079 N HIS D 351 92.430 16.740 155.346 1.00 31.83 ATOM 5080 CA HIS D 351 92.967 15.996 156.479 1.00 32.23 ATOM 5081 CB HIS D 351 93.269 16.930 157.642 1.00 35.19 ATOM 5082 CG HIS D 351 92.048 17.560 158.228 1.00 39.93 ATOM 5083 CD2 HIS D 351 91.287 17.204 159.290 1.00 40.95 ATOM 5084 ND1 HIS D 351 91.417 18.640 157.648 1.00 40.27 ATOM 5085 CE1 HIS D 351 90.319 18.919 158.326 1.00 41.63 ATOM 5086 NE2 HIS D 351 90.217 18.061 159.326 1.00 41.54 ATOM 5087 C HIS D 351 91.985 14.941 156.962 1.00 31.71 ATOM 5088 O HIS D 351 90.783 15.184 156.998 1.00 31.07 ATOM 5089 N HIS D 352 92.513 13.770 157.317 1.00 31.75 ATOM 5090 CA HIS D 352 91.722 12.661 157.851 1.00 30.61 ATOM 5091 CB HIS D 352 91.844 11.392 156.999 1.00 30.06 ATOM 5092 CG HIS D 352 91.018 11.396 155.750 1.00 30.96 ATOM 5093 CD2 HIS D 352 90.243 12.353 155.187 1.00 32.11 ATOM 5094 ND1 HIS D 352 90.957 10.310 154.901 1.00 30.90 ATOM 5095 CE1 HIS D 352 90.183 10.599 153.871 1.00 30.38 ATOM 5096 NE2 HIS D 352 89.737 11.833 154.019 1.00 30.27 ATOM 5097 C HIS D 352 92.323 12.357 159.216 1.00 31.42 ATOM 5098 O HIS D 352 93.540 12.467 159.400 1.00 31.56 ATOM 5099 N SER D 353 91.484 11.967 160.168 1.00 31.10 ATOM 5100 CA SER D 353 91.966 11.652 161.502 1.00 31.28 ATOM 5101 CB SER D 353 91.305 12.575 162.521 1.00 31.16 ATOM 5102 OG SER D 353 91.417 13.927 162.115 1.00 32.98 ATOM 5103 C SER D 353 91.639 10.211 161.839 1.00 31.23 ATOM 5104 O SER D 353 90.733 9.630 161.257 1.00 33.53 ATOM 5105 N ALA D 354 92.390 9.634 162.769 1.00 31.01 ATOM 5106 CA ALA D 354 92.170 8.262 163.203 1.00 30.47 ATOM 5107 CB ALA D 354 93.095 7.313 162.466 1.00 28.96 ATOM 5108 C ALA D 354 92.435 8.197 164.696 1.00 31.37 ATOM 5109 O ALA D 354 93.118 9.058 165.260 1.00 29.49 ATOM 5110 N TRP D 355 91.901 7.167 165.337 1.00 33.61 ATOM 5111 CA TRP D 355 92.080 7.025 166.765 1.00 34.51 ATOM 5112 CB TRP D 355 90.720 6.974 167.453 1.00 36.20 ATOM 5113 CG TRP D 355 90.724 7.824 168.658 1.00 42.37 ATOM 5114 CD2 TRP D 355 90.095 9.102 168.793 1.00 44.32 ATOM 5115 CE2 TRP D 355 90.483 9.626 170.055 1.00 44.27 ATOM 5116 CE3 TRP D 355 89.247 9.858 167.972 1.00 43.24 ATOM 5117 CD1 TRP D 355 91.439 7.619 169.815 1.00 44.23 ATOM 5118 NE1 TRP D 355 91.300 8.704 170.656 1.00 45.49 ATOM 5119 CZ2 TRP D 355 90.049 10.871 170.505 1.00 43.28 ATOM 5120 CZ3 TRP D 355 88.818 11.093 168.423 1.00 43.34 ATOM 5121 CH2 TRP D 355 89.221 11.589 169.679 1.00 43.92 ATOM 5122 C TRP D 355 92.887 5.812 167.178 1.00 33.47 ATOM 5123 O TRP D 355 92.590 4.693 166.765 1.00 33.00 ATOM 5124 N LEU D 356 93.908 6.044 167.998 1.00 32.81 ATOM 5125 CA LEU D 356 94.728 4.955 168.515 1.00 33.21 ATOM 5126 CB LEU D 356 96.194 5.347 168.594 1.00 34.73 ATOM 5127 CG LEU D 356 97.143 4.144 168.566 1.00 35.38 ATOM 5128 CD1 LEU D 356 98.543 4.609 168.923 1.00 35.96 ATOM 5129 CD2 LEU D 356 96.680 3.065 169.521 1.00 35.85 ATOM 5130 C LEU D 356 94.263 4.609 169.925 1.00 33.74 ATOM 5131 O LEU D 356 94.379 5.412 170.847 1.00 32.37 ATOM 5132 N THR D 357 93.735 3.404 170.081 1.00 35.42 ATOM 5133 CA THR D 357 93.265 2.931 171.375 1.00 37.14 ATOM 5134 CB THR D 357 91.875 2.264 171.250 1.00 37.60 ATOM 5135 OG1 THR D 357 90.965 3.173 170.610 1.00 36.16 ATOM 5136 CG2 THR D 357 91.342 1.876 172.632 1.00 34.23 ATOM 5137 C THR D 357 94.269 1.898 171.870 1.00 37.63 ATOM 5138 O THR D 357 94.509 0.900 171.196 1.00 38.36 ATOM 5139 N VAL D 358 94.857 2.138 173.039 1.00 38.60 ATOM 5140 CA VAL D 358 95.849 1.218 173.602 1.00 40.52 ATOM 5141 CB VAL D 358 97.132 1.996 174.025 1.00 40.83 ATOM 5142 CG1 VAL D 358 98.160 1.048 174.606 1.00 40.51 ATOM 5143 CG2 VAL D 358 97.708 2.739 172.828 1.00 39.34 ATOM 5144 C VAL D 358 95.308 0.444 174.814 1.00 40.94 ATOM 5145 O VAL D 358 94.574 0.998 175.640 1.00 40.87 ATOM 5146 N LEU D 359 95.673 0.834 174.909 1.00 40.73 ATOM 5147 CA LEU D 359 95.243 1.694 176.015 1.00 40.07 ATOM 5148 CB LEU D 359 94.083 2.584 175.567 1.00 37.19 ATOM 5149 CG LEU D 359 92.900 1.926 174.858 1.00 37.09 ATOM 5150 CD1 LEU D 359 91.866 2.983 174.499 1.00 34.94 ATOM 5151 CD2 LEU D 359 92.291 0.851 175.739 1.00 36.94 ATOM 5152 C LEU D 359 96.405 2.583 176.490 1.00 41.50 ATOM 5153 O LEU D 359 96.472 2.906 177.705 1.00 43.25 HETATM 5154 S SO4 1 101.860 26.306 120.782 1.00 67.75 HETATM 5155 O1 SO4 1 101.069 25.832 121.933 1.00 68.48 HETATM 5156 O2 SO4 1 101.467 25.556 119.574 1.00 67.57 HETATM 5157 O3 SO4 1 101.618 27.745 120.575 1.00 69.30 HETATM 5158 O4 SO4 1 103.293 26.096 121.052 1.00 68.39 HETATM 5159 S SO4 2 112.071 33.384 123.815 1.00 66.75 HETATM 5160 O1 SO4 2 113.069 34.455 123.623 1.00 67.50 HETATM 5161 O2 SO4 2 112.663 32.092 123.418 1.00 66.52 HETATM 5162 O3 SO4 2 111.676 33.341 125.238 1.00 65.71 HETATM 5163 O4 SO4 2 110.883 33.652 122.975 1.00 66.55 HETATM 5164 S SO4 3 77.189 23.441 106.691 1.00 83.31 HETATM 5165 O1 SO4 3 78.088 22.827 105.694 1.00 84.63 HETATM 5166 O2 SO4 3 77.908 23.560 107.969 1.00 84.80 HETATM 5167 O3 SO4 3 76.762 24.778 106.237 1.00 82.90 HETATM 5168 O4 SO4 3 76.003 22.590 106.876 1.00 83.82 HETATM 5169 S SO4 4 85.406 27.736 115.455 1.00 90.59 HETATM 5170 O1 SO4 4 86.326 28.866 115.704 1.00 89.09 HETATM 5171 O2 SO4 4 86.162 26.578 114.945 1.00 89.08 HETATM 5172 O3 SO4 4 84.725 27.358 116.711 1.00 89.23 HETATM 5173 O4 SO4 4 84.404 28.146 114.455 1.00 89.64

TABLE 2 FGFR1 D2–D3 Complexed with FGF1 ATOM 1 CB TYR 8 −6.051 51.528 11.919 1.00 28.44 ATOM 2 CG TYR 8 −6.818 50.221 12.093 1.00 27.45 ATOM 3 CD1 TYR 8 −8.094 50.053 11.541 1.00 24.63 ATOM 4 CE1 TYR 8 −8.834 48.901 11.773 1.00 20.69 ATOM 5 CD2 TYR 8 −6.302 49.185 12.876 1.00 25.25 ATOM 6 CE2 TYR 8 −7.038 48.029 13.114 1.00 22.59 ATOM 7 CZ TYR 8 −8.303 47.896 12.564 1.00 22.85 ATOM 8 OH TYR 8 −9.040 46.769 12.836 1.00 21.66 ATOM 9 C TYR 8 −8.095 52.815 12.656 1.00 32.48 ATOM 10 O TYR 8 −8.624 53.046 11.564 1.00 33.42 ATOM 11 N TYR 8 −6.151 52.546 14.217 1.00 28.27 ATOM 12 CA TYR 8 −6.567 52.705 12.782 1.00 31.41 ATOM 13 N LYS 9 −8.801 52.636 13.768 1.00 31.66 ATOM 14 CA LYS 9 −10.252 52.748 13.756 1.00 32.17 ATOM 15 CB LYS 9 −10.885 51.750 14.723 1.00 32.91 ATOM 16 CG LYS 9 −10.816 50.308 14.230 1.00 36.66 ATOM 17 CD LYS 9 −11.854 49.432 14.901 1.00 34.19 ATOM 18 CE LYS 9 −12.006 48.114 14.163 1.00 36.17 ATOM 19 NZ LYS 9 −13.244 47.392 14.591 1.00 36.62 ATOM 20 C LYS 9 −10.680 54.160 14.127 1.00 34.00 ATOM 21 O LYS 9 −11.772 54.598 13.773 1.00 37.26 ATOM 22 N LYS 10 −9.808 54.872 14.831 1.00 32.38 ATOM 23 CA LYS 10 −10.082 56.238 15.254 1.00 30.25 ATOM 24 CB LYS 10 −9.059 56.650 16.324 1.00 29.82 ATOM 25 C LYS 10 −10.044 57.227 14.079 1.00 28.52 ATOM 26 O LYS 10 −9.275 57.051 13.131 1.00 27.07 ATOM 27 N PRO 11 −10.880 58.281 14.129 1.00 27.69 ATOM 28 CD PRO 11 −11.964 58.562 15.084 1.00 26.12 ATOM 29 CA PRO 11 −10.885 59.261 13.035 1.00 27.89 ATOM 30 GB PRO 11 −12.094 60.145 13.357 1.00 26.47 ATOM 31 CG PRO 11 −12.967 59.261 14.206 1.00 27.98 ATOM 32 C PRO 11 −9.579 60.041 13.061 1.00 28.01 ATOM 33 O PRO 11 −9.038 60.303 14.126 1.00 31.43 ATOM 34 N LYS 12 −9.071 60.412 11.896 1.00 27.87 ATOM 35 CA LYS 12 −7.825 61.159 11.837 1.00 27.45 ATOM 36 CB LYS 12 −6.745 60.357 11.111 1.00 26.62 ATOM 37 CG LYS 12 −6.764 58.877 11.359 1.00 33.32 ATOM 38 CD LYS 12 −5.765 58.177 10.429 1.00 39.88 ATOM 39 CE LYS 12 −5.737 56.658 10.631 1.00 42.08 ATOM 40 NZ LYS 12 −4.753 56.011 9.717 1.00 45.02 ATOM 41 C LYS 12 −8.047 62.440 11.050 1.00 26.96 ATOM 42 O LYS 12 −9.171 62.785 10.684 1.00 27.06 ATOM 43 N LED 13 −6.950 63.137 10.797 1.00 22.89 ATOM 44 CA LED 13 −6.975 64.342 10.008 1.00 20.98 ATOM 45 CB LED 13 −6.530 65.547 10.828 1.00 18.90 ATOM 46 CG LED 13 −6.972 65.613 12.286 1.00 19.21 ATOM 47 CD1 LED 13 −6.081 66.620 13.034 1.00 17.37 ATOM 48 CD2 LED 13 −8.448 65.957 12.368 1.00 11.37 ATOM 49 C LEU 13 −5.916 64.030 8.962 1.00 23.04 ATOM 50 O LEU 13 −4.903 63.388 9.272 1.00 20.71 ATOM 51 N LED 14 −6.155 64.453 7.723 1.00 24.54 ATOM 52 CA LED 14 −5.192 64.230 6.657 1.00 25.10 ATOM 53 CB LEU 14 −5.877 63.676 5.395 1.00 26.61 ATOM 54 CG LED 14 −6.531 62.285 5.454 1.00 26.43 ATOM 55 CD1 LED 14 −6.795 61.800 4.037 1.00 26.12 ATOM 56 CD2 LED 14 −5.621 61.289 6.157 1.00 26.35 ATOM 57 CB LEU 14 −4.532 65.578 6.382 1.00 24.80 ATOM 58 O LEU 14 −5.057 66.414 5.650 1.00 29.43 ATOM 59 N TYR 15 −3.383 65.778 7.011 1.00 20.82 ATOM 60 CA TYR 15 −2.610 66.994 6.900 1.00 16.34 ATOM 61 GB TYR 15 −1.619 67.035 8.076 1.00 16.55 ATOM 62 CG TYR 15 −0.514 68.069 7.993 1.00 15.27 ATOM 63 CD1 TYR 15 0.667 67.811 7.296 1.00 11.64 ATOM 64 CE1 TYR 15 1.680 68.768 7.213 1.00 12.97 ATOM 65 CD2 TYR 15 −0.656 69.314 8.610 1.00 18.36 ATOM 66 CE2 TYR 15 0.351 70.281 8.538 1.00 17.26 ATOM 67 CZ TYR 15 1.513 70.005 7.838 1.00 16.66 ATOM 68 OH TYR 15 2.497 70.973 7.754 1.00 17.84 ATOM 69 C TYR 15 −1.886 66.980 5.571 1.00 16.68 ATOM 70 O TYR 15 −1.275 65.984 5.215 1.00 16.87 ATOM 71 N CYS 16 −1.970 68.074 4.824 1.00 17.57 ATOM 72 CA CYS 16 −1.277 68.158 3.546 1.00 21.60 ATOM 73 GB CYS 16 −2.156 68.814 2.491 1.00 21.60 ATOM 74 SG CYS 16 −1.350 68.884 0.878 1.00 24.76 ATOM 75 C CYS 16 −0.019 68.991 3.739 1.00 24.96 ATOM 76 O CYS 16 −0.082 70.116 4.239 1.00 24.56 ATOM 77 N SER 17 1.121 68.454 3.318 1.00 27.88 ATOM 78 CA SER 17 2.396 69.146 3.507 1.00 32.13 ATOM 79 GB SER 17 3.537 68.134 3.420 1.00 31.38 ATOM 80 OG SER 17 3.423 67.359 2.243 1.00 37.53 ATOM 81 C SER 17 2.697 70.337 2.596 1.00 33.49 ATOM 82 O SER 17 3.683 71.055 2.805 1.00 34.92 ATOM 83 N ASN 18 1.847 70.563 1.601 1.00 34.25 ATOM 84 CA ASN 18 2.057 71.665 0.670 1.00 33.45 ATOM 85 GB ASN 18 1.176 71.458 −0.564 1.00 35.74 ATOM 86 CG ASN 18 1.612 72.304 −1.742 1.00 37.98 ATOM 87 OD1 ASN 18 2.767 72.247 −2.175 1.00 39.41 ATOM 88 ND2 ASN 18 0.685 73.092 −2.273 1.00 39.81 ATOM 89 C ASN 18 1.814 73.057 1.285 1.00 31.98 ATOM 90 O ASN 18 2.399 74.035 0.843 1.00 34.60 ATOM 91 N GLY 19 0.971 73.150 2.306 1.00 29.15 ATOM 92 CA GLY 19 0.714 74.441 2.921 1.00 25.91 ATOM 93 C GLY 19 0.290 74.337 4.375 1.00 24.97 ATOM 94 O GLY 19 −0.056 75.331 5.025 1.00 20.29 ATOM 95 N GLY 20 0.314 73.113 4.886 1.00 26.22 ATOM 96 CA GLY 20 −0.066 72.881 6.264 1.00 28.13 ATOM 97 C GLY 20 −1.565 72.825 6.474 1.00 29.03 ATOM 98 O GLY 20 −2.030 72.932 7.614 1.00 30.16 ATOM 99 N HIS 21 −2.320 72.643 5.388 1.00 28.28 ATOM 100 CA HIS 21 −3.783 72.580 5.463 1.00 26.97 ATOM 101 GB HIS 21 −4.428 73.093 4.167 1.00 26.00 ATOM 102 CG HIS 21 −4.145 74.534 3.875 1.00 27.23 ATOM 103 CD2 HIS 21 −4.774 75.664 4.281 1.00 26.36 ATOM 104 ND1 HIS 21 −3.095 74.941 3.080 1.00 24.16 ATOM 105 CE1 HIS 21 −3.090 76.261 3.005 1.00 26.23 ATOM 106 NE2 HIS 21 −4.098 76.724 3.725 1.00 28.72 ATOM 107 C HIS 21 −4.326 71.188 5.740 1.00 26.11 ATOM 108 O HIS 21 −3.840 70.195 5.198 1.00 25.92 ATOM 109 N PHE 22 −5.343 71.130 6.592 1.00 26.87 ATOM 110 CA PHE 22 −5.998 69.872 6.934 1.00 26.99 ATOM 111 CB PHE 22 −6.611 69.925 8.339 1.00 27.89 ATOM 112 CG PHE 22 −5.597 70.021 9.441 1.00 34.47 ATOM 113 CD1 PHE 22 −5.700 69.214 10.567 1.00 35.19 ATOM 114 CD2 PHE 22 −4.530 70.917 9.353 1.00 37.94 ATOM 115 GE1 PHE 22 −4.764 69.296 11.582 1.00 35.09 ATOM 116 CE2 PHE 22 −3.590 71.005 10.366 1.00 36.95 ATOM 117 CZ PHE 22 −3.708 70.191 11.482 1.00 36.26 ATOM 118 C PHE 22 −7.114 69.645 5.929 1.00 26.43 ATOM 119 O PHE 22 −7.964 70.519 5.728 1.00 24.41 ATOM 120 N LEU 23 −7.116 68.472 5.301 1.00 24.90 ATOM 121 CA LEU 23 −8.148 68.163 4.330 1.00 21.79 ATOM 122 GB LEU 23 −7.981 66.731 3.829 1.00 20.26 ATOM 123 CG LEU 23 −8.783 66.381 2.571 1.00 22.41 ATOM 124 GD1 LEU 23 −8.610 67.473 1.509 1.00 21.81 ATOM 125 CD2 LEU 23 −8.323 65.032 2.035 1.00 20.82 ATOM 126 C LEU 23 −9.507 68.365 4.999 1.00 20.18 ATOM 127 O LEU 23 −9.754 67.854 6.089 1.00 19.53 ATOM 128 N ARG 24 −10.371 69.137 4.341 1.00 21.33 ATOM 129 CA ARG 24 −11.710 69.460 4.848 1.00 21.46 ATOM 130 GB ARG 24 −11.778 70.954 5.211 1.00 21.37 ATOM 131 CG ARG 24 −13.175 71.469 5.476 1.00 18.70 ATOM 132 CD ARG 24 −13.176 72.825 6.148 1.00 19.39 ATOM 133 NE ARG 24 −12.566 73.877 5.331 1.00 21.99 ATOM 134 GZ ARG 24 −12.638 75.179 5.610 1.00 18.80 ATOM 135 NH1 ARG 24 −13.296 75.601 6.682 1.00 14.56 ATOM 136 NH2 ARG 24 −12.043 76.063 4.822 1.00 18.72 ATOM 137 C ARG 24 −12.835 69.142 3.871 1.00 21.12 ATOM 138 O ARG 24 −12.712 69.368 2.669 1.00 24.62 ATOM 139 N ILE 25 −13.937 68.625 4.390 1.00 20.99 ATOM 140 GA ILE 25 −15.091 68.314 3.548 1.00 24.24 ATOM 141 GB ILE 25 −15.446 66.799 3.576 1.00 25.03 ATOM 142 CG2 ILE 25 −16.653 66.530 2.679 1.00 24.51 ATOM 143 CG1 ILE 25 −14.253 65.962 3.103 1.00 23.59 ATOM 144 CD1 ILE 25 −14.524 64.470 3.093 1.00 20.41 ATOM 145 C ILE 25 −16.298 69.105 4.059 1.00 25.48 ATOM 146 O ILE 25 −17.031 68.632 4.935 1.00 27.47 ATOM 147 N LEU 26 −16.490 70.308 3.515 1.00 25.58 ATOM 148 CA LEU 26 −17.594 71.179 3.913 1.00 26.62 ATOM 149 GB LEU 26 −17.450 72.535 3.231 1.00 27.43 ATOM 150 CG LEU 26 −16.176 73.273 3.645 1.00 27.65 ATOM 151 CD1 LEU 26 −15.932 74.464 2.718 1.00 26.42 ATOM 152 GD2 LEU 26 −16.302 73.703 5.105 1.00 21.68 ATOM 153 C LEU 26 −18.935 70.551 3.563 1.00 27.42 ATOM 154 O LEU 26 −19.108 70.007 2.477 1.00 27.49 ATOM 155 N PRO 27 −19.910 70.640 4.489 1.00 27.87 ATOM 156 GD PRO 27 −19.797 71.543 5.639 1.00 26.97 ATOM 157 CA PRO 27 −21.274 70.095 4.389 1.00 28.57 ATOM 158 GB PRO 27 −21.965 70.683 5.622 1.00 27.09 ATOM 159 CG PRO 27 −21.225 71.945 5.862 1.00 27.51 ATOM 160 C PRO 27 −22.067 70.316 3.097 1.00 29.49 ATOM 161 O PRO 27 −23.089 69.674 2.871 1.00 31.43 ATOM 162 N ASP 28 −21.584 71.198 2.242 1.00 29.56 ATOM 163 CA ASP 28 −22.239 71.494 0.977 1.00 31.81 ATOM 164 GB ASP 28 −22.107 72.980 0.732 1.00 35.00 ATOM 165 CG ASP 28 −20.752 73.492 1.163 1.00 39.97 ATOM 166 OD1 ASP 28 −19.774 73.299 0.398 1.00 38.80 ATOM 167 OD2 ASP 28 −20.663 74.049 2.288 1.00 40.66 ATOM 168 C ASP 28 −21.578 70.720 −0.165 1.00 32.77 ATOM 169 O ASP 28 −21.946 70.874 −1.331 1.00 32.13 ATOM 170 N GLY 29 −20.592 69.897 0.174 1.00 32.44 ATOM 171 GA GLY 29 −19.894 69.126 −0.834 1.00 32.39 ATOM 172 C GLY 29 −18.548 69.728 −1.199 1.00 34.62 ATOM 173 O GLY 29 −17.768 69.108 −1.923 1.00 35.14 ATOM 174 N THR 30 −18.264 70.931 −0.700 1.00 34.26 ATOM 175 GA THR 30 −16.997 71.596 −1.001 1.00 34.72 ATOM 176 GB THR 30 −17.054 73.104 −0.641 1.00 36.00 ATOM 177 OG1 THR 30 −17.726 73.813 −1.688 1.00 35.48 ATOM 178 CG2 THR 30 −15.643 73.684 −0.453 1.00 35.94 ATOM 179 C THR 30 −15.803 70.971 −0.289 1.00 34.24 ATOM 180 O THR 30 −15.786 70.875 0.939 1.00 36.02 ATOM 181 N VAL 31 −14.807 70.562 −1.075 1.00 33.03 ATOM 182 CA VAL 31 −13.581 69.946 −0.561 1.00 31.16 ATOM 183 GB VAL 31 −13.221 68.679 −1.375 1.00 30.16 ATOM 184 CG1 VAL 31 −11.803 68.227 −1.054 1.00 27.58 ATOM 185 CG2 VAL 31 −14.222 67.567 −1.063 1.00 24.85 ATOM 186 C VAL 31 −12.426 70.945 −0.618 1.00 30.88 ATOM 187 O VAL 31 −12.103 71.496 −1.675 1.00 30.91 ATOM 188 N ASP 32 −11.797 71.171 0.526 1.00 30.08 ATOM 189 CA ASP 32 −10.710 72.143 0.603 1.00 29.27 ATOM 190 GB ASP 32 −11.295 73.551 0.712 1.00 26.28 ATOM 191 CG ASP 32 −11.861 73.839 2.100 1.00 24.69 ATOM 192 OD1 ASP 32 −12.213 72.887 2.838 1.00 24.75 ATOM 193 OD2 ASP 32 −11.960 75.022 2.460 1.00 26.59 ATOM 194 C ASP 32 −9.855 71.889 1.834 1.00 28.84 ATOM 195 O ASP 32 −9.974 70.850 2.484 1.00 25.70 ATOM 196 N GLY 33 −9.013 72.870 2.158 1.00 29.42 ATOM 197 CA GLY 33 −8.148 72.764 3.317 1.00 28.55 ATOM 198 C GLY 33 −8.264 73.951 4.252 1.00 26.20 ATOM 199 O GLY 33 −8.721 75.017 3.861 1.00 25.20 ATOM 200 N THR 34 −7.853 73.749 5.499 1.00 27.35 ATOM 201 CA THR 34 −7.872 74.796 6.517 1.00 27.58 ATOM 202 GB THR 34 −9.186 74.802 7.313 1.00 27.59 ATOM 203 OG1 THR 34 −8.988 75.504 8.547 1.00 26.09 ATOM 204 CG2 THR 34 −9.642 73.387 7.605 1.00 30.18 ATOM 205 C THR 34 −6.730 74.588 7.500 1.00 28.50 ATOM 206 O THR 34 −6.192 73.485 7.611 1.00 31.02 ATOM 207 N ARG 35 −6.357 75.642 8.216 1.00 27.33 ATOM 208 CA ARG 35 −5.278 75.525 9.187 1.00 25.21 ATOM 209 GB ARG 35 −4.282 76.671 9.014 1.00 25.09 ATOM 210 CG ARG 35 −3.544 76.673 7.685 1.00 25.03 ATOM 211 CD ARG 35 −2.526 77.804 7.631 1.00 26.07 ATOM 212 NE ARG 35 −1.560 77.601 6.554 1.00 28.74 ATOM 213 CZ ARG 35 −1.337 78.472 5.572 1.00 32.52 ATOM 214 NH1 ARG 35 −2.003 79.624 5.517 1.00 32.37 ATOM 215 NH2 ARG 35 −0.457 78.185 4.628 1.00 34.71 ATOM 216 C ARG 35 −5.826 75.532 10.604 1.00 26.22 ATOM 217 O ARG 35 −5.095 75.788 11.550 1.00 28.51 ATOM 218 N ASP 36 −7.115 75.252 10.751 1.00 27.90 ATOM 219 CA ASP 36 −7.753 75.234 12.064 1.00 30.78 ATOM 220 GB ASP 36 −8.994 76.111 12.032 1.00 33.11 ATOM 221 CG ASP 36 −9.836 75.956 13.270 1.00 36.94 ATOM 222 OD1 ASP 36 −10.985 76.458 13.260 1.00 36.42 ATOM 223 OD2 ASP 36 −9.342 75.335 14.246 1.00 35.09 ATOM 224 C ASP 36 −8.141 73.817 12.523 1.00 32.42 ATOM 225 O ASP 36 −8.946 73.140 11.876 1.00 31.43 ATOM 226 N ARG 37 −7.587 73.386 13.657 1.00 32.70 ATOM 227 CA ARG 37 −7.863 72.046 14.173 1.00 30.63 ATOM 228 GB ARG 37 −6.715 71.530 15.053 1.00 28.29 ATOM 229 CG ARG 37 −5.446 71.235 14.284 1.00 30.34 ATOM 230 CD ARG 37 −4.372 70.546 15.121 1.00 28.87 ATOM 231 NE ARG 37 −4.700 69.167 15.474 1.00 26.36 ATOM 232 CZ ARG 37 −3.783 68.223 15.691 1.00 28.48 ATOM 233 NH1 ARG 37 −2.484 68.505 15.588 1.00 20.85 ATOM 234 NH2 ARG 37 −4.160 66.994 16.016 1.00 28.70 ATOM 235 C ARG 37 −9.143 71.938 14.951 1.00 28.28 ATOM 236 O ARG 37 −9.576 70.833 15.262 1.00 27.31 ATOM 237 N SER 38 −9.744 73.067 15.290 1.00 25.88 ATOM 238 CA SER 38 −10.984 72.998 16.036 1.00 28.07 ATOM 239 GB SER 38 −11.111 74.183 16.996 1.00 28.83 ATOM 240 OG SER 38 −10.866 75.412 16.344 1.00 34.41 ATOM 241 C SER 38 −12.161 72.939 15.070 1.00 27.66 ATOM 242 O SER 38 −13.306 72.723 15.489 1.00 28.69 ATOM 243 N ASP 39 −11.859 73.119 13.780 1.00 25.52 ATOM 244 CA ASP 39 −12.856 73.070 12.707 1.00 21.79 ATOM 245 CB ASP 39 −12.161 73.216 11.354 1.00 24.27 ATOM 246 CG ASP 39 −13.134 73.216 10.183 1.00 27.75 ATOM 247 OD1 ASP 39 −13.849 72.217 9.989 1.00 32.47 ATOM 248 OD2 ASP 39 −13.184 74.217 9.437 1.00 28.63 ATOM 249 C ASP 39 −13.529 71.716 12.800 1.00 21.20 ATOM 250 O ASP 39 −12.852 70.690 12.818 1.00 19.87 ATOM 251 N GLN 40 −14.857 71.710 12.859 1.00 22.40 ATOM 252 CA GLN 40 −15.617 70.467 12.988 1.00 23.65 ATOM 253 CB GLN 40 −17.051 70.781 13.402 1.00 23.78 ATOM 254 C GLN 40 −15.663 69.525 11.787 1.00 26.05 ATOM 255 O GLN 40 −16.152 68.407 11.922 1.00 28.44 ATOM 256 N HIS 41 −15.152 69.945 10.629 1.00 27.23 ATOM 257 CA HIS 41 −15.206 69.100 9.433 1.00 30.01 ATOM 258 CB HIS 41 −15.914 69.859 8.306 1.00 33.08 ATOM 259 CG HIS 41 −17.335 70.219 8.623 1.00 36.53 ATOM 260 CD2 HIS 41 −18.481 69.511 8.491 1.00 36.05 ATOM 261 ND1 HIS 41 −17.691 71.426 9.185 1.00 34.96 ATOM 262 CE1 HIS 41 −18.997 71.445 9.388 1.00 33.67 ATOM 263 NE2 HIS 41 −19.501 70.296 8.977 1.00 34.10 ATOM 264 C HIS 41 −13.900 68.500 8.883 1.00 30.83 ATOM 265 O HIS 41 −13.843 68.071 7.715 1.00 29.28 ATOM 266 N ILE 42 −12.859 68.455 9.709 1.00 29.98 ATOM 267 CA ILE 42 −11.578 67.899 9.274 1.00 27.41 ATOM 268 CB ILE 42 −10.392 68.785 9.737 1.00 26.47 ATOM 269 CG2 ILE 42 −10.168 69.898 8.740 1.00 28.37 ATOM 270 CG1 ILE 42 −10.658 69.351 11.133 1.00 22.43 ATOM 271 CD1 ILE 42 −9.469 70.047 11.736 1.00 21.79 ATOM 272 C ILE 42 −11.332 66.453 9.729 1.00 26.46 ATOM 273 O ILE 42 −10.399 65.801 9.247 1.00 25.66 ATOM 274 N GLN 43 −12.168 65.959 10.642 1.00 23.87 ATOM 275 CA GLN 43 −12.037 64.595 11.148 1.00 24.15 ATOM 276 CB GLN 43 −12.778 64.438 12.477 1.00 24.07 ATOM 277 CC GLN 43 −12.360 65.405 13.552 1.00 26.31 ATOM 278 CD GLN 43 −12.992 66.764 13.382 1.00 27.49 ATOM 279 OE1 GLN 43 −14.216 66.897 13.447 1.00 32.47 ATOM 280 NE2 GLN 43 −12.168 67.786 13.167 1.00 24.21 ATOM 281 C GLN 43 −12.577 63.562 10.157 1.00 22.64 ATOM 282 O GLN 43 −13.765 63.524 9.862 1.00 23.92 ATOM 283 N LEU 44 −11.698 62.697 9.686 1.00 21.43 ATOM 284 CA LEU 44 −12.072 61.691 8.715 1.00 22.69 ATOM 285 CB LEU 44 −11.224 61.871 7.452 1.00 18.32 ATOM 286 CG LEU 44 −10.987 63.346 7.110 1.00 17.15 ATOM 287 CD1 LEU 44 −9.968 63.467 5.977 1.00 12.49 ATOM 288 CD2 LEU 44 −12.322 64.014 6.773 1.00 11.74 ATOM 289 C LEU 44 −11.922 60.261 9.216 1.00 25.60 ATOM 290 O LEU 44 −11.048 59.943 10.031 1.00 27.19 ATOM 291 N GLN 45 −12.782 59.398 8.693 1.00 26.35 ATOM 292 CA GLN 45 −12.775 57.996 9.039 1.00 26.11 ATOM 293 CB GLN 45 −14.130 57.600 9.610 1.00 29.41 ATOM 294 CC GLN 45 −14.122 56.242 10.247 1.00 33.87 ATOM 295 CD GLN 45 −13.128 56.188 11.378 1.00 37.58 ATOM 296 OE1 GLN 45 −13.257 56.925 12.359 1.00 39.35 ATOM 297 NE2 GLN 45 −12.119 55.325 11.247 1.00 37.04 ATOM 298 C GLN 45 −12.481 57.173 7.781 1.00 26.30 ATOM 299 O GLN 45 −13.370 56.933 6.960 1.00 27.12 ATOM 300 N LEU 46 −11.228 56.752 7.637 1.00 23.91 ATOM 301 CA LEU 46 −10.806 55.954 6.502 1.00 21.84 ATOM 302 GB LEU 46 −9.293 56.072 6.312 1.00 21.30 ATOM 303 CG LEU 46 −8.801 57.321 5.564 1.00 22.12 ATOM 304 CD1 LEU 46 −9.167 58.593 6.300 1.00 19.17 ATOM 305 CD2 LEU 46 −7.308 57.221 5.386 1.00 24.79 ATOM 306 C LEU 46 −11.196 54.499 6.706 1.00 22.57 ATOM 307 O LEU 46 −11.141 53.992 7.821 1.00 21.81 ATOM 308 N SER 47 −11.598 53.835 5.624 1.00 25.02 ATOM 309 CA SER 47 −12.010 52.429 5.677 1.00 25.85 ATOM 310 CB SER 47 −13.529 52.328 5.762 1.00 23.77 ATOM 311 OG SER 47 −14.085 53.517 6.293 1.00 29.89 ATOM 312 C SER 47 −11.540 51.683 4.429 1.00 27.64 ATOM 313 O SER 47 −11.490 52.248 3.332 1.00 28.03 ATOM 314 N ALA 48 −11.207 50.408 4.588 1.00 28.72 ATOM 315 CA ALA 48 −10.755 49.618 3.456 1.00 31.22 ATOM 316 GB ALA 48 −9.605 48.716 3.875 1.00 31.58 ATOM 317 C ALA 48 −11.876 48.779 2.855 1.00 33.53 ATOM 318 O ALA 48 −12.469 47.938 3.528 1.00 34.12 ATOM 319 N GLU 49 −12.178 49.023 1.586 1.00 35.72 ATOM 320 CA GLU 49 −13.201 48.247 0.900 1.00 37.48 ATOM 321 GB GLU 49 −13.668 48.988 −0.357 1.00 41.73 ATOM 322 CG GLU 49 −14.710 48.245 −1.190 1.00 49.89 ATOM 323 CD GLU 49 −15.845 47.643 −0.350 1.00 56.40 ATOM 324 OE1 GLU 49 −16.359 48.326 0.570 1.00 58.69 ATOM 325 OE2 GLU 49 −16.233 46.483 −0.623 1.00 59.10 ATOM 326 C GLU 49 −12.510 46.938 0.519 1.00 36.22 ATOM 327 O GLU 49 −13.113 45.864 0.516 1.00 36.49 ATOM 328 N SER 50 −11.222 47.061 0.217 1.00 33.53 ATOM 329 CA SER 50 −10.369 45.950 −0.175 1.00 29.49 ATOM 330 GB SER 50 −10.395 45.768 −1.690 1.00 29.77 ATOM 331 OG SER 50 −11.727 45.725 −2.174 1.00 33.14 ATOM 332 C SER 50 −8.976 46.376 0.242 1.00 28.11 ATOM 333 O SER 50 −8.779 47.531 0.625 1.00 29.53 ATOM 334 N VAL 51 −8.015 45.459 0.172 1.00 23.82 ATOM 335 CA VAL 51 −6.643 45.782 0.537 1.00 18.87 ATOM 336 GB VAL 51 −5.678 44.594 0.243 1.00 18.83 ATOM 337 CG1 VAL 51 −4.234 44.969 0.600 1.00 16.48 ATOM 338 CG2 VAL 51 −6.103 43.372 1.024 1.00 15.72 ATOM 339 C VAL 51 −6.197 46.982 −0.294 1.00 18.34 ATOM 340 O VAL 51 −6.427 47.026 −1.500 1.00 19.32 ATOM 341 N GLY 52 −5.582 47.961 0.357 1.00 17.24 ATOM 342 CA GLY 52 −5.085 49.135 −0.344 1.00 16.86 ATOM 343 C GLY 52 −6.058 50.189 −0.839 1.00 17.15 ATOM 344 O GLY 52 −5.634 51.293 −1.154 1.00 16.89 ATOM 345 N GLU 53 −7.345 49.865 −0.919 1.00 20.93 ATOM 346 CA GLU 53 −8.354 50.809 −1.404 1.00 24.08 ATOM 347 GB GLU 53 −9.283 50.113 −2.387 1.00 26.57 ATOM 348 CG GLU 53 −8.591 49.029 −3.178 1.00 31.61 ATOM 349 CD GLU 53 −9.445 48.463 −4.292 1.00 34.45 ATOM 350 OE1 GLU 53 −10.637 48.139 −4.048 1.00 36.05 ATOM 351 OE2 GLU 53 −8.904 48.336 −5.412 1.00 34.43 ATOM 352 C GLU 53 −9.153 51.321 −0.224 1.00 25.65 ATOM 353 O GLU 53 −9.654 50.533 0.582 1.00 26.79 ATOM 354 N VAL 54 −9.306 52.637 −0.132 1.00 25.28 ATOM 355 CA VAL 54 −10.000 53.198 1.012 1.00 25.84 ATOM 356 GB VAL 54 −8.991 53.874 1.986 1.00 27.15 ATOM 357 CG1 VAL 54 −7.793 52.970 2.223 1.00 26.22 ATOM 358 CG2 VAL 54 −8.520 55.202 1.420 1.00 26.83 ATOM 359 C VAL 54 −11.081 54.221 0.737 1.00 27.05 ATOM 360 O VAL 54 −11.087 54.896 −0.290 1.00 29.16 ATOM 361 N TYR 55 −12.007 54.310 1.680 1.00 27.41 ATOM 362 CA TYR 55 −13.063 55.305 1.642 1.00 26.40 ATOM 363 CB TYR 55 −14.401 54.734 2.114 1.00 27.97 ATOM 364 CG TYR 55 −15.119 53.901 1.079 1.00 31.95 ATOM 365 CD1 TYR 55 −15.442 54.432 −0.174 1.00 30.89 ATOM 366 CE1 TYR 55 −16.139 53.686 −1.113 1.00 29.38 ATOM 367 CD2 TYR 55 −15.511 52.594 1.364 1.00 32.02 ATOM 368 CE2 TYR 55 −16.211 51.840 0.432 1.00 33.83 ATOM 369 CZ TYR 55 −16.525 52.390 −0.806 1.00 31.97 ATOM 370 OH TYR 55 −17.239 51.642 −1.716 1.00 29.18 ATOM 371 C TYR 55 −12.559 56.324 2.665 1.00 25.59 ATOM 372 O TYR 55 −11.805 55.977 3.584 1.00 21.61 ATOM 373 N ILE 56 −12.972 57.573 2.504 1.00 22.88 ATOM 374 CA ILE 56 −12.547 58.628 3.398 1.00 20.19 ATOM 375 CB ILE 56 −11.459 59.468 2.728 1.00 18.99 ATOM 376 CG2 ILE 56 −11.139 60.690 3.585 1.00 20.24 ATOM 377 CG1 ILE 56 −10.234 58.589 2.461 1.00 15.90 ATOM 378 CD1 ILE 56 −9.179 59.251 1.601 1.00 17.40 ATOM 379 C ILE 56 −13.750 59.491 3.656 1.00 20.26 ATOM 380 O ILE 56 −14.124 60.276 2.797 1.00 23.54 ATOM 381 N LYS 57 −14.370 59.371 4.823 1.00 22.25 ATOM 382 CA LYS 57 −15.556 60.189 5.055 1.00 26.24 ATOM 383 CB LYS 57 −16.821 59.323 5.029 1.00 26.57 ATOM 384 CG LYS 57 −17.092 58.562 6.298 1.00 28.92 ATOM 385 CD LYS 57 −18.595 58.459 6.529 1.00 33.90 ATOM 386 CE LYS 57 −18.903 57.855 7.894 1.00 36.61 ATOM 387 NZ LYS 57 −20.284 58.199 8.350 1.00 38.42 ATOM 388 C LYS 57 −15.590 61.058 6.301 1.00 26.39 ATOM 389 O LYS 57 −15.146 60.663 7.374 1.00 24.91 ATOM 390 N SER 58 −16.146 62.251 6.134 1.00 27.09 ATOM 391 CA SER 58 −16.287 63.185 7.230 1.00 27.99 ATOM 392 CB SER 58 −16.995 64.457 6.754 1.00 28.30 ATOM 393 OG SER 58 −17.171 65.390 7.806 1.00 24.98 ATOM 394 C SER 58 −17.118 62.508 8.309 1.00 29.22 ATOM 395 O SER 58 −18.149 61.895 8.027 1.00 28.11 ATOM 396 N THR 59 −16.653 62.616 9.545 1.00 31.50 ATOM 397 CA THR 59 −17.344 62.033 10.684 1.00 32.90 ATOM 398 CB THR 59 −16.410 61.942 11.879 1.00 35.91 ATOM 399 OG1 THR 59 −15.721 63.193 12.011 1.00 40.36 ATOM 400 CG2 THR 59 −15.397 60.808 11.694 1.00 39.43 ATOM 401 C THR 59 −18.505 62.932 11.067 1.00 30.76 ATOM 402 O THR 59 −19.514 62.474 11.589 1.00 28.04 ATOM 403 N GLU 60 −18.347 64.221 10.793 1.00 31.18 ATOM 404 CA GLU 60 −19.367 65.201 11.119 1.00 30.56 ATOM 405 CB GLU 60 −18.790 66.614 10.998 1.00 32.59 ATOM 406 CC GLU 60 −19.522 67.642 11.850 1.00 34.81 ATOM 407 CD GLU 60 −19.646 67.193 13.304 1.00 36.76 ATOM 408 OE1 GLU 60 −18.625 66.744 13.885 1.00 38.08 ATOM 409 OE2 GLU 60 −20.760 67.288 13.864 1.00 33.66 ATOM 410 C GLU 60 −20.603 65.087 10.244 1.00 29.55 ATOM 411 O GLU 60 −21.719 64.952 10.744 1.00 27.43 ATOM 412 N THR 61 −20.394 65.132 8.933 1.00 30.33 ATOM 413 CA THR 61 −21.497 65.073 7.983 1.00 29.96 ATOM 414 CB THR 61 −21.283 66.103 6.855 1.00 28.13 ATOM 415 OG1 THR 61 −20.209 65.682 6.013 1.00 28.36 ATOM 416 CG2 THR 61 −20.933 67.452 7.441 1.00 25.56 ATOM 417 C THR 61 −21.775 63.702 7.355 1.00 31.53 ATOM 418 O THR 61 −22.871 63.464 6.851 1.00 35.52 ATOM 419 N GLY 62 −20.806 62.795 7.386 1.00 30.76 ATOM 420 CA GLY 62 −21.038 61.492 6.791 1.00 28.64 ATOM 421 C GLY 62 −20.905 61.548 5.276 1.00 28.22 ATOM 422 O GLY 62 −21.453 60.718 4.555 1.00 26.62 ATOM 423 N GLN 63 −20.182 62.548 4.788 1.00 27.17 ATOM 424 CA GLN 63 −19.965 62.685 3.359 1.00 26.55 ATOM 425 GB GLN 63 −19.825 64.150 2.950 1.00 26.28 ATOM 426 CG GLN 63 −21.023 65.036 3.212 1.00 29.09 ATOM 427 CD GLN 63 −20.740 66.481 2.825 1.00 30.75 ATOM 428 OE1 GLN 63 −20.734 66.832 1.639 1.00 30.33 ATOM 429 NE2 GLN 63 −20.478 67.320 3.823 1.00 26.29 ATOM 430 C GLN 63 −18.670 61.975 3.010 1.00 25.88 ATOM 431 O GLN 63 −17.733 61.958 3.812 1.00 27.47 ATOM 432 N TYR 64 −18.620 61.397 1.813 1.00 23.34 ATOM 433 CA TYR 64 −17.426 60.706 1.350 1.00 21.48 ATOM 434 GB TYR 64 −17.786 59.442 0.568 1.00 20.38 ATOM 435 CG TYR 64 −18.377 58.359 1.426 1.00 20.27 ATOM 436 CD1 TYR 64 −19.697 58.430 1.864 1.00 19.31 ATOM 437 CE1 TYR 64 −20.225 57.466 2.711 1.00 18.93 ATOM 438 CD2 TYR 64 −17.601 57.289 1.853 1.00 21.00 ATOM 439 CE2 TYR 64 −18.124 56.317 2.701 1.00 20.56 ATOM 440 CZ TYR 64 −19.430 56.414 3.128 1.00 19.38 ATOM 441 OH TYR 64 −19.929 55.470 3.994 1.00 22.05 ATOM 442 C TYR 64 −16.622 61.626 0.459 1.00 20.42 ATOM 443 O TYR 64 −17.178 62.458 −0.250 1.00 20.96 ATOM 444 N LEU 65 −15.306 61.500 0.525 1.00 19.55 ATOM 445 CA LEU 65 −14.455 62.310 −0.307 1.00 20.09 ATOM 446 GB LEU 65 −13.037 62.355 0.250 1.00 20.85 ATOM 447 CG LEU 65 −11.985 63.017 −0.650 1.00 23.92 ATOM 448 CD1 LEU 65 −12.249 64.512 −0.740 1.00 22.56 ATOM 449 CD2 LEU 65 −10.591 62.749 −0.104 1.00 23.40 ATOM 450 C LEU 65 −14.481 61.564 −1.624 1.00 23.95 ATOM 451 O LEU 65 −14.342 60.340 −1.659 1.00 25.36 ATOM 452 N ALA 66 −14.676 62.302 −2.705 1.00 27.03 ATOM 453 CA ALA 66 −14.742 61.709 −4.023 1.00 27.15 ATOM 454 GB ALA 66 −16.183 61.376 −4.356 1.00 24.77 ATOM 455 C ALA 66 −14.159 62.648 −5.071 1.00 30.07 ATOM 456 O ALA 66 −13.918 63.831 −4.817 1.00 30.31 ATOM 457 N MET 67 −13.941 62.104 −6.258 1.00 34.43 ATOM 458 CA MET 67 −13.382 62.857 −7.367 1.00 36.96 ATOM 459 GB MET 67 −11.962 62.358 −7.648 1.00 35.46 ATOM 460 CG MET 67 −11.258 63.064 −8.787 1.00 38.86 ATOM 461 SD MET 67 −9.536 62.515 −9.015 1.00 37.06 ATOM 462 CE MET 67 −8.656 63.791 −8.190 1.00 37.88 ATOM 463 C MET 67 −14.280 62.676 −8.599 1.00 38.79 ATOM 464 O MET 67 −14.544 61.546 −9.021 1.00 40.47 ATOM 465 N ASP 68 −14.755 63.793 −9.152 1.00 38.95 ATOM 466 CA ASP 68 −15.618 63.787 −10.328 1.00 38.31 ATOM 467 GB ASP 68 −16.291 65.159 −10.506 1.00 41.23 ATOM 468 CG ASP 68 −15.304 66.266 −10.876 1.00 43.09 ATOM 469 OD1 ASP 68 −15.723 67.440 −10.950 1.00 43.77 ATOM 470 OD2 ASP 68 −14.115 65.967 −11.097 1.00 44.63 ATOM 471 C ASP 68 −14.794 63.448 −11.561 1.00 37.61 ATOM 472 O ASP 68 −13.568 63.374 −11.496 1.00 35.14 ATOM 473 N THR 69 −15.465 63.260 −12.690 1.00 39.16 ATOM 474 CA THR 69 −14.761 62.924 −13.920 1.00 40.40 ATOM 475 GB THR 69 −15.744 62.541 −15.031 1.00 39.26 ATOM 476 OG1 THR 69 −16.749 61.668 −14.497 1.00 41.34 ATOM 477 CG2 THR 69 −15.005 61.806 −16.147 1.00 39.63 ATOM 478 C THR 69 −13.857 64.053 −14.411 1.00 40.83 ATOM 479 O THR 69 −13.095 63.873 −15.357 1.00 40.64 ATOM 480 N ASP 70 −13.936 65.213 −13.760 1.00 42.39 ATOM 481 CA ASP 70 −13.109 66.372 −14.114 1.00 41.09 ATOM 482 GB ASP 70 −13.790 67.681 −13.702 1.00 46.08 ATOM 483 CG ASP 70 −14.998 68.015 −14.553 1.00 51.55 ATOM 484 OD1 ASP 70 −15.830 68.826 −14.092 1.00 52.51 ATOM 485 OD2 ASP 70 −15.113 67.483 −15.680 1.00 54.94 ATOM 486 C ASP 70 −11.798 66.289 −13.358 1.00 38.67 ATOM 487 O ASP 70 −10.768 66.769 −13.817 1.00 37.28 ATOM 488 N GLY 71 −11.856 65.673 −12.184 1.00 37.56 ATOM 489 CA GLY 71 −10.683 65.559 −11.338 1.00 33.59 ATOM 490 C GLY 71 −10.841 66.565 −10.219 1.00 29.81 ATOM 491 O GLY 71 −9.875 67.163 −9.760 1.00 26.66 ATOM 492 N LEU 72 −12.085 66.755 −9.795 1.00 28.78 ATOM 493 CA LEU 72 −12.399 67.697 −8.742 1.00 29.10 ATOM 494 CB LEU 72 −13.393 68.739 −9.246 1.00 28.03 ATOM 495 CG LEU 72 −12.841 69.618 −10.364 1.00 29.44 ATOM 496 CD1 LEU 72 −13.782 70.807 −10.572 1.00 30.22 ATOM 497 CD2 LEU 72 −11.440 70.103 −10.003 1.00 28.57 ATOM 498 C LEU 72 −12.960 67.003 −7.517 1.00 29.08 ATOM 499 O LEU 72 −13.933 66.252 −7.600 1.00 27.03 ATOM 500 N LEU 73 −12.338 67.275 −6.374 1.00 27.78 ATOM 501 CA LEU 73 −12.750 66.675 −5.113 1.00 26.97 ATOM 502 CB LEU 73 −11.681 66.924 −4.045 1.00 27.63 ATOM 503 CG LEU 73 −10.278 66.405 −4.357 1.00 27.56 ATOM 504 CD1 LEU 73 −9.301 66.946 −3.324 1.00 27.62 ATOM 505 CD2 LEU 73 −10.283 64.882 −4.377 1.00 27.97 ATOM 506 C LEU 73 −14.080 67.248 −4.652 1.00 25.28 ATOM 507 O LEU 73 −14.342 68.438 −4.827 1.00 25.28 ATOM 508 N TYR 74 −14.918 66.399 −4.064 1.00 21.91 ATOM 509 CA TYR 74 −16.212 66.844 −3.579 1.00 18.97 ATOM 510 CB TYR 74 −17.169 66.991 −4.755 1.00 17.95 ATOM 511 CG TYR 74 −17.592 65.673 −5.361 1.00 16.96 ATOM 512 CD1 TYR 74 −18.741 65.008 −4.905 1.00 15.81 ATOM 513 CE1 TYR 74 −19.112 63.783 −5.424 1.00 12.54 ATOM 514 CD2 TYR 74 −16.832 65.071 −6.359 1.00 15.33 ATOM 515 CE2 TYR 74 −17.196 63.839 −6.888 1.00 14.99 ATOM 516 CZ TYR 74 −18.336 63.206 −6.414 1.00 16.26 ATOM 517 OH TYR 74 −18.700 61.989 −6.931 1.00 21.19 ATOM 518 C TYR 74 −16.777 65.857 −2.562 1.00 19.47 ATOM 519 O TYR 74 −16.400 64.686 −2.550 1.00 16.67 ATOM 520 N GLY 75 −17.676 66.337 −1.707 1.00 19.57 ATOM 521 CA GLY 75 −18.275 65.475 −0.707 1.00 22.20 ATOM 522 C GLY 75 −19.448 64.718 −1.294 1.00 24.60 ATOM 523 O GLY 75 −20.259 65.294 −2.020 1.00 27.99 ATOM 524 N SER 76 −19.552 63.433 −0.978 1.00 22.61 ATOM 525 CA SER 76 −20.630 62.618 −1.506 1.00 21.82 ATOM 526 CB SER 76 −20.035 61.486 −2.348 1.00 20.60 ATOM 527 OG SER 76 −21.048 60.702 −2.949 1.00 21.71 ATOM 528 C SER 76 −21.533 62.056 −0.411 1.00 21.49 ATOM 529 O SER 76 −21.073 61.376 0.490 1.00 20.33 ATOM 530 N GLN 77 −22.826 62.335 −0.508 1.00 24.07 ATOM 531 CA GLN 77 −23.798 61.869 0.479 1.00 28.51 ATOM 532 CB GLN 77 −25.205 62.352 0.098 1.00 34.41 ATOM 533 CG GLN 77 −25.326 63.863 −0.168 1.00 45.41 ATOM 534 CD GLN 77 −24.368 64.366 −1.267 1.00 54.19 ATOM 535 OE1 GLN 77 −24.358 63.851 −2.396 1.00 55.96 ATOM 536 NE2 GLN 77 −23.560 65.379 −0.932 1.00 56.37 ATOM 537 C GLN 77 −23.798 60.342 0.621 1.00 27.85 ATOM 538 O GLN 77 −24.117 59.810 1.681 1.00 27.20 ATOM 539 N THR 78 −23.453 59.645 −0.456 1.00 27.43 ATOM 540 CA THR 78 −23.407 58.186 −0.455 1.00 27.61 ATOM 541 CB THR 78 −24.645 57.547 −1.165 1.00 27.98 ATOM 542 OG1 THR 78 −24.739 58.046 −2.506 1.00 28.83 ATOM 543 CG2 THR 78 −25.937 57.861 −0.417 1.00 26.27 ATOM 544 C THR 78 −22.152 57.751 −1.202 1.00 27.82 ATOM 545 O THR 78 −21.729 58.408 −2.150 1.00 23.73 ATOM 546 N PRO 79 −21.549 56.624 −0.787 1.00 30.18 ATOM 547 CD PRO 79 −22.019 55.768 0.319 1.00 30.98 ATOM 548 CA PRO 79 −20.334 56.063 −1.388 1.00 31.93 ATOM 549 CB PRO 79 −19.925 54.995 −0.383 1.00 30.66 ATOM 550 CG PRO 79 −21.250 54.488 0.086 1.00 30.46 ATOM 551 C PRO 79 −20.541 55.483 −2.783 1.00 32.59 ATOM 552 O PRO 79 −21.607 54.966 −3.096 1.00 33.82 ATOM 553 N ASN 80 −19.509 55.564 −3.612 1.00 33.04 ATOM 554 CA ASN 80 −19.572 55.039 −4.971 1.00 33.28 ATOM 555 CB ASN 80 −20.420 55.936 −5.859 1.00 29.97 ATOM 556 CG ASN 80 −20.002 57.386 −5.784 1.00 29.20 ATOM 557 OD1 ASN 80 −20.748 58.214 −5.269 1.00 30.68 ATOM 558 ND2 ASN 80 −18.803 57.704 −6.291 1.00 23.38 ATOM 559 C ASN 80 −18.177 54.945 −5.561 1.00 35.65 ATOM 560 O ASN 80 −17.189 55.300 −4.909 1.00 35.39 ATOM 561 N GLU 81 −18.104 54.480 −6.805 1.00 36.21 ATOM 562 CA GLU 81 −16.825 54.314 −7.488 1.00 36.30 ATOM 563 CB GLU 81 −17.071 53.887 −8.939 1.00 36.57 ATOM 564 CG GLU 81 −18.466 54.213 −9.440 1.00 40.67 ATOM 565 CD GLU 81 −18.543 55.520 −10.204 1.00 42.55 ATOM 566 OE1 GLU 81 −19.640 56.126 −10.222 1.00 41.85 ATOM 567 OE2 GLU 81 −17.517 55.928 −10.801 1.00 43.69 ATOM 568 C GLU 81 −15.943 55.561 −7.425 1.00 34.33 ATOM 569 O GLU 81 −14.705 55.467 −7.394 1.00 34.21 ATOM 570 N GLU 82 −16.576 56.726 −7.375 1.00 31.15 ATOM 571 CA GLU 82 −15.826 57.967 −7.317 1.00 31.48 ATOM 572 CB GLU 82 −16.699 59.121 −7.786 1.00 32.95 ATOM 573 CG GLU 82 −17.301 58.921 −9.159 1.00 32.36 ATOM 574 CD GLU 82 −17.451 60.229 −9.903 1.00 33.17 ATOM 575 OE1 GLU 82 −18.079 61.161 −9.340 1.00 28.95 ATOM 576 OE2 GLU 82 −16.932 60.321 −11.045 1.00 35.17 ATOM 577 C GLU 82 −15.273 58.283 −5.921 1.00 31.15 ATOM 578 O GLU 82 −14.557 59.262 −5.745 1.00 29.43 ATOM 579 N CYS 83 −15.597 57.446 −4.939 1.00 30.14 ATOM 580 CA CYS 83 −15.146 57.650 −3.568 1.00 29.65 ATOM 581 CB CYS 83 −16.271 57.325 −2.590 1.00 30.22 ATOM 582 SG CYS 83 −17.782 58.220 −2.865 1.00 34.01 ATOM 583 C CYS 83 −13.929 56.816 −3.179 1.00 30.18 ATOM 584 O CYS 83 −13.219 57.161 −2.238 1.00 33.02 ATOM 585 N LEU 84 −13.701 55.717 −3.888 1.00 29.32 ATOM 586 CA LEU 84 −12.580 54.832 −3.598 1.00 28.07 ATOM 587 CB LEU 84 −12.810 53.461 −4.231 1.00 29.59 ATOM 588 CG LEU 84 −13.832 52.567 −3.541 1.00 30.10 ATOM 589 CD1 LEU 84 −14.063 51.344 −4.380 1.00 30.11 ATOM 590 CD2 LEU 84 −13.332 52.186 −2.156 1.00 31.23 ATOM 591 C LEU 84 −11.233 55.361 −4.057 1.00 27.57 ATOM 592 O LEU 84 −11.047 55.711 −5.228 1.00 26.72 ATOM 593 N PHE 85 −10.289 55.390 −3.122 1.00 24.59 ATOM 594 CA PHE 85 −8.946 55.860 −3.405 1.00 24.16 ATOM 595 CB PHE 85 −8.681 57.157 −2.635 1.00 23.67 ATOM 596 CG PHE 85 −9.458 58.333 −3.148 1.00 22.06 ATOM 597 CD1 PHE 85 −8.978 59.084 −4.220 1.00 22.74 ATOM 598 CD2 PHE 85 −10.694 58.658 −2.598 1.00 17.88 ATOM 599 GE1 PHE 85 −9.723 60.139 −4.738 1.00 18.93 ATOM 600 CE2 PHE 85 −11.443 59.703 −3.106 1.00 15.03 ATOM 601 CZ PHE 85 −10.959 60.445 −4.178 1.00 17.54 ATOM 602 C PHE 85 −7.887 54.819 −3.043 1.00 25.51 ATOM 603 O PHE 85 −8.044 54.032 −2.096 1.00 25.66 ATOM 604 N LEU 86 −6.805 54.818 −3.814 1.00 24.59 ATOM 605 CA LEU 86 −5.707 53.905 −3.579 1.00 23.48 ATOM 606 CB LEU 86 −5.006 53.591 −4.891 1.00 21.27 ATOM 607 CG LEU 86 −5.915 52.794 −5.824 1.00 21.04 ATOM 608 CD1 LEU 86 −5.175 52.438 −7.087 1.00 19.70 ATOM 609 CD2 LEU 86 −6.395 51.541 −5.105 1.00 19.85 ATOM 610 C LEU 86 −4.750 54.566 −2.614 1.00 25.62 ATOM 611 O LEU 86 −4.183 55.615 −2.925 1.00 25.42 ATOM 612 N GLU 87 −4.594 53.963 −1.436 1.00 26.44 ATOM 613 CA GLU 87 −3.709 54.504 −0.412 1.00 28.40 ATOM 614 CB GLU 87 −4.317 54.301 0.985 1.00 27.98 ATOM 615 CG GLU 87 −3.463 54.875 2.145 1.00 26.64 ATOM 616 CD GLU 87 −4.014 54.511 3.515 1.00 23.94 ATOM 617 OE1 GLU 87 −4.073 53.307 3.829 1.00 27.96 ATOM 618 OE2 GLU 87 −4.398 55.416 4.281 1.00 21.92 ATOM 619 C GLU 87 −2.330 53.860 −0.465 1.00 28.13 ATOM 620 O GLU 87 −2.203 52.640 −0.421 1.00 30.05 ATOM 621 N ARG 88 −1.296 54.681 −0.571 1.00 27.67 ATOM 622 CA ARG 88 0.050 54.147 −0.598 1.00 31.22 ATOM 623 CB ARG 88 0.628 54.133 −2.018 1.00 34.68 ATOM 624 CG ARG 88 1.956 53.371 −2.084 1.00 41.67 ATOM 625 CD ARG 88 2.837 53.733 −3.277 1.00 45.98 ATOM 626 NE ARG 88 4.232 53.379 −3.000 1.00 51.46 ATOM 627 CZ ARG 88 5.283 53.843 −3.676 1.00 54.59 ATOM 628 NH1 ARG 88 5.107 54.689 −4.689 1.00 55.27 ATOM 629 NH2 ARG 88 6.513 53.476 −3.326 1.00 52.53 ATOM 630 C ARG 88 0.976 54.949 0.303 1.00 30.54 ATOM 631 O ARG 88 1.063 56.180 0.195 1.00 30.76 ATOM 632 N LEU 89 1.650 54.239 1.204 1.00 27.05 ATOM 633 CA LEU 89 2.604 54.857 2.108 1.00 25.80 ATOM 634 CB LEU 89 2.762 54.006 3.374 1.00 26.00 ATOM 635 CG LEU 89 3.853 54.360 4.399 1.00 25.93 ATOM 636 CD1 LEU 89 4.031 55.866 4.547 1.00 24.56 ATOM 637 CD2 LEU 89 3.474 53.740 5.727 1.00 26.66 ATOM 638 C LEU 89 3.918 54.929 1.343 1.00 22.78 ATOM 639 O LEU 89 4.587 53.927 1.166 1.00 23.03 ATOM 640 N GLU 90 4.278 56.118 0.883 1.00 23.05 ATOM 641 CA GLU 90 5.501 56.296 0.114 1.00 25.74 ATOM 642 CB GLU 90 5.505 57.670 −0.559 1.00 26.96 ATOM 643 CG GLU 90 4.231 58.018 −1.346 1.00 30.37 ATOM 644 CD GLU 90 3.883 56.999 −2.421 1.00 30.68 ATOM 645 OE1 GLU 90 4.736 56.728 −3.292 1.00 32.66 ATOM 646 OE2 GLU 90 2.750 56.475 −2.396 1.00 31.43 ATOM 647 C GLU 90 6.804 56.128 0.901 1.00 27.47 ATOM 648 O GLU 90 6.842 56.149 2.137 1.00 26.96 ATOM 649 N GLU 91 7.880 55.961 0.153 1.00 28.46 ATOM 650 CA GLU 91 9.197 55.802 0.733 1.00 30.58 ATOM 651 CB GLU 91 10.204 55.557 −0.388 1.00 36.00 ATOM 652 CG GLU 91 9.820 54.367 −1.251 1.00 44.17 ATOM 653 CD GLU 91 10.713 54.198 −2.463 1.00 49.46 ATOM 654 OE1 GLU 91 10.435 53.284 −3.277 1.00 50.63 ATOM 655 OE2 GLU 91 11.687 54.977 −2.601 1.00 52.77 ATOM 656 C GLU 91 9.573 57.040 1.542 1.00 27.34 ATOM 657 O GLU 91 10.241 56.941 2.567 1.00 28.42 ATOM 658 N ASN 92 9.132 58.202 1.079 1.00 24.91 ATOM 659 CA ASN 92 9.405 59.460 1.757 1.00 22.31 ATOM 660 CB ASN 92 9.064 60.616 0.840 1.00 20.97 ATOM 661 CG ASN 92 7.571 60.779 0.650 1.00 23.29 ATOM 662 OD1 ASN 92 6.778 59.874 0.965 1.00 22.87 ATOM 663 ND2 ASN 92 7.171 61.935 0.130 1.00 21.91 ATOM 664 C ASN 92 8.558 59.551 3.027 1.00 23.86 ATOM 665 O ASN 92 8.481 60.600 3.666 1.00 25.03 ATOM 666 N HIS 93 7.899 58.447 3.358 1.00 23.09 ATOM 667 CA HIS 93 7.086 58.339 4.559 1.00 22.39 ATOM 668 GB HIS 93 7.945 58.601 5.793 1.00 23.17 ATOM 669 CG HIS 93 8.847 57.461 6.137 1.00 26.20 ATOM 670 CD2 HIS 93 9.770 57.312 7.114 1.00 30.14 ATOM 671 ND1 HIS 93 8.841 56.276 5.432 1.00 29.43 ATOM 672 GE1 HIS 93 9.723 55.446 5.959 1.00 28.79 ATOM 673 NE2 HIS 93 10.301 56.049 6.982 1.00 30.20 ATOM 674 C HIS 93 5.825 59.166 4.612 1.00 22.28 ATOM 675 O HIS 93 5.259 59.406 5.688 1.00 20.33 ATOM 676 N TYR 94 5.372 59.585 3.440 1.00 22.58 ATOM 677 CA TYR 94 4.141 60.348 3.345 1.00 20.96 ATOM 678 GB TYR 94 4.348 61.593 2.489 1.00 18.29 ATOM 679 CG TYR 94 4.940 62.749 3.243 1.00 16.89 ATOM 680 CD1 TYR 94 4.159 63.484 4.136 1.00 17.65 ATOM 681 CE1 TYR 94 4.707 64.543 4.861 1.00 16.95 ATOM 682 CD2 TYR 94 6.293 63.098 3.090 1.00 13.56 ATOM 683 CE2 TYR 94 6.849 64.146 3.808 1.00 10.87 ATOM 684 CZ TYR 94 6.048 64.863 4.691 1.00 13.37 ATOM 685 OH TYR 94 6.555 65.916 5.399 1.00 15.56 ATOM 686 C TYR 94 3.125 59.438 2.682 1.00 21.15 ATOM 687 O TYR 94 3.482 58.394 2.130 1.00 18.49 ATOM 688 N ASN 95 1.859 59.827 2.757 1.00 20.46 ATOM 689 CA ASN 95 0.801 59.067 2.119 1.00 20.78 ATOM 690 GB ASN 95 −0.413 58.915 3.033 1.00 18.65 ATOM 691 CG ASN 95 −0.316 57.709 3.915 1.00 22.19 ATOM 692 OD1 ASN 95 0.564 56.848 3.716 1.00 22.07 ATOM 693 ND2 ASN 95 −1.225 57.616 4.899 1.00 13.47 ATOM 694 C ASN 95 0.345 59.806 0.880 1.00 22.07 ATOM 695 O ASN 95 0.415 61.040 0.806 1.00 24.43 ATOM 696 N THR 96 −0.104 59.050 −0.107 1.00 19.08 ATOM 697 CA THR 96 −0.648 59.654 −1.301 1.00 17.85 ATOM 698 GB THR 96 0.293 59.564 −2.494 1.00 13.90 ATOM 699 OG1 THR 96 0.627 58.194 −2.733 1.00 16.54 ATOM 700 CG2 THR 96 1.534 60.388 −2.245 1.00 8.64 ATOM 701 C THR 96 −1.905 58.870 −1.604 1.00 19.75 ATOM 702 O THR 96 −1.952 57.656 −1.398 1.00 19.27 ATOM 703 N TYR 97 −2.931 59.573 −2.065 1.00 21.57 ATOM 704 CA TYR 97 −4.188 58.932 −2.400 1.00 23.58 ATOM 705 GB TYR 97 −5.283 59.469 −1.485 1.00 23.44 ATOM 706 CG TYR 97 −5.031 59.152 −0.029 1.00 25.02 ATOM 707 CD1 TYR 97 −5.403 57.918 0.511 1.00 26.72 ATOM 708 GE1 TYR 97 −5.157 57.610 1.851 1.00 25.40 ATOM 709 CD2 TYR 97 −4.399 60.076 0.810 1.00 24.77 ATOM 710 CE2 TYR 97 −4.149 59.781 2.145 1.00 23.43 ATOM 711 CZ TYR 97 −4.532 58.547 2.660 1.00 25.51 ATOM 712 OH TYR 97 −4.299 58.253 3.984 1.00 25.72 ATOM 713 C TYR 97 −4.521 59.184 −3.871 1.00 25.49 ATOM 714 O TYR 97 −4.761 60.322 −4.281 1.00 26.61 ATOM 715 N ILE 98 −4.501 58.116 −4.662 1.00 26.27 ATOM 716 GA ILE 98 −4.807 58.199 −6.083 1.00 25.07 ATOM 717 GB ILE 98 −3.864 57.292 −6.913 1.00 26.82 ATOM 718 CG2 ILE 98 −4.420 57.106 −8.333 1.00 26.59 ATOM 719 CG1 ILE 98 −2.457 57.905 −6.933 1.00 29.67 ATOM 720 CD1 ILE 98 −1.412 57.093 −7.682 1.00 29.38 ATOM 721 C ILE 98 −6.239 57.757 −6.333 1.00 24.20 ATOM 722 O ILE 98 −6.703 56.784 −5.739 1.00 21.30 ATOM 723 N SER 99 −6.934 58.485 −7.205 1.00 25.81 ATOM 724 CA SER 99 −8.312 58.143 −7.564 1.00 25.53 ATOM 725 GB SER 99 −8.845 59.082 −8.644 1.00 24.28 ATOM 726 OG SER 99 −9.827 58.425 −9.419 1.00 25.10 ATOM 727 C SER 99 −8.310 56.729 −8.115 1.00 26.04 ATOM 728 O SER 99 −7.602 56.432 −9.084 1.00 23.70 ATOM 729 N LYS 100 −9.101 55.863 −7.491 1.00 27.88 ATOM 730 CA LYS 100 −9.195 54.468 −7.903 1.00 27.72 ATOM 731 CB LYS 100 −10.045 53.687 −6.897 1.00 26.37 ATOM 732 CG LYS 100 −9.848 52.176 −6.908 1.00 25.42 ATOM 733 CD LYS 100 −10.364 51.544 −8.171 1.00 23.12 ATOM 734 CE LYS 100 −10.292 50.028 −8.091 1.00 26.78 ATOM 735 NZ LYS 100 −11.136 49.473 −6.995 1.00 27.99 ATOM 736 C LYS 100 −9.809 54.391 −9.293 1.00 28.12 ATOM 737 O LYS 100 −9.402 53.571 −10.113 1.00 27.55 ATOM 738 N LYS 101 −10.777 55.264 −9.552 1.00 30.25 ATOM 739 CA LYS 101 −11.454 55.297 −10.840 1.00 34.17 ATOM 740 CE LYS 101 −12.770 56.070 −10.720 1.00 36.86 ATOM 741 CG LYS 101 −13.554 56.186 −12.025 1.00 37.77 ATOM 742 CD LYS 101 −14.802 57.027 −11.843 1.00 38.43 ATOM 743 CE LYS 101 −15.534 57.241 −13.161 1.00 39.99 ATOM 744 NZ LYS 101 −16.726 58.124 −12.996 1.00 39.40 ATOM 745 C LYS 101 −10.604 55.923 −11.943 1.00 34.72 ATOM 746 O LYS 101 −10.696 55.536 −13.102 1.00 35.47 ATOM 747 N HIS 102 −9.780 56.895 −11.591 1.00 34.55 ATOM 748 CA HIS 102 −8.955 57.543 −12.596 1.00 36.40 ATOM 749 CB HIS 102 −9.241 59.048 −12.584 1.00 40.56 ATOM 750 CG HIS 102 −10.628 59.392 −13.040 1.00 44.63 ATOM 751 CD2 HIS 102 −11.758 59.655 −12.340 1.00 45.60 ATOM 752 NO1 HIS 102 −10.983 59.438 −14.372 1.00 47.62 ATOM 753 CE1 HIS 102 −12.272 59.715 −14.472 1.00 49.39 ATOM 754 NE2 HIS 102 −12.766 59.851 −13.253 1.00 48.16 ATOM 755 C HIS 102 −7.471 57.249 −12.393 1.00 35.09 ATOM 756 O HIS 102 −6.604 58.097 −12.635 1.00 30.28 ATOM 757 N ALA 103 −7.198 56.019 −11.962 1.00 35.43 ATOM 758 CA ALA 103 −5.842 55.561 −11.705 1.00 37.35 ATOM 759 CE ALA 103 −5.871 54.138 −11.211 1.00 34.67 ATOM 760 C ALA 103 −4.948 55.666 −12.934 1.00 39.11 ATOM 761 O ALA 103 −3.886 56.287 −12.887 1.00 41.02 ATOM 762 N GLU 104 −5.382 55.046 −14.025 1.00 40.77 ATOM 763 CA GLU 104 −4.641 55.059 −15.282 1.00 40.86 ATOM 764 CE GLU 104 −5.591 54.695 −16.422 1.00 43.20 ATOM 765 CG GLU 104 −5.130 55.168 −17.787 1.00 49.96 ATOM 766 CD GLU 104 −6.293 55.507 −18.713 1.00 52.78 ATOM 767 OE1 GLU 104 −6.045 56.087 −19.796 1.00 52.63 ATOM 768 OE2 GLU 104 −7.453 55.194 −18.357 1.00 53.57 ATOM 769 C GLU 104 −3.971 56.408 −15.569 1.00 39.23 ATOM 770 O GLU 104 −2.804 56.462 −15.944 1.00 38.66 ATOM 771 N LYS 105 −4.714 57.493 −15.390 1.00 39.54 ATOM 772 CA LYS 105 −4.192 58.833 −15.641 1.00 38.83 ATOM 773 CE LYS 105 −5.345 59.814 −15.842 1.00 35.41 ATOM 774 CG LYS 105 −6.562 59.186 −16.484 1.00 34.90 ATOM 775 CD LYS 105 −7.832 59.953 −16.147 1.00 36.61 ATOM 776 CE LYS 105 −9.058 59.174 −16.584 1.00 37.07 ATOM 777 NZ LYS 105 −8.974 57.765 −16.092 1.00 38.64 ATOM 778 C LYS 105 −3.340 59.314 −14.473 1.00 39.73 ATOM 779 O LYS 105 −2.691 60.350 −14.564 1.00 42.17 ATOM 780 N ASN 106 −3.345 58.568 −13.375 1.00 39.76 ATOM 781 CA ASN 106 −2.586 58.962 −12.194 1.00 41.17 ATOM 782 CB ASN 106 −1.099 59.080 −12.538 1.00 41.89 ATOM 783 CG ASN 106 −0.386 57.741 −12.474 1.00 45.65 ATOM 784 OD1 ASN 106 0.626 57.531 −13.143 1.00 48.02 ATOM 785 ND2 ASN 106 −0.908 56.827 −11.653 1.00 44.93 ATOM 786 C ASN 106 −3.117 60.279 −11.625 1.00 39.74 ATOM 787 O ASN 106 −2.413 61.281 −11.557 1.00 39.43 ATOM 788 N TRP 107 −4.379 60.254 −11.222 1.00 39.27 ATOM 789 CA TRP 107 −5.051 61.412 −10.651 1.00 39.02 ATOM 790 CB TRP 107 −6.515 61.410 −11.096 1.00 42.22 ATOM 791 CG TRP 107 −6.733 62.007 −12.451 1.00 45.87 ATOM 792 CD2 TRP 107 −7.984 62.429 −13.008 1.00 47.87 ATOM 793 CE2 TRP 107 −7.713 62.964 −14.286 1.00 48.19 ATOM 794 CE3 TRP 107 −9.311 62.407 −12.549 1.00 46.97 ATOM 795 CD1 TRP 107 −5.782 62.290 −13.391 1.00 45.43 ATOM 796 NE1 TRP 107 −6.362 62.869 −14.494 1.00 45.12 ATOM 797 CZ2 TRP 107 −8.723 63.475 −15.113 1.00 49.27 ATOM 798 CZ3 TRP 107 −10.313 62.916 −13.370 1.00 46.53 ATOM 799 CH2 TRP 107 −10.012 63.442 −14.638 1.00 47.09 ATOM 800 C TRP 107 −4.958 61.385 −9.123 1.00 36.02 ATOM 801 O TRP 107 −5.563 60.537 −8.466 1.00 32.66 ATOM 802 N PHE 108 −4.205 62.322 −8.560 1.00 33.43 ATOM 803 CA PHE 108 −4.021 62.364 −7.118 1.00 29.53 ATOM 804 GB PHE 108 −2.617 62.854 −6.747 1.00 25.07 ATOM 805 CG PHE 108 −1.501 62.011 −7.278 1.00 24.26 ATOM 806 CO1 PHE 108 −0.959 62.263 −8.544 1.00 20.53 ATOM 807 CO2 PHE 108 −0.965 60.982 −6.502 1.00 23.65 ATOM 808 GE1 PHE 108 0.098 61.511 −9.030 1.00 19.10 ATOM 809 CE2 PHE 108 0.098 60.215 −6.977 1.00 23.67 ATOM 810 CZ PHE 108 0.632 60.481 −8.248 1.00 24.38 ATOM 811 C PHE 108 −4.990 63.268 −6.394 1.00 29.53 ATOM 812 O PHE 108 −5.611 64.150 −6.991 1.00 28.70 ATOM 813 N VAL 109 −5.095 63.021 −5.087 1.00 28.71 ATOM 814 CA VAL 109 −5.885 63.833 −4.181 1.00 28.24 ATOM 815 GB VAL 109 −6.384 63.036 −2.966 1.00 28.28 ATOM 816 CG1 VAL 109 −6.582 63.972 −1.794 1.00 28.81 ATOM 817 CG2 VAL 109 −7.703 62.347 −3.289 1.00 29.67 ATOM 818 C VAL 109 −4.791 64.776 −3.712 1.00 28.77 ATOM 819 O VAL 109 −3.783 64.334 −3.162 1.00 30.15 ATOM 820 N GLY 110 −4.957 66.065 −3.959 1.00 28.53 ATOM 821 CA GLY 110 −3.926 66.997 −3.552 1.00 27.81 ATOM 822 C GLY 110 −4.525 68.296 −3.079 1.00 27.32 ATOM 823 O GLY 110 −5.745 68.448 −3.043 1.00 27.33 ATOM 824 N LEU 111 −3.667 69.237 −2.711 1.00 25.62 ATOM 825 CA LEU 111 −4.128 70.530 −2.246 1.00 25.47 ATOM 826 GB LEU 111 −4.374 70.482 −0.738 1.00 25.49 ATOM 827 CG LEU 111 −5.595 69.678 −0.277 1.00 25.80 ATOM 828 CD1 LEU 111 −5.407 69.184 1.157 1.00 21.96 ATOM 829 CD2 LEU 111 −6.845 70.561 −0.400 1.00 24.98 ATOM 830 C LEU 111 −3.069 71.556 −2.601 1.00 26.94 ATOM 831 O LEU 111 −1.868 71.270 −2.575 1.00 25.36 ATOM 832 N LYS 112 −3.519 72.757 −2.938 1.00 29.56 ATOM 833 CA LYS 112 −2.613 73.825 −3.335 1.00 31.20 ATOM 834 GB LYS 112 −3.305 74.708 −4.370 1.00 34.94 ATOM 835 CG LYS 112 −3.551 74.027 −5.697 1.00 35.87 ATOM 836 CD LYS 112 −4.189 74.997 −6.675 1.00 39.81 ATOM 837 CE LYS 112 −3.450 75.001 −8.006 1.00 43.47 ATOM 838 NZ LYS 112 −4.076 75.931 −8.996 1.00 46.95 ATOM 839 C LYS 112 −2.091 74.695 −2.190 1.00 29.91 ATOM 840 O LYS 112 −2.672 74.727 −1.111 1.00 27.10 ATOM 841 N LYS 113 −0.996 75.405 −2.456 1.00 29.29 ATOM 842 CA LYS 113 −0.371 76.294 −1.485 1.00 31.65 ATOM 843 GB LYS 113 0.510 77.311 −2.198 1.00 33.37 ATOM 844 CG LYS 113 1.824 76.744 −2.686 1.00 37.28 ATOM 845 CD LYS 113 2.788 76.487 −1.544 1.00 37.50 ATOM 846 CE LYS 113 3.602 75.225 −1.785 1.00 39.66 ATOM 847 NZ LYS 113 4.235 75.174 −3.133 1.00 40.46 ATOM 848 C LYS 113 −1.354 77.040 −0.599 1.00 32.81 ATOM 849 O LYS 113 −1.047 77.354 0.544 1.00 34.94 ATOM 850 N ASN 114 −2.537 77.330 −1.115 1.00 34.59 ATOM 851 CA ASN 114 −3.525 78.046 −0.324 1.00 34.22 ATOM 852 CD ASN 114 −4.133 79.187 −1.136 1.00 36.34 ATOM 853 CG ASN 114 −4.910 78.691 −2.328 1.00 36.23 ATOM 854 OD1 ASN 114 −5.778 77.836 −2.196 1.00 36.00 ATOM 855 ND2 ASN 114 −4.603 79.225 −3.501 1.00 37.05 ATOM 856 C ASN 114 −4.636 77.133 0.168 1.00 33.79 ATOM 857 O ASN 114 −5.635 77.608 0.701 1.00 36.07 ATOM 858 N GLY 115 −4.480 75.830 −0.037 1.00 32.03 ATOM 859 CA GLY 115 −5.474 74.885 0.444 1.00 34.61 ATOM 860 C GLY 115 −6.698 74.667 −0.417 1.00 35.87 ATOM 861 O GLY 115 −7.632 73.962 −0.035 1.00 34.51 ATOM 862 N SER 116 −6.700 75.280 −1.586 1.00 38.93 ATOM 863 CA SER 116 −7.817 75.128 −2.489 1.00 39.18 ATOM 864 CB SER 116 −7.872 76.303 −3.462 1.00 38.46 ATOM 865 OG SER 116 −8.902 76.120 −4.408 1.00 39.70 ATOM 866 C SER 116 −7.651 73.826 −3.251 1.00 40.32 ATOM 867 O SER 116 −6.532 73.399 −3.542 1.00 39.78 ATOM 868 N CYS 117 −8.785 73.201 −3.549 1.00 42.63 ATOM 869 CA CYS 117 −8.829 71.951 −4.290 1.00 44.43 ATOM 870 CB CYS 117 −10.261 71.738 −4.788 1.00 42.26 ATOM 871 SG CYS 117 −10.434 70.534 −6.094 1.00 42.90 ATOM 872 C CYS 117 −7.856 71.988 −5.476 1.00 46.45 ATOM 873 O CYS 117 −7.838 72.964 −6.223 1.00 49.26 ATOM 874 N LYS 118 −7.030 70.956 −5.638 1.00 46.83 ATOM 875 CA LYS 118 −6.104 70.920 −6.777 1.00 48.07 ATOM 876 CB LYS 118 −4.665 70.620 −6.320 1.00 47.48 ATOM 877 CG LYS 118 −3.660 70.503 −7.480 1.00 46.98 ATOM 878 CD LYS 118 −2.286 71.111 −7.147 1.00 47.17 ATOM 879 CE LYS 118 −1.352 71.100 −8.376 1.00 47.11 ATOM 880 NZ LYS 118 −0.079 71.867 −8.193 1.00 41.89 ATOM 881 C LYS 118 −6.561 69.880 −7.808 1.00 48.93 ATOM 882 O LYS 118 −6.445 68.677 −7.587 1.00 49.49 ATOM 883 N ARG 119 −7.091 70.361 −8.929 1.00 49.25 ATOM 884 CA ARG 119 −7.585 69.507 −10.001 1.00 47.75 ATOM 885 CD ARG 119 −7.671 70.302 −11.303 1.00 50.94 ATOM 886 CG ARG 119 −8.068 71.764 −11.113 1.00 56.67 ATOM 887 CD ARC 119 −8.327 72.459 −12.449 1.00 59.61 ATOM 888 NE ARC 119 −9.407 71.804 −13.182 1.00 60.94 ATOM 889 CZ ARC 119 −9.241 71.117 −14.308 1.00 61.86 ATOM 890 NH1 ARG 119 −8.031 71.000 −14.844 1.00 63.34 ATOM 891 NH2 ARC 119 −10.283 70.533 −14.887 1.00 60.50 ATOM 892 C ARC 119 −6.686 68.298 −10.209 1.00 47.41 ATOM 893 O ARC 119 −5.503 68.437 −10.504 1.00 46.81 ATOM 894 N GLY 120 −7.257 67.110 −10.056 1.00 47.81 ATOM 895 CA GLY 120 −6.497 65.886 −10.236 1.00 48.33 ATOM 896 C GLY 120 −5.611 65.830 −11.472 1.00 49.08 ATOM 897 O GLY 120 −4.489 65.339 −11.387 1.00 49.07 ATOM 898 N PRO 121 −6.071 66.313 −12.637 1.00 49.33 ATOM 899 CD PRO 121 −7.404 66.837 −12.974 1.00 48.84 ATOM 900 CA PRO 121 −5.233 66.267 −13.836 1.00 49.58 ATOM 901 CB PRO 121 −6.214 66.603 −14.945 1.00 48.50 ATOM 902 CC PRO 121 −7.131 67.551 −14.270 1.00 48.21 ATOM 903 C PRO 121 −4.032 67.209 −13.828 1.00 50.68 ATOM 904 O PRO 121 −3.309 67.285 −14.820 1.00 51.26 ATOM 905 N ARC 122 −3.821 67.927 −12.727 1.00 51.69 ATOM 906 CA ARG 122 −2.681 68.847 −12.629 1.00 51.88 ATOM 907 CB ARC 122 −3.148 70.286 −12.367 1.00 56.07 ATOM 908 CC ARC 122 −4.602 70.587 −12.723 1.00 61.69 ATOM 909 CD ARC 122 −4.904 70.420 −14.211 1.00 67.71 ATOM 910 NE ARC 122 −4.299 71.449 −15.057 1.00 70.79 ATOM 911 CZ ARG 122 −4.503 71.547 −16.370 1.00 73.15 ATOM 912 NH1 ARG 122 −5.298 70.679 −16.992 1.00 73.19 ATOM 913 NH2 ARG 122 −3.912 72.509 −17.066 1.00 74.22 ATOM 914 C ARG 122 −1.748 68.408 −11.492 1.00 50.05 ATOM 915 O ARG 122 −0.853 69.153 −11.079 1.00 47.68 ATOM 916 N THR 123 −1.974 67.194 −10.995 1.00 47.61 ATOM 917 CA THR 123 −1.172 66.638 −9.919 1.00 45.19 ATOM 918 GB THR 123 −2.054 65.882 −8.914 1.00 40.61 ATOM 919 OG1 THR 123 −2.418 64.611 −9.453 1.00 34.32 ATOM 920 CG2 THR 123 −3.318 66.672 −8.630 1.00 38.47 ATOM 921 C THR 123 −0.106 65.687 −10.470 1.00 48.36 ATOM 922 O THR 123 −0.403 64.783 −11.258 1.00 49.22 ATOM 923 N HIS 124 1.136 65.899 −10.043 1.00 51.15 ATOM 924 CA HIS 124 2.269 65.091 −10.485 1.00 52.99 ATOM 925 GB HIS 124 3.333 66.001 −11.121 1.00 57.19 ATOM 926 CG HIS 124 4.480 65.262 −11.739 1.00 61.62 ATOM 927 CD2 HIS 124 4.886 65.165 −13.029 1.00 64.23 ATOM 928 ND1 HIS 124 5.363 64.501 −11.003 1.00 64.57 ATOM 929 CE1 HIS 124 6.262 63.965 −11.811 1.00 64.97 ATOM 930 NE2 HIS 124 5.994 64.354 −13.046 1.00 66.03 ATOM 931 C HIS 124 2.883 64.314 −9.324 1.00 53.02 ATOM 932 O HIS 124 2.746 64.698 −8.162 1.00 52.95 ATOM 933 N TYR 125 3.562 63.219 −9.658 1.00 53.83 ATOM 934 CA TYR 125 4.221 62.369 −8.676 1.00 53.98 ATOM 935 CB TYR 125 4.996 61.262 −9.387 1.00 59.15 ATOM 936 CG TYR 125 5.894 60.463 −8.469 1.00 66.50 ATOM 937 CD1 TYR 125 5.358 59.606 −7.496 1.00 69.66 ATOM 938 GE1 TYR 125 6.193 58.878 −6.629 1.00 72.55 ATOM 939 CD2 TYR 125 7.284 60.576 −8.557 1.00 69.56 ATOM 940 CE2 TYR 125 8.128 59.856 −7.698 1.00 72.02 ATOM 941 CZ TYR 125 7.579 59.011 −6.740 1.00 73.15 ATOM 942 OH TYR 125 8.417 58.301 −5.906 1.00 73.04 ATOM 943 C TYR 125 5.178 63.134 −7.765 1.00 52.11 ATOM 944 O TYR 125 5.307 62.812 −6.583 1.00 53.02 ATOM 945 N GLY 126 5.844 64.147 −8.306 1.00 48.32 ATOM 946 CA GLY 126 6.793 64.901 −7.507 1.00 44.37 ATOM 947 C GLY 126 6.261 66.128 −6.790 1.00 42.58 ATOM 948 O GLY 126 7.041 66.958 −6.313 1.00 41.62 ATOM 949 N GLN 127 4.944 66.249 −6.688 1.00 39.00 ATOM 950 CA GLN 127 4.369 67.411 −6.031 1.00 35.99 ATOM 951 GB GLN 127 3.023 67.747 −6.678 1.00 36.59 ATOM 952 CG GLN 127 3.098 67.961 −8.183 1.00 36.01 ATOM 953 CD GLN 127 1.862 68.646 −8.737 1.00 37.86 ATOM 954 OE1 GLN 127 0.737 68.196 −8.512 1.00 39.21 ATOM 955 NE2 GLN 127 2.066 69.742 −9.468 1.00 39.34 ATOM 956 C GLN 127 4.205 67.283 −4.512 1.00 33.73 ATOM 957 O GLN 127 4.070 66.184 −3.970 1.00 32.12 ATOM 958 N LYS 128 4.238 68.426 −3.833 1.00 31.42 ATOM 959 CA LYS 128 4.074 68.478 −2.388 1.00 30.39 ATOM 960 GB LYS 128 4.706 69.754 −1.821 1.00 32.97 ATOM 961 CG LYS 128 6.187 69.665 −1.469 1.00 35.91 ATOM 962 CD LYS 128 6.748 71.060 −1.135 1.00 39.16 ATOM 963 CE LYS 128 7.544 71.085 0.170 1.00 38.59 ATOM 964 NZ LYS 128 6.677 70.905 1.383 1.00 36.98 ATOM 965 C LYS 128 2.578 68.508 −2.132 1.00 28.93 ATOM 966 O LYS 128 2.105 68.196 −1.039 1.00 27.14 ATOM 967 N ALA 129 1.835 68.889 −3.161 1.00 27.52 ATOM 968 CA ALA 129 0.388 68.980 −3.061 1.00 28.25 ATOM 969 GB ALA 129 −0.173 69.620 −4.320 1.00 27.44 ATOM 970 C ALA 129 −0.299 67.638 −2.812 1.00 27.33 ATOM 971 O ALA 129 −1.341 67.591 −2.156 1.00 25.70 ATOM 972 N ILE 130 0.276 66.551 −3.329 1.00 26.39 ATOM 973 CA ILE 130 −0.331 65.230 −3.154 1.00 26.25 ATOM 974 CB ILE 130 −0.166 64.360 −4.425 1.00 24.09 ATOM 975 CG2 ILE 130 −0.764 65.075 −5.617 1.00 24.03 ATOM 976 CG1 ILE 130 1.308 64.069 −4.685 1.00 21.11 ATOM 977 CD1 ILE 130 1.535 63.077 −5.810 1.00 16.42 ATOM 978 C ILE 130 0.172 64.435 −1.948 1.00 25.50 ATOM 979 O ILE 130 −0.242 63.295 −1.736 1.00 28.33 ATOM 980 N LEU 131 1.054 65.039 −1.159 1.00 23.92 ATOM 981 CA LEU 131 1.608 64.389 0.023 1.00 19.80 ATOM 982 CB LEU 131 3.050 64.848 0.248 1.00 15.70 ATOM 983 CG LEU 131 4.031 64.395 −0.838 1.00 13.31 ATOM 984 CD1 LEU 131 5.388 65.061 −0.640 1.00 12.10 ATOM 985 CD2 LEU 131 4.163 62.885 −0.791 1.00 7.44 ATOM 986 C LEU 131 0.765 64.675 1.257 1.00 20.49 ATOM 987 O LEU 131 0.506 65.834 1.609 1.00 20.71 ATOM 988 N PHE 132 0.337 63.605 1.915 1.00 20.52 ATOM 989 CA PHE 132 −0.495 63.726 3.103 1.00 21.43 ATOM 990 GB PHE 132 −1.909 63.210 2.803 1.00 23.94 ATOM 991 CG PHE 132 −2.707 64.124 1.914 1.00 28.64 ATOM 992 CD1 PHE 132 −3.445 65.175 2.459 1.00 28.95 ATOM 993 CD2 PHE 132 −2.676 63.971 0.529 1.00 29.70 ATOM 994 GE1 PHE 132 −4.135 66.060 1.636 1.00 30.99 ATOM 995 CE2 PHE 132 −3.360 64.853 −0.306 1.00 30.81 ATOM 996 CZ PHE 132 −4.092 65.899 0.245 1.00 32.10 ATOM 997 C PHE 132 0.084 62.989 4.299 1.00 20.23 ATOM 998 O PHE 132 0.827 62.026 4.157 1.00 21.47 ATOM 999 N LEU 133 −0.288 63.444 5.483 1.00 18.17 ATOM 1000 CA LEU 133 0.198 62.854 6.703 1.00 18.68 ATOM 1001 GB LEU 133 1.212 63.809 7.323 1.00 20.20 ATOM 1002 CG LEU 133 2.279 63.282 8.266 1.00 20.39 ATOM 1003 CD1 LEU 133 3.062 62.191 7.582 1.00 16.71 ATOM 1004 CD2 LEU 133 3.202 64.429 8.661 1.00 21.39 ATOM 1005 C LEU 133 −0.974 62.635 7.651 1.00 20.10 ATOM 1006 O LEU 133 −1.768 63.550 7.878 1.00 19.72 ATOM 1007 N PRO 134 −1.121 61.411 8.196 1.00 21.14 ATOM 1008 CD PRO 134 −0.513 60.153 7.733 1.00 20.54 ATOM 1009 CA PRO 134 −2.226 61.133 9.125 1.00 21.38 ATOM 1010 CB PRO 134 −2.287 59.606 9.153 1.00 17.91 ATOM 1011 CG PRO 134 −1.654 59.200 7.863 1.00 19.11 ATOM 1012 C PRO 134 −1.902 61.710 10.508 1.00 21.87 ATOM 1013 O PRO 134 −0.785 61.575 10.990 1.00 22.43 ATOM 1014 N LEU 135 −2.866 62.369 11.138 1.00 22.87 ATOM 1015 CA LEU 135 −2.634 62.926 12.466 1.00 21.38 ATOM 1016 GB LEU 135 −2.405 64.438 12.426 1.00 17.99 ATOM 1017 CG LEU 135 −1.223 65.052 11.672 1.00 16.42 ATOM 1018 GD1 LEU 135 −0.994 66.466 12.186 1.00 9.72 ATOM 1019 CD2 LEU 135 0.019 64.227 11.873 1.00 12.39 ATOM 1020 C LEU 135 −3.828 62.670 13.349 1.00 22.74 ATOM 1021 O LEU 135 −4.952 62.557 12.863 1.00 23.73 ATOM 1022 N PRO 136 −3.596 62.560 14.669 1.00 26.01 ATOM 1023 CD PRO 136 −2.263 62.410 15.279 1.00 25.14 ATOM 1024 CA PRO 136 −4.650 62.322 15.667 1.00 25.96 ATOM 1025 GB PRO 136 −3.860 62.059 16.944 1.00 26.54 ATOM 1026 CG PRO 136 −2.559 61.505 16.437 1.00 25.10 ATOM 1027 C PRO 136 −5.468 63.601 15.757 1.00 26.58 ATOM 1028 O PRO 136 −4.971 64.678 15.449 1.00 28.99 ATOM 1029 N VAL 137 −6.713 63.509 16.187 1.00 27.68 ATOM 1030 CA VAL 137 −7.523 64.717 16.244 1.00 27.15 ATOM 1031 GB VAL 137 −8.908 64.423 16.818 1.00 24.53 ATOM 1032 CG1 VAL 137 −9.665 65.719 17.015 1.00 26.11 ATOM 1033 CG2 VAL 137 −9.676 63.502 15.863 1.00 23.43 ATOM 1034 C VAL 137 −6.877 65.846 17.039 1.00 29.13 ATOM 1035 O VAL 137 −6.850 66.998 16.581 1.00 26.88 ATOM 1036 N SER 138 −6.350 65.502 18.218 1.00 32.45 ATOM 1037 CA SER 138 −5.708 66.464 19.128 1.00 32.31 ATOM 1038 CB SER 138 −6.133 66.176 20.575 1.00 30.03 ATOM 1039 C SER 138 −4.180 66.494 19.043 1.00 31.29 ATOM 1040 O SER 138 −3.602 67.477 19.570 1.00 30.54 ATOM 1041 GB TYR 1008 12.631 46.833 26.062 1.00 31.16 ATOM 1042 CG TYR 1008 13.713 47.571 25.287 1.00 30.94 ATOM 1043 CD1 TYR 1008 15.010 47.693 25.793 1.00 27.23 ATOM 1044 GE1 TYR 1008 15.977 48.436 25.124 1.00 25.79 ATOM 1045 CD2 TYR 1008 13.421 48.207 24.076 1.00 30.33 ATOM 1046 CE2 TYR 1008 14.385 48.956 23.403 1.00 26.73 ATOM 1047 CZ TYR 1008 15.659 49.067 23.935 1.00 25.79 ATOM 1048 OH TYR 1008 16.602 49.836 23.297 1.00 24.67 ATOM 1049 C TYR 1008 13.192 48.186 28.111 1.00 35.73 ATOM 1050 O TYR 1008 14.012 47.437 28.658 1.00 36.45 ATOM 1051 N TYR 1008 11.123 48.698 26.792 1.00 32.07 ATOM 1052 CA TYR 1008 12.049 47.614 27.261 1.00 34.16 ATOM 1053 N LYS 1009 13.255 49.513 28.205 1.00 35.03 ATOM 1054 CA LYS 1009 14.289 50.155 29.005 1.00 35.16 ATOM 1055 CB LYS 1009 14.747 51.459 28.349 1.00 34.86 ATOM 1056 CG LYS 1009 15.601 51.245 27.107 1.00 36.13 ATOM 1057 CD LYS 1009 16.422 52.478 26.773 1.00 35.32 ATOM 1058 CE LYS 1009 17.518 52.145 25.772 1.00 37.93 ATOM 1059 NZ LYS 1009 18.571 53.214 25.709 1.00 39.50 ATOM 1060 C LYS 1009 13.783 50.431 30.421 1.00 35.77 ATOM 1061 O LYS 1009 14.569 50.561 31.361 1.00 37.64 ATOM 1062 N LYS 1010 12.464 50.507 30.564 1.00 33.46 ATOM 1063 CA LYS 1010 11.833 50.766 31.850 1.00 31.68 ATOM 1064 GB LYS 1010 10.358 51.138 31.633 1.00 28.72 ATOM 1065 C LYS 1010 11.941 49.557 32.788 1.00 31.01 ATOM 1066 O LYS 1010 11.957 48.409 32.344 1.00 30.93 ATOM 1067 N PRO 1011 12.029 49.805 34.103 1.00 30.79 ATOM 1068 CD PRO 1011 12.250 51.089 34.788 1.00 29.71 ATOM 1069 CA PRO 1011 12.131 48.687 35.047 1.00 30.41 ATOM 1070 GB PRO 1011 12.464 49.376 36.373 1.00 30.93 ATOM 1071 CG PRO 1011 13.115 50.667 35.943 1.00 32.31 ATOM 1072 C PRO 1011 10.798 47.961 35.099 1.00 28.96 ATOM 1073 O PRO 1011 9.759 48.592 34.985 1.00 31.83 ATOM 1074 N LYS 1012 10.823 46.645 35.273 1.00 27.44 ATOM 1075 GA LYS 1012 9.584 45.885 35.321 1.00 27.45 ATOM 1076 GB LYS 1012 9.504 44.892 34.160 1.00 28.07 ATOM 1077 CG LYS 1012 10.095 45.369 32.856 1.00 35.39 ATOM 1078 CD LYS 1012 10.115 44.231 31.835 1.00 41.91 ATOM 1079 CE LYS 1012 10.690 44.665 30.478 1.00 44.00 ATOM 1080 NZ LYS 1012 10.707 43.530 29.503 1.00 45.76 ATOM 1081 C LYS 1012 9.555 45.085 36.598 1.00 27.92 ATOM 1082 O LYS 1012 10.420 45.224 37.462 1.00 27.67 ATOM 1083 N LEU 1013 8.541 44.236 36.696 1.00 25.10 ATOM 1084 CA LEU 1013 8.394 43.341 37.822 1.00 24.38 ATOM 1085 GB LEU 1013 7.102 43.631 38.590 1.00 22.68 ATOM 1086 CG LEU 1013 6.685 45.090 38.740 1.00 22.27 ATOM 1087 CD1 LEU 1013 5.211 45.149 39.144 1.00 19.72 ATOM 1088 CD2 LEU 1013 7.591 45.789 39.743 1.00 18.29 ATOM 1089 C LEU 1013 8.271 41.988 37.120 1.00 26.07 ATOM 1090 O LEU 1013 7.665 41.897 36.047 1.00 25.61 ATOM 1091 N LEU 1014 8.864 40.948 37.697 1.00 26.39 ATOM 1092 CA LEU 1014 8.771 39.617 37.121 1.00 24.33 ATOM 1093 GB LEU 1014 10.144 38.933 37.087 1.00 23.95 ATOM 1094 CG LEU 1014 11.238 39.533 36.193 1.00 24.67 ATOM 1095 CD1 LEU 1014 12.344 38.511 36.017 1.00 23.77 ATOM 1096 CD2 LEU 1014 10.677 39.904 34.823 1.00 27.16 ATOM 1097 C LEU 1014 7.800 38.839 38.000 1.00 24.55 ATOM 1098 O LEU 1014 8.175 38.290 39.032 1.00 29.11 ATOM 1099 N TYR 1015 6.541 38.833 37.584 1.00 21.89 ATOM 1100 CA TYR 1015 5.465 38.158 38.285 1.00 19.64 ATOM 1101 GB TYR 1015 4.135 38.708 37.757 1.00 19.02 ATOM 1102 CG TYR 1015 2.889 37.937 38.129 1.00 17.57 ATOM 1103 CD1 TYR 1015 2.476 36.825 37.395 1.00 12.24 ATOM 1104 GE1 TYR 1015 1.316 36.130 37.739 1.00 12.74 ATOM 1105 CD2 TYR 1015 2.111 38.332 39.219 1.00 20.06 ATOM 1106 CE2 TYR 1015 0.950 37.642 39.570 1.00 17.48 ATOM 1107 GZ TYR 1015 0.560 36.544 38.832 1.00 14.74 ATOM 1108 OH TYR 1015 −0.574 35.866 39.224 1.00 17.22 ATOM 1109 C TYR 1015 5.575 36.669 38.025 1.00 22.05 ATOM 1110 O TYR 1015 5.731 36.254 36.880 1.00 23.85 ATOM 1111 N CYS 1016 5.520 35.864 39.080 1.00 23.50 ATOM 1112 CA CYS 1016 5.588 34.413 38.916 1.00 28.51 ATOM 1113 GB CYS 1016 6.462 33.775 39.988 1.00 28.93 ATOM 1114 SG CYS 1016 6.619 31.990 39.744 1.00 35.75 ATOM 1115 C CYS 1016 4.177 33.848 39.020 1.00 30.00 ATOM 1116 O CYS 1016 3.465 34.110 39.992 1.00 31.04 ATOM 1117 N SER 1017 3.781 33.053 38.032 1.00 31.14 ATOM 1118 CA SER 1017 2.426 32.504 38.005 1.00 33.96 ATOM 1119 GB SER 1017 2.096 32.065 36.578 1.00 33.83 ATOM 1120 OG SER 1017 3.123 31.238 36.061 1.00 37.73 ATOM 1121 C SER 1017 2.102 31.369 38.987 1.00 35.14 ATOM 1122 O SER 1017 0.934 30.988 39.142 1.00 34.27 ATOM 1123 N ASN 1018 3.122 30.851 39.666 1.00 35.68 ATOM 1124 CA ASN 1018 2.919 29.754 40.603 1.00 35.41 ATOM 1125 GB ASN 1018 4.271 29.121 40.947 1.00 37.23 ATOM 1126 CG ASN 1018 4.131 27.744 41.565 1.00 36.80 ATOM 1127 OD1 ASN 1018 3.520 26.843 40.987 1.00 36.57 ATOM 1128 ND2 ASN 1018 4.704 27.575 42.748 1.00 40.08 ATOM 1129 C ASN 1018 2.162 30.148 41.880 1.00 34.04 ATOM 1130 O ASN 1018 1.490 29.314 42.485 1.00 36.26 ATOM 1131 N GLY 1019 2.253 31.410 42.288 1.00 32.38 ATOM 1132 CA GLY 1019 1.548 31.839 43.489 1.00 30.23 ATOM 1133 C GLY 1019 1.185 33.313 43.472 1.00 30.12 ATOM 1134 O GLY 1019 0.650 33.863 44.443 1.00 28.62 ATOM 1135 N GLY 1020 1.487 33.958 42.353 1.00 30.37 ATOM 1136 CA GLY 1020 1.196 35.369 42.217 1.00 32.01 ATOM 1137 C GLY 1020 2.228 36.257 42.882 1.00 31.94 ATOM 1138 O GLY 1020 1.955 37.437 43.120 1.00 34.75 ATOM 1139 N HIS 1021 3.409 35.704 43.171 1.00 31.44 ATOM 1140 CA HIS 1021 4.480 36.460 43.831 1.00 29.29 ATOM 1141 CB HIS 1021 5.358 35.541 44.699 1.00 29.74 ATOM 1142 CG HIS 1021 4.633 34.903 45.844 1.00 30.85 ATOM 1143 CD2 HIS 1021 4.368 35.354 47.093 1.00 30.24 ATOM 1144 ND1 HIS 1021 4.076 33.643 45.764 1.00 28.93 ATOM 1145 GE1 HIS 1021 3.499 33.346 46.916 1.00 30.37 ATOM 1146 NE2 HIS 1021 3.661 34.366 47.740 1.00 32.23 ATOM 1147 C HIS 1021 5.389 37.194 42.867 1.00 27.47 ATOM 1148 O HIS 1021 5.773 36.658 41.828 1.00 28.41 ATOM 1149 N PHE 1022 5.741 38.421 43.229 1.00 26.08 ATOM 1150 CA PHE 1022 6.637 39.234 42.422 1.00 26.98 ATOM 1151 GB PHE 1022 6.378 40.726 42.652 1.00 29.06 ATOM 1152 CG PHE 1022 5.044 41.194 42.152 1.00 33.42 ATOM 1153 CD1 PHE 1022 4.942 42.356 41.399 1.00 35.57 ATOM 1154 CD2 PHE 1022 3.887 40.472 42.430 1.00 36.07 ATOM 1155 CE1 PHE 1022 3.713 42.791 40.930 1.00 35.49 ATOM 1156 CE2 PHE 1022 2.655 40.899 41.966 1.00 36.57 ATOM 1157 CZ PHE 1022 2.568 42.062 41.213 1.00 35.79 ATOM 1158 C PHE 1022 8.058 38.916 42.842 1.00 27.74 ATOM 1159 O PHE 1022 8.386 38.978 44.037 1.00 28.42 ATOM 1160 N LEU 1023 8.905 38.586 41.869 1.00 26.44 ATOM 1161 CA LEU 1023 10.294 38.278 42.173 1.00 25.87 ATOM 1162 GB LEU 1023 11.070 38.015 40.885 1.00 22.37 ATOM 1163 CG LEU 1023 12.441 37.371 41.093 1.00 24.38 ATOM 1164 CD1 LEU 1023 12.332 36.176 42.043 1.00 20.70 ATOM 1165 CD2 LEU 1023 13.002 36.951 39.743 1.00 23.30 ATOM 1166 C LEU 1023 10.898 39.457 42.948 1.00 25.50 ATOM 1167 O LEU 1023 10.807 40.608 42.516 1.00 24.70 ATOM 1168 N ARG 1024 11.489 39.150 44.104 1.00 27.06 ATOM 1169 CA ARG 1024 12.092 40.149 44.998 1.00 26.64 ATOM 1170 CB ARG 1024 11.282 40.229 46.301 1.00 24.40 ATOM 1171 CG ARG 1024 11.960 41.004 47.407 1.00 19.74 ATOM 1172 CD ARG 1024 10.992 41.364 48.527 1.00 17.02 ATOM 1173 NE ARG 1024 10.461 40.193 49.219 1.00 19.05 ATOM 1174 CZ ARG 1024 9.777 40.245 50.363 1.00 21.94 ATOM 1175 NH1 ARG 1024 9.541 41.407 50.955 1.00 20.91 ATOM 1176 NH2 ARG 1024 9.310 39.137 50.919 1.00 25.83 ATOM 1177 C ARG 1024 13.548 39.873 45.348 1.00 24.92 ATOM 1178 O ARG 1024 13.932 38.729 45.586 1.00 27.55 ATOM 1179 N ILE 1025 14.355 40.925 45.376 1.00 25.20 ATOM 1180 CA ILE 1025 15.770 40.791 45.734 1.00 27.59 ATOM 1181 GB ILE 1025 16.704 41.245 44.581 1.00 27.75 ATOM 1182 CG2 ILE 1025 18.162 41.066 44.994 1.00 27.22 ATOM 1183 CG1 ILE 1025 16.424 40.431 43.313 1.00 25.51 ATOM 1184 CD1 ILE 1025 17.321 40.810 42.144 1.00 22.73 ATOM 1185 C ILE 1025 16.059 41.656 46.966 1.00 27.93 ATOM 1186 O ILE 1025 16.398 42.837 46.837 1.00 28.55 ATOM 1187 N LEU 1026 15.901 41.067 48.152 1.00 29.13 ATOM 1188 CA LEU 1026 16.133 41.764 49.420 1.00 30.12 ATOM 1189 CB LEU 1026 15.744 40.864 50.583 1.00 30.24 ATOM 1190 CG LEU 1026 14.253 40.510 50.579 1.00 30.34 ATOM 1191 GD1 LEU 1026 13.980 39.378 51.578 1.00 29.27 ATOM 1192 GD2 LEU 1026 13.432 41.759 50.909 1.00 24.29 ATOM 1193 C LEU 1026 17.594 42.202 49.544 1.00 30.91 ATOM 1194 O LEU 1026 18.512 41.436 49.235 1.00 29.93 ATOM 1195 N PRO 1027 17.822 43.438 50.015 1.00 31.36 ATOM 1196 CD PRO 1027 16.754 44.228 50.666 1.00 30.05 ATOM 1197 CA PRO 1027 19.127 44.086 50.212 1.00 30.53 ATOM 1198 GB PRO 1027 18.771 45.368 50.963 1.00 29.38 ATOM 1199 CG PRO 1027 17.520 45.004 51.693 1.00 30.61 ATOM 1200 C PRO 1027 20.250 43.282 50.879 1.00 30.41 ATOM 1201 O PRO 1027 21.415 43.650 50.804 1.00 30.55 ATOM 1202 N ASP 1028 19.897 42.175 51.509 1.00 31.88 ATOM 1203 CA ASP 1028 20.865 41.316 52.175 1.00 33.73 ATOM 1204 CB ASP 1028 20.212 40.774 53.421 1.00 36.11 ATOM 1205 CG ASP 1028 18.770 40.437 53.182 1.00 40.54 ATOM 1206 OD1 ASP 1028 18.502 39.362 52.595 1.00 39.57 ATOM 1207 OD2 ASP 1028 17.907 41.273 53.546 1.00 44.85 ATOM 1208 C ASP 1028 21.294 40.154 51.273 1.00 34.93 ATOM 1209 O ASP 1028 22.074 39.292 51.679 1.00 35.53 ATOM 1210 N GLY 1029 20.771 40.129 50.054 1.00 35.81 ATOM 1211 CA GLY 1029 21.110 39.070 49.125 1.00 34.91 ATOM 1212 C GLY 1029 20.015 38.025 49.017 1.00 35.42 ATOM 1213 O GLY 1029 20.078 37.159 48.150 1.00 33.85 ATOM 1214 N THR 1030 19.012 38.104 49.890 1.00 36.08 ATOM 1215 CA THR 1030 17.907 37.143 49.885 1.00 36.46 ATOM 1216 CB THR 1030 17.082 37.217 51.204 1.00 39.04 ATOM 1217 OC1 THR 1030 17.765 36.484 52.229 1.00 37.14 ATOM 1218 CG2 THR 1030 15.668 36.638 51.012 1.00 37.72 ATOM 1219 C THR 1030 16.952 37.322 48.711 1.00 36.12 ATOM 1220 O THR 1030 16.364 38.393 48.535 1.00 37.82 ATOM 1221 N VAL 1031 16.797 36.256 47.925 1.00 34.66 ATOM 1222 CA VAL 1031 15.914 36.241 46.757 1.00 32.25 ATOM 1223 CB VAL 1031 16.622 35.588 45.557 1.00 32.21 ATOM 1224 CG1 VAL 1031 15.617 35.305 44.443 1.00 28.71 ATOM 1225 CG2 VAL 1031 17.742 36.502 45.069 1.00 27.43 ATOM 1226 C VAL 1031 14.622 35.481 47.079 1.00 31.61 ATOM 1227 O VAL 1031 14.644 34.315 47.485 1.00 31.86 ATOM 1228 N ASP 1032 13.493 36.145 46.882 1.00 29.65 ATOM 1229 CA ASP 1032 12.207 35.538 47.204 1.00 28.58 ATOM 1230 GB ASP 1032 11.959 35.656 48.707 1.00 27.71 ATOM 1231 CC ASP 1032 11.545 37.075 49.125 1.00 27.66 ATOM 1232 OD1 ASP 1032 11.886 38.060 48.418 1.00 26.65 ATOM 1233 OD2 ASP 1032 10.880 37.203 50.170 1.00 22.45 ATOM 1234 C ASP 1032 11.082 36.258 46.471 1.00 28.37 ATOM 1235 O ASP 1032 11.330 37.059 45.572 1.00 26.82 ATOM 1236 N GLY 1033 9.847 35.986 46.892 1.00 27.76 ATOM 1237 CA GLY 1033 8.698 36.612 46.267 1.00 26.49 ATOM 1238 C GLY 1033 7.779 37.247 47.277 1.00 26.11 ATOM 1239 O GLY 1033 7.820 36.912 48.458 1.00 27.57 ATOM 1240 N THR 1034 6.956 38.178 46.805 1.00 26.39 ATOM 1241 CA THR 1034 5.987 38.882 47.646 1.00 27.75 ATOM 1242 GB THR 1034 6.576 40.181 48.236 1.00 28.31 ATOM 1243 OG1 THR 1034 5.508 41.047 48.646 1.00 30.58 ATOM 1244 CG2 THR 1034 7.439 40.890 47.216 1.00 30.03 ATOM 1245 C THR 1034 4.742 39.247 46.846 1.00 27.63 ATOM 1246 O THR 1034 4.775 39.294 45.619 1.00 31.50 ATOM 1247 N ARG 1035 3.641 39.502 47.532 1.00 24.78 ATOM 1248 CA ARG 1035 2.423 39.864 46.837 1.00 25.50 ATOM 1249 GB ARG 1035 1.249 39.046 47.371 1.00 25.09 ATOM 1250 CG ARG 1035 1.349 37.553 47.119 1.00 23.18 ATOM 1251 CD ARG 1035 0.085 36.839 47.606 1.00 27.17 ATOM 1252 NE ARG 1035 −0.011 35.491 47.048 1.00 31.66 ATOM 1253 CZ ARG 1035 −0.103 34.377 47.771 1.00 33.76 ATOM 1254 NM ARC 1035 −0.122 34.422 49.101 1.00 34.54 ATOM 1255 NH2 ARG 1035 −0.146 33.204 47.162 1.00 35.20 ATOM 1256 C ARG 1035 2.130 41.348 46.992 1.00 27.20 ATOM 1257 O ARG 1035 1.005 41.785 46.805 1.00 28.13 ATOM 1258 N ASP 1036 3.150 42.127 47.332 1.00 31.07 ATOM 1259 CA ASP 1036 2.989 43.568 47.521 1.00 32.80 ATOM 1260 GB ASP 1036 3.524 43.959 48.887 1.00 35.64 ATOM 1261 CG ASP 1036 3.599 45.457 49.067 1.00 40.73 ATOM 1262 OD1 ASP 1036 4.229 45.893 50.064 1.00 41.06 ATOM 1263 OD2 ASP 1036 3.028 46.186 48.217 1.00 36.48 ATOM 1264 C ASP 1036 3.699 44.396 46.445 1.00 33.66 ATOM 1265 O ASP 1036 4.923 44.336 46.309 1.00 34.64 ATOM 1266 N ARG 1037 2.931 45.185 45.700 1.00 33.72 ATOM 1267 CA ARG 1037 3.496 46.000 44.626 1.00 32.18 ATOM 1268 CE ARG 1037 2.438 46.321 43.563 1.00 31.11 ATOM 1269 CG ARG 1037 2.015 45.120 42.750 1.00 31.44 ATOM 1270 CD ARG 1037 1.118 45.481 41.571 1.00 32.91 ATOM 1271 NE ARG 1037 1.828 46.167 40.492 1.00 32.28 ATOM 1272 CZ ARC 1037 1.478 46.085 39.208 1.00 32.10 ATOM 1273 NH1 ARG 1037 0.434 45.346 38.848 1.00 25.01 ATOM 1274 NH2 ARG 1037 2.167 46.745 38.286 1.00 32.51 ATOM 1275 C ARC 1037 4.120 47.295 45.087 1.00 31.28 ATOM 1276 O ARC 1037 4.809 47.958 44.313 1.00 29.49 ATOM 1277 N SER 1038 3.873 47.676 46.333 1.00 31.03 ATOM 1278 CA SER 1038 4.458 48.912 46.818 1.00 31.59 ATOM 1279 GB SER 1038 3.537 49.589 47.836 1.00 31.45 ATOM 1280 CG SER 1038 3.109 48.682 48.832 1.00 37.63 ATOM 1281 C SER 1038 5.833 48.621 47.413 1.00 31.52 ATOM 1282 O SER 1038 6.585 49.549 47.745 1.00 34.45 ATOM 1283 N ASP 1039 6.154 47.330 47.529 1.00 27.62 ATOM 1284 CA ASP 1039 7.443 46.878 48.047 1.00 23.67 ATOM 1285 CB ASP 1039 7.525 45.352 47.963 1.00 24.35 ATOM 1286 CG ASP 1039 8.821 44.791 48.532 1.00 25.55 ATOM 1287 OD1 ASP 1039 9.914 45.113 48.004 1.00 26.48 ATOM 1288 OD2 ASP 1039 8.743 44.014 49.509 1.00 23.80 ATOM 1289 C ASP 1039 8.522 47.516 47.179 1.00 22.77 ATOM 1290 O ASP 1039 8.488 47.414 45.960 1.00 22.56 ATOM 1291 N GLN 1040 9.480 48.180 47.810 1.00 25.29 ATOM 1292 CA GLN 1040 10.551 48.861 47.084 1.00 25.09 ATOM 1293 GB GLN 1040 11.270 49.828 48.027 1.00 24.45 ATOM 1294 C GLN 1040 11.603 47.986 46.394 1.00 25.43 ATOM 1295 O GLN 1040 12.423 48.509 45.645 1.00 26.66 ATOM 1296 N HIS 1041 11.589 46.673 46.620 1.00 25.52 ATOM 1297 CA HIS 1041 12.607 45.809 46.009 1.00 30.58 ATOM 1298 GB HIS 1041 13.342 45.022 47.105 1.00 32.53 ATOM 1299 CG HIS 1041 14.078 45.892 48.078 1.00 36.17 ATOM 1300 CD2 HIS 1041 15.311 46.448 48.017 1.00 35.66 ATOM 1301 ND1 HIS 1041 13.511 46.340 49.254 1.00 35.22 ATOM 1302 CE1 HIS 1041 14.364 47.137 49.874 1.00 34.23 ATOM 1303 NE2 HIS 1041 15.463 47.220 49.145 1.00 35.50 ATOM 1304 C HIS 1041 12.176 44.833 44.898 1.00 31.64 ATOM 1305 O HIS 1041 12.896 43.871 44.594 1.00 28.85 ATOM 1306 N ILE 1042 11.018 45.079 44.288 1.00 32.50 ATOM 1307 CA ILE 1042 10.533 44.212 43.215 1.00 30.50 ATOM 1308 CB ILE 1042 9.023 43.908 43.374 1.00 29.31 ATOM 1309 CG2 ILE 1042 8.834 42.728 44.303 1.00 31.07 ATOM 1310 CG1 ILE 1042 8.285 45.135 43.909 1.00 25.07 ATOM 1311 CD1 ILE 1042 6.785 44.986 43.893 1.00 24.73 ATOM 1312 C ILE 1042 10.794 44.753 41.800 1.00 29.65 ATOM 1313 O ILE 1042 10.647 44.015 40.819 1.00 29.85 ATOM 1314 N GLN 1043 11.191 46.024 41.700 1.00 25.69 ATOM 1315 CA GLN 1043 11.474 46.635 40.403 1.00 25.44 ATOM 1316 CB GLN 1043 11.444 48.163 40.509 1.00 24.97 ATOM 1317 CG GLN 1043 10.162 48.731 41.061 1.00 27.05 ATOM 1318 CD GLN 1043 10.087 48.636 42.564 1.00 30.82 ATOM 1319 OE1 GLN 1043 10.899 49.240 43.272 1.00 38.30 ATOM 1320 NE2 GLN 1043 9.116 47.882 43.068 1.00 27.25 ATOM 1321 C GLN 1043 12.831 46.194 39.840 1.00 23.37 ATOM 1322 O GLN 1043 13.879 46.471 40.411 1.00 25.56 ATOM 1323 N LEU 1044 12.805 45.540 38.692 1.00 21.81 ATOM 1324 CA LEU 1044 14.027 45.049 38.088 1.00 21.98 ATOM 1325 GB LEU 1044 13.942 43.530 37.937 1.00 17.13 ATOM 1326 CG LEU 1044 13.249 42.869 39.132 1.00 18.26 ATOM 1327 CD1 LEU 1044 12.988 41.382 38.843 1.00 15.17 ATOM 1328 CD2 LEU 1044 14.101 43.081 40.389 1.00 12.40 ATOM 1329 C LEU 1044 14.321 45.672 36.734 1.00 23.97 ATOM 1330 O LEU 1044 13.411 46.042 35.983 1.00 24.06 ATOM 1331 N GLN 1045 15.612 45.765 36.434 1.00 24.15 ATOM 1332 CA GLN 1045 16.084 46.311 35.182 1.00 25.60 ATOM 1333 CB GLN 1045 16.999 47.502 35.442 1.00 29.63 ATOM 1334 CG GLN 1045 17.300 48.292 34.194 1.00 32.04 ATOM 1335 CD GLN 1045 16.030 48.816 33.577 1.00 36.81 ATOM 1336 OE1 GLN 1045 15.306 49.596 34.200 1.00 40.53 ATOM 1337 NE2 GLN 1045 15.735 48.382 32.355 1.00 36.91 ATOM 1338 C GLN 1045 16.856 45.230 34.423 1.00 26.34 ATOM 1339 O GLN 1045 18.035 44.977 34.700 1.00 26.34 ATOM 1340 N LEU 1046 16.185 44.597 33.464 1.00 25.58 ATOM 1341 CA LEU 1046 16.806 43.549 32.666 1.00 23.78 ATOM 1342 CB LEU 1046 15.732 42.647 32.046 1.00 22.97 ATOM 1343 CG LEU 1046 15.147 41.560 32.960 1.00 23.09 ATOM 1344 CD1 LEU 1046 14.469 42.162 34.174 1.00 17.46 ATOM 1345 CD2 LEU 1046 14.167 40.733 32.163 1.00 25.21 ATOM 1346 C LEU 1046 17.661 44.171 31.581 1.00 22.40 ATOM 1347 O LEU 1046 17.311 45.223 31.047 1.00 19.22 ATOM 1348 N SER 1047 18.782 43.524 31.269 1.00 23.55 ATOM 1349 CA SER 1047 19.699 44.017 30.237 1.00 26.45 ATOM 1350 CB SER 1047 20.830 44.820 30.871 1.00 21.82 ATOM 1351 OG SER 1047 20.423 45.328 32.123 1.00 25.79 ATOM 1352 C SER 1047 20.300 42.850 29.460 1.00 28.44 ATOM 1353 O SER 1047 20.522 41.775 30.018 1.00 29.64 ATOM 1354 N ALA 1048 20.578 43.064 28.178 1.00 30.05 ATOM 1355 CA ALA 1048 21.158 42.009 27.358 1.00 31.08 ATOM 1356 CB ALA 1048 20.510 42.002 25.973 1.00 29.58 ATOM 1357 C ALA 1048 22.670 42.151 27.225 1.00 33.28 ATOM 1358 O ALA 1048 23.180 43.165 26.741 1.00 33.23 ATOM 1359 N GLU 1049 23.395 41.140 27.679 1.00 35.86 ATOM 1360 CA GLU 1049 24.844 41.163 27.555 1.00 38.31 ATOM 1361 GB GLU 1049 25.467 40.164 28.532 1.00 43.39 ATOM 1362 CG GLU 1049 26.992 40.046 28.448 1.00 52.18 ATOM 1363 CD GLU 1049 27.706 41.401 28.409 1.00 57.15 ATOM 1364 OE1 GLU 1049 27.319 42.318 29.172 1.00 60.15 ATOM 1365 OE2 GLU 1049 28.667 41.542 27.619 1.00 58.73 ATOM 1366 C GLU 1049 25.121 40.746 26.111 1.00 36.83 ATOM 1367 O GLU 1049 26.063 41.211 25.471 1.00 36.38 ATOM 1368 N SER 1050 24.253 39.868 25.617 1.00 34.63 ATOM 1369 CA SER 1050 24.316 39.328 24.271 1.00 30.69 ATOM 1370 CB SER 1050 25.168 38.061 24.245 1.00 32.49 ATOM 1371 OG SER 1050 26.415 38.268 24.883 1.00 36.39 ATOM 1372 C SER 1050 22.880 38.962 23.939 1.00 29.47 ATOM 1373 O SER 1050 22.015 39.005 24.818 1.00 27.73 ATOM 1374 N VAL 1051 22.627 38.601 22.682 1.00 27.04 ATOM 1375 CA VAL 1051 21.282 38.226 22.256 1.00 22.31 ATOM 1376 CB VAL 1051 21.260 37.727 20.774 1.00 21.56 ATOM 1377 CG1 VAL 1051 19.845 37.323 20.367 1.00 20.09 ATOM 1378 CG2 VAL 1051 21.762 38.801 19.851 1.00 19.56 ATOM 1379 C VAL 1051 20.812 37.093 23.157 1.00 21.36 ATOM 1380 O VAL 1051 21.564 36.147 23.405 1.00 20.77 ATOM 1381 N GLY 1052 19.589 37.206 23.666 1.00 20.09 ATOM 1382 CA GLY 1052 19.023 36.166 24.512 1.00 20.83 ATOM 1383 C GLY 1052 19.501 36.003 25.947 1.00 22.14 ATOM 1384 O GLY 1052 18.819 35.359 26.744 1.00 21.79 ATOM 1385 N GLU 1053 20.660 36.564 26.281 1.00 24.79 ATOM 1386 CA GLU 1053 21.215 36.454 27.631 1.00 27.88 ATOM 1387 CB GLU 1053 22.706 36.163 27.553 1.00 26.83 ATOM 1388 CG GLU 1053 23.068 35.352 26.346 1.00 30.13 ATOM 1389 CD GLU 1053 24.499 34.877 26.370 1.00 34.21 ATOM 1390 OE1 GLU 1053 25.405 35.697 26.646 1.00 37.12 ATOM 1391 OE2 GLU 1053 24.715 33.677 26.100 1.00 36.45 ATOM 1392 C GLU 1053 20.988 37.767 28.370 1.00 29.37 ATOM 1393 O GLU 1053 21.326 38.842 27.863 1.00 30.58 ATOM 1394 N VAL 1054 20.446 37.684 29.579 1.00 27.70 ATOM 1395 CA VAL 1054 20.139 38.896 30.313 1.00 26.97 ATOM 1396 CB VAL 1054 18.602 39.150 30.335 1.00 27.40 ATOM 1397 CG1 VAL 1054 18.023 38.965 28.954 1.00 29.21 ATOM 1398 CG2 VAL 1054 17.916 38.209 31.313 1.00 25.23 ATOM 1399 C VAL 1054 20.606 38.986 31.750 1.00 27.70 ATOM 1400 O VAL 1054 20.793 37.983 32.432 1.00 29.51 ATOM 1401 N TYR 1055 20.797 40.221 32.195 1.00 28.25 ATOM 1402 CA TYR 1055 21.148 40.499 33.577 1.00 27.38 ATOM 1403 CB TYR 1055 22.169 41.629 33.690 1.00 26.13 ATOM 1404 CG TYR 1055 23.591 41.215 33.396 1.00 29.84 ATOM 1405 CD1 TYR 1055 24.201 40.194 34.118 1.00 29.78 ATOM 1406 GE1 TYR 1055 25.524 39.838 33.881 1.00 28.70 ATOM 1407 GD2 TYR 1055 24.343 41.869 32.418 1.00 31.06 ATOM 1408 CE2 TYR 1055 25.665 41.522 32.173 1.00 29.16 ATOM 1409 CZ TYR 1055 26.251 40.508 32.910 1.00 29.44 ATOM 1410 OH TYR 1055 27.570 40.179 32.696 1.00 29.79 ATOM 1411 C TYR 1055 19.806 40.966 34.129 1.00 27.37 ATOM 1412 O TYR 1055 18.952 41.460 33.376 1.00 24.82 ATOM 1413 N ILE 1056 19.614 40.799 35.432 1.00 26.35 ATOM 1414 CA ILE 1056 18.371 41.196 36.078 1.00 23.67 ATOM 1415 GB ILE 1056 17.504 39.968 36.340 1.00 20.83 ATOM 1416 CG2 ILE 1056 16.278 40.356 37.161 1.00 17.28 ATOM 1417 CG1 ILE 1056 17.160 39.302 35.005 1.00 18.55 ATOM 1418 CD1 ILE 1056 16.483 37.959 35.149 1.00 17.09 ATOM 1419 C ILE 1056 18.747 41.822 37.403 1.00 26.11 ATOM 1420 O ILE 1056 19.082 41.104 38.343 1.00 29.33 ATOM 1421 N LYS 1057 18.698 43.146 37.506 1.00 26.46 ATOM 1422 CA LYS 1057 19.098 43.749 38.769 1.00 27.70 ATOM 1423 GB LYS 1057 20.449 44.459 38.622 1.00 30.03 ATOM 1424 CG LYS 1057 20.379 45.835 37.990 1.00 32.95 ATOM 1425 CD LYS 1057 21.436 46.748 38.597 1.00 36.32 ATOM 1426 CE LYS 1057 21.260 48.182 38.120 1.00 38.81 ATOM 1427 NZ LYS 1057 21.900 49.160 39.052 1.00 39.14 ATOM 1428 C LYS 1057 18.124 44.698 39.429 1.00 27.84 ATOM 1429 O LYS 1057 17.457 45.492 38.772 1.00 26.59 ATOM 1430 N SER 1058 18.073 44.608 40.755 1.00 29.81 ATOM 1431 CA SER 1058 17.217 45.459 41.558 1.00 30.48 ATOM 1432 GB SER 1058 17.415 45.161 43.048 1.00 29.38 ATOM 1433 OG SER 1058 16.578 45.971 43.859 1.00 26.62 ATOM 1434 C SER 1058 17.599 46.901 41.271 1.00 31.88 ATOM 1435 O SER 1058 18.776 47.251 41.240 1.00 31.86 ATOM 1436 N THR 1059 16.593 47.730 41.040 1.00 33.83 ATOM 1437 CA THR 1059 16.815 49.143 40.770 1.00 36.28 ATOM 1438 GB THR 1059 15.576 49.768 40.137 1.00 36.90 ATOM 1439 OG1 THR 1059 14.424 49.358 40.887 1.00 38.69 ATOM 1440 CG2 THR 1059 15.437 49.339 38.676 1.00 38.15 ATOM 1441 C THR 1059 17.073 49.862 42.092 1.00 35.37 ATOM 1442 O THR 1059 17.759 50.882 42.144 1.00 33.67 ATOM 1443 N GLU 1060 16.508 49.315 43.161 1.00 34.77 ATOM 1444 CA GLU 1060 16.651 49.901 44.480 1.00 33.62 ATOM 1445 GB GLU 1060 15.634 49.270 45.439 1.00 35.37 ATOM 1446 CG GLU 1060 15.275 50.158 46.620 1.00 39.28 ATOM 1447 CD GLU 1060 14.878 51.559 46.176 1.00 42.79 ATOM 1448 OE1 GLU 1060 14.036 51.679 45.251 1.00 45.51 ATOM 1449 OE2 GLU 1060 15.408 52.538 46.750 1.00 43.34 ATOM 1450 C GLU 1060 18.053 49.732 45.045 1.00 31.82 ATOM 1451 O GLU 1060 18.696 50.707 45.428 1.00 29.86 ATOM 1452 N THR 1061 18.525 48.490 45.077 1.00 30.63 ATOM 1453 CA THR 1061 19.826 48.183 45.638 1.00 29.40 ATOM 1454 CB THR 1061 19.750 46.919 46.521 1.00 28.93 ATOM 1455 OG1 THR 1061 19.569 45.764 45.697 1.00 28.79 ATOM 1456 CG2 THR 1061 18.575 47.021 47.492 1.00 27.11 ATOM 1457 C THR 1061 20.962 48.005 44.647 1.00 29.99 ATOM 1458 O THR 1061 22.127 48.086 45.030 1.00 35.77 ATOM 1459 N GLY 1062 20.651 47.771 43.380 1.00 29.28 ATOM 1460 CA GLY 1062 21.719 47.585 42.409 1.00 26.00 ATOM 1461 C GLY 1062 22.337 46.199 42.511 1.00 25.76 ATOM 1462 O GLY 1062 23.469 45.975 42.098 1.00 21.22 ATOM 1463 N GLN 1063 21.589 45.262 43.083 1.00 28.51 ATOM 1464 CA GLN 1063 22.065 43.890 43.208 1.00 29.88 ATOM 1465 CB GLN 1063 21.497 43.212 44.457 1.00 32.67 ATOM 1466 CG GLN 1063 21.849 43.849 45.792 1.00 34.71 ATOM 1467 CD GLN 1063 21.175 43.122 46.942 1.00 35.28 ATOM 1468 OE1 GLN 1063 21.609 42.044 47.343 1.00 34.42 ATOM 1469 NE2 GLN 1063 20.088 43.697 47.458 1.00 35.06 ATOM 1470 C GLN 1063 21.587 43.106 41.992 1.00 29.02 ATOM 1471 O GLN 1063 20.494 43.358 41.478 1.00 30.23 ATOM 1472 N TYR 1064 22.405 42.159 41.544 1.00 26.69 ATOM 1473 CA TYR 1064 22.061 41.317 40.408 1.00 25.12 ATOM 1474 CB TYR 1064 23.292 41.014 39.557 1.00 23.81 ATOM 1475 CG TYR 1064 23.813 42.220 38.829 1.00 26.95 ATOM 1476 CD1 TYR 1064 24.545 43.198 39.495 1.00 26.65 ATOM 1477 CE1 TYR 1064 24.964 44.362 38.837 1.00 28.15 ATOM 1478 CD2 TYR 1064 23.513 42.425 37.484 1.00 28.00 ATOM 1479 CE2 TYR 1064 23.924 43.581 36.819 1.00 27.98 ATOM 1480 CZ TYR 1064 24.644 44.546 37.499 1.00 28.03 ATOM 1481 OH TYR 1064 25.022 45.699 36.846 1.00 28.06 ATOM 1482 C TYR 1064 21.474 40.011 40.902 1.00 24.50 ATOM 1483 O TYR 1064 21.851 39.517 41.957 1.00 25.42 ATOM 1484 N LEU 1065 20.523 39.473 40.153 1.00 24.42 ATOM 1485 CA LEU 1065 19.923 38.207 40.512 1.00 23.15 ATOM 1486 CB LEU 1065 18.582 38.035 39.814 1.00 23.90 ATOM 1487 CG LEU 1065 17.932 36.658 39.952 1.00 27.51 ATOM 1488 CD1 LEU 1065 17.497 36.430 41.401 1.00 27.40 ATOM 1489 CD2 LEU 1065 16.743 36.555 39.003 1.00 24.52 ATOM 1490 C LEU 1065 20.927 37.204 39.983 1.00 25.36 ATOM 1491 O LEU 1065 21.413 37.326 38.853 1.00 26.57 ATOM 1492 N ALA 1066 21.264 36.228 40.811 1.00 27.42 ATOM 1493 CA ALA 1066 22.236 35.221 40.429 1.00 27.55 ATOM 1494 CB ALA 1066 23.624 35.657 40.855 1.00 24.63 ATOM 1495 C ALA 1066 21.890 33.879 41.047 1.00 29.36 ATOM 1496 O ALA 1066 21.021 33.773 41.916 1.00 28.66 ATOM 1497 N MET 1067 22.579 32.852 40.581 1.00 33.15 ATOM 1498 CA MET 1067 22.351 31.500 41.058 1.00 37.68 ATOM 1499 CB MET 1067 21.655 30.681 39.961 1.00 38.84 ATOM 1500 CG MET 1067 21.367 29.234 40.328 1.00 41.87 ATOM 1501 SD MET 1067 20.485 28.324 39.025 1.00 44.00 ATOM 1502 CE MET 1067 18.807 28.413 39.652 1.00 41.60 ATOM 1503 C MET 1067 23.698 30.880 41.432 1.00 39.02 ATOM 1504 O MET 1067 24.624 30.844 40.611 1.00 38.23 ATOM 1505 N ASP 1068 23.798 30.412 42.678 1.00 39.88 ATOM 1506 CA ASP 1068 25.022 29.795 43.185 1.00 40.05 ATOM 1507 CB ASP 1068 24.975 29.714 44.717 1.00 41.63 ATOM 1508 CG ASP 1068 23.904 28.753 45.225 1.00 45.16 ATOM 1509 OD1 ASP 1068 23.692 28.677 46.457 1.00 46.56 ATOM 1510 OD2 ASP 1068 23.273 28.067 44.396 1.00 45.84 ATOM 1511 C ASP 1068 25.175 28.400 42.586 1.00 39.62 ATOM 1512 O ASP 1068 24.269 27.899 41.922 1.00 39.76 ATOM 1513 N THR 1069 26.316 27.768 42.822 1.00 39.31 ATOM 1514 CA THR 1069 26.543 26.434 42.286 1.00 40.50 ATOM 1515 CB THR 1069 27.992 25.997 42.514 1.00 39.46 ATOM 1516 OG1 THR 1069 28.868 27.080 42.171 1.00 42.34 ATOM 1517 CG2 THR 1069 28.329 24.805 41.633 1.00 38.96 ATOM 1518 C THR 1069 25.590 25.387 42.879 1.00 41.08 ATOM 1519 O THR 1069 25.558 24.245 42.429 1.00 40.48 ATOM 1520 N ASP 1070 24.810 25.784 43.879 1.00 42.31 ATOM 1521 CA ASP 1070 23.845 24.888 44.516 1.00 42.77 ATOM 1522 CB ASP 1070 23.551 25.331 45.955 1.00 49.36 ATOM 1523 CG ASP 1070 24.715 25.094 46.897 1.00 54.58 ATOM 1524 OD1 ASP 1070 24.731 25.724 47.979 1.00 56.34 ATOM 1525 OD2 ASP 1070 25.602 24.275 46.564 1.00 57.54 ATOM 1526 C ASP 1070 22.541 24.946 43.752 1.00 39.94 ATOM 1527 O ASP 1070 21.787 23.977 43.715 1.00 39.21 ATOM 1528 N GLY 1071 22.282 26.105 43.155 1.00 38.65 ATOM 1529 CA GLY 1071 21.049 26.320 42.419 1.00 34.25 ATOM 1530 C GLY 1071 20.160 27.176 43.292 1.00 30.47 ATOM 1531 O GLY 1071 18.947 27.003 43.338 1.00 29.38 ATOM 1532 N LEU 1072 20.789 28.099 44.008 1.00 29.55 ATOM 1533 CA LEU 1072 20.076 28.991 44.903 1.00 30.81 ATOM 1534 CB LEU 1072 20.583 28.827 46.339 1.00 30.75 ATOM 1535 CG LEU 1072 20.306 27.440 46.929 1.00 32.71 ATOM 1536 CD1 LEU 1072 20.558 27.471 48.430 1.00 32.26 ATOM 1537 CD2 LEU 1072 18.856 27.025 46.643 1.00 29.92 ATOM 1538 C LEU 1072 20.212 30.436 44.465 1.00 30.66 ATOM 1539 O LEU 1072 21.319 30.944 44.273 1.00 28.03 ATOM 1540 N LEU 1073 19.065 31.088 44.310 1.00 30.39 ATOM 1541 CA LEU 1073 19.020 32.474 43.881 1.00 30.80 ATOM 1542 CB LEU 1073 17.585 32.851 43.497 1.00 31.40 ATOM 1543 CG LEU 1073 16.935 32.037 42.373 1.00 28.83 ATOM 1544 CD1 LEU 1073 15.457 32.382 42.281 1.00 25.56 ATOM 1545 CD2 LEU 1073 17.649 32.313 41.060 1.00 27.91 ATOM 1546 C LEU 1073 19.515 33.389 44.990 1.00 30.29 ATOM 1547 O LEU 1073 19.245 33.145 46.168 1.00 30.31 ATOM 1548 N TYR 1074 20.227 34.447 44.609 1.00 27.89 ATOM 1549 CA TYR 1074 20.752 35.392 45.583 1.00 26.07 ATOM 1550 CB TYR 1074 21.977 34.790 46.263 1.00 22.93 ATOM 1551 CG TYR 1074 23.177 34.697 45.358 1.00 18.75 ATOM 1552 CD1 TYR 1074 24.101 35.741 45.293 1.00 17.28 ATOM 1553 CE1 TYR 1074 25.199 35.673 44.451 1.00 19.02 ATOM 1554 CD2 TYR 1074 23.380 33.580 44.552 1.00 17.20 ATOM 1555 CE2 TYR 1074 24.475 33.502 43.701 1.00 18.58 ATOM 1556 CZ TYR 1074 25.378 34.552 43.657 1.00 20.10 ATOM 1557 OH TYR 1074 26.458 34.494 42.813 1.00 25.05 ATOM 1558 C TYR 1074 21.130 36.711 44.917 1.00 26.56 ATOM 1559 O TYR 1074 21.403 36.745 43.718 1.00 25.36 ATOM 1560 N GLY 1075 21.142 37.791 45.699 1.00 26.90 ATOM 1561 CA GLY 1075 21.508 39.093 45.164 1.00 27.88 ATOM 1562 C GLY 1075 23.020 39.252 45.105 1.00 29.27 ATOM 1563 O GLY 1075 23.724 38.873 46.046 1.00 32.09 ATOM 1564 N SER 1076 23.530 39.806 44.011 1.00 26.40 ATOM 1565 CA SER 1076 24.966 39.983 43.868 1.00 26.05 ATOM 1566 CB SER 1076 25.465 39.180 42.673 1.00 24.24 ATOM 1567 OG SER 1076 26.871 39.285 42.555 1.00 22.31 ATOM 1568 C SER 1076 25.357 41.451 43.715 1.00 28.14 ATOM 1569 O SER 1076 24.887 42.142 42.822 1.00 27.04 ATOM 1570 N GLN 1077 26.234 41.917 44.593 1.00 31.22 ATOM 1571 CA GLN 1077 26.679 43.305 44.579 1.00 34.21 ATOM 1572 CB GLN 1077 27.692 43.535 45.709 1.00 39.89 ATOM 1573 CG GLN 1077 27.220 43.090 47.109 1.00 49.08 ATOM 1574 CD GLN 1077 26.818 41.604 47.183 1.00 53.27 ATOM 1575 OE1 GLN 1077 27.597 40.713 46.825 1.00 54.54 ATOM 1576 NE2 GLN 1077 25.596 41.340 47.652 1.00 54.11 ATOM 1577 C GLN 1077 27.299 43.694 43.238 1.00 32.60 ATOM 1578 O GLN 1077 27.238 44.851 42.832 1.00 32.95 ATOM 1579 N THR 1078 27.909 42.729 42.562 1.00 32.16 ATOM 1580 CA THR 1078 28.536 42.973 41.262 1.00 32.21 ATOM 1581 CB THR 1078 30.094 43.044 41.359 1.00 32.67 ATOM 1582 OG1 THR 1078 30.595 41.836 41.946 1.00 33.55 ATOM 1583 CG2 THR 1078 30.540 44.231 42.199 1.00 30.31 ATOM 1584 C THR 1078 28.170 41.816 40.335 1.00 32.63 ATOM 1585 O THR 1078 28.027 40.681 40.779 1.00 30.17 ATOM 1586 N PRO 1079 28.029 42.094 39.029 1.00 34.72 ATOM 1587 CD PRO 1079 28.243 43.421 38.420 1.00 36.18 ATOM 1588 CA PRO 1079 27.677 41.107 38.001 1.00 35.22 ATOM 1589 CB PRO 1079 27.373 41.977 36.791 1.00 34.64 ATOM 1590 CG PRO 1079 28.368 43.084 36.948 1.00 34.95 ATOM 1591 C PRO 1079 28.780 40.100 37.707 1.00 35.41 ATOM 1592 O PRO 1079 29.958 40.422 37.791 1.00 36.31 ATOM 1593 N ASN 1080 28.387 38.882 37.352 1.00 36.45 ATOM 1594 CA ASN 1080 29.341 37.823 37.032 1.00 36.47 ATOM 1595 CB ASN 1080 29.990 37.285 38.303 1.00 33.73 ATOM 1596 CG ASN 1080 28.968 36.896 39.358 1.00 33.02 ATOM 1597 OD1 ASN 1080 28.868 37.543 40.396 1.00 33.03 ATOM 1598 ND2 ASN 1080 28.197 35.841 39.093 1.00 31.80 ATOM 1599 C ASN 1080 28.637 36.680 36.316 1.00 37.82 ATOM 1600 O ASN 1080 27.420 36.719 36.106 1.00 38.73 ATOM 1601 N GLU 1081 29.405 35.658 35.957 1.00 38.00 ATOM 1602 CA GLU 1081 28.867 34.499 35.256 1.00 37.30 ATOM 1603 CB GLU 1081 29.963 33.431 35.114 1.00 39.90 ATOM 1604 CG GLU 1081 31.106 33.567 36.118 1.00 46.27 ATOM 1605 CD GLU 1081 30.917 32.717 37.370 1.00 50.08 ATOM 1606 OE1 GLU 1081 31.452 33.099 38.442 1.00 50.21 ATOM 1607 OE2 GLU 1081 30.248 31.659 37.275 1.00 52.50 ATOM 1608 C GLU 1081 27.614 33.919 35.924 1.00 35.43 ATOM 1609 O GLU 1081 26.727 33.387 35.246 1.00 35.83 ATOM 1610 N GLU 1082 27.525 34.044 37.243 1.00 31.71 ATOM 1611 CA GLU 1082 26.372 33.524 37.961 1.00 31.35 ATOM 1612 CB GLU 1082 26.724 33.323 39.431 1.00 31.86 ATOM 1613 CG GLU 1082 27.935 32.455 39.661 1.00 32.37 ATOM 1614 CD GLU 1082 27.808 31.638 40.927 1.00 35.13 ATOM 1615 OE1 GLU 1082 27.576 32.245 41.998 1.00 34.64 ATOM 1616 OE2 GLU 1082 27.931 30.388 40.851 1.00 37.63 ATOM 1617 C GLU 1082 25.138 34.420 37.865 1.00 30.97 ATOM 1618 O GLU 1082 24.083 34.078 38.387 1.00 28.54 ATOM 1619 N CYS 1083 25.274 35.563 37.197 1.00 32.94 ATOM 1620 CA CYS 1083 24.172 36.515 37.056 1.00 34.49 ATOM 1621 GB CYS 1083 24.681 37.946 37.256 1.00 36.74 ATOM 1622 SG CYS 1083 25.554 38.234 38.807 1.00 38.01 ATOM 1623 C CYS 1083 23.461 36.440 35.709 1.00 34.35 ATOM 1624 O CYS 1083 22.309 36.864 35.592 1.00 36.33 ATOM 1625 N LEU 1084 24.151 35.920 34.694 1.00 33.18 ATOM 1626 CA LEU 1084 23.583 35.802 33.349 1.00 31.59 ATOM 1627 CB LEU 1084 24.693 35.598 32.326 1.00 29.82 ATOM 1628 CG LEU 1084 25.519 36.830 31.998 1.00 29.05 ATOM 1629 CD1 LEU 1084 26.668 36.436 31.117 1.00 31.19 ATOM 1630 CD2 LEU 1084 24.649 37.856 31.310 1.00 30.96 ATOM 1631 C LEU 1084 22.560 34.684 33.187 1.00 31.04 ATOM 1632 O LEU 1084 22.835 33.521 33.488 1.00 31.52 ATOM 1633 N PHE 1085 21.384 35.053 32.695 1.00 29.39 ATOM 1634 CA PHE 1085 20.302 34.107 32.472 1.00 27.51 ATOM 1635 CB PHE 1085 19.140 34.418 33.412 1.00 25.56 ATOM 1636 CG PHE 1085 19.437 34.122 34.850 1.00 26.35 ATOM 1637 CD1 PHE 1085 19.256 32.837 35.364 1.00 26.39 ATOM 1638 CD2 PHE 1085 19.939 35.117 35.688 1.00 26.04 ATOM 1639 GE1 PHE 1085 19.576 32.542 36.698 1.00 25.79 ATOM 1640 CE2 PHE 1085 20.263 34.837 37.022 1.00 25.17 ATOM 1641 CZ PHE 1085 20.081 33.546 37.526 1.00 24.81 ATOM 1642 C PHE 1085 19.814 34.120 31.020 1.00 28.23 ATOM 1643 O PHE 1085 19.846 35.148 30.326 1.00 26.28 ATOM 1644 N LEU 1086 19.377 32.952 30.563 1.00 28.35 ATOM 1645 CA LEU 1086 18.872 32.797 29.212 1.00 25.31 ATOM 1646 GB LEU 1086 19.145 31.385 28.709 1.00 19.69 ATOM 1647 CG LEU 1086 20.649 31.146 28.547 1.00 21.64 ATOM 1648 CD1 LEU 1086 20.919 29.763 27.995 1.00 18.82 ATOM 1649 CD2 LEU 1086 21.227 32.215 27.631 1.00 19.38 ATOM 1650 C LEU 1086 17.391 33.073 29.255 1.00 25.89 ATOM 1651 O LEU 1086 16.647 32.360 29.925 1.00 25.83 ATOM 1652 N GLU 1087 16.974 34.131 28.562 1.00 26.76 ATOM 1653 CA GLU 1087 15.570 34.511 28.527 1.00 28.92 ATOM 1654 GB GLU 1087 15.428 36.039 28.538 1.00 28.77 ATOM 1655 CG GLU 1087 13.976 36.543 28.523 1.00 27.49 ATOM 1656 CD GLU 1087 13.883 38.060 28.352 1.00 29.97 ATOM 1657 OE1 GLU 1087 14.340 38.573 27.306 1.00 30.86 ATOM 1658 OE2 GLU 1087 13.357 38.747 29.261 1.00 31.30 ATOM 1659 C GLU 1087 14.879 33.944 27.292 1.00 29.76 ATOM 1660 O GLU 1087 15.336 34.141 26.164 1.00 30.29 ATOM 1661 N ARG 1088 13.784 33.227 27.510 1.00 29.72 ATOM 1662 CA ARG 1088 13.041 32.667 26.400 1.00 31.93 ATOM 1663 CB ARG 1088 13.310 31.169 26.238 1.00 36.51 ATOM 1664 CG ARG 1088 12.700 30.625 24.947 1.00 43.94 ATOM 1665 CD ARG 1088 12.476 29.112 24.932 1.00 46.90 ATOM 1666 NE ARG 1088 11.471 28.768 23.922 1.00 52.33 ATOM 1667 CZ ARG 1088 10.807 27.614 23.867 1.00 54.24 ATOM 1668 NH1 ARG 1088 11.037 26.664 24.770 1.00 53.32 ATOM 1669 NH2 ARG 1088 9.894 27.421 22.916 1.00 52.86 ATOM 1670 C ARG 1088 11.547 32.876 26.582 1.00 31.39 ATOM 1671 O ARG 1088 10.975 32.525 27.628 1.00 31.35 ATOM 1672 N LEU 1089 10.927 33.467 25.562 1.00 28.47 ATOM 1673 C LEU 1089 9.490 33.706 25.564 1.00 26.29 ATOM 1674 CB LEU 1089 9.145 34.879 24.641 1.00 23.74 ATOM 1675 CG LEU 1089 7.675 35.197 24.343 1.00 21.80 ATOM 1676 CD1 LEU 1089 6.774 34.974 25.559 1.00 23.10 ATOM 1677 CD2 LEU 1089 7.599 36.636 23.880 1.00 23.12 ATOM 1678 C LEU 1089 8.857 32.423 25.056 1.00 25.24 ATOM 1679 O LEU 1089 8.916 32.122 23.870 1.00 26.06 ATOM 1680 N GLU 1090 8.262 31.658 25.961 1.00 26.17 ATOM 1681 CA GLU 1090 7.656 30.386 25.592 1.00 28.55 ATOM 1682 GB GLU 1090 7.358 29.562 26.850 1.00 28.73 ATOM 1683 CG GLU 1090 8.535 29.404 27.824 1.00 31.24 ATOM 1684 CD GLU 1090 9.790 28.808 27.186 1.00 32.62 ATOM 1685 OE1 GLU 1090 9.712 27.703 26.609 1.00 33.25 ATOM 1686 OE2 GLU 1090 10.862 29.450 27.273 1.00 34.62 ATOM 1687 C GLU 1090 6.379 30.490 24.754 1.00 30.27 ATOM 1688 O GLU 1090 5.722 31.540 24.672 1.00 28.66 ATOM 1689 N GLU 1091 6.034 29.368 24.138 1.00 29.86 ATOM 1690 CA GLU 1091 4.847 29.289 23.316 1.00 30.85 ATOM 1691 CB GLU 1091 4.759 27.895 22.706 1.00 36.47 ATOM 1692 CG GLU 1091 6.007 27.536 21.924 1.00 44.98 ATOM 1693 CD GLU 1091 6.014 26.099 21.445 1.00 49.97 ATOM 1694 OE1 GLU 1091 7.041 25.680 20.859 1.00 53.36 ATOM 1695 OE2 GLU 1091 4.998 25.393 21.654 1.00 52.79 ATOM 1696 C GLU 1091 3.603 29.597 24.145 1.00 27.67 ATOM 1697 O GLU 1091 2.643 30.181 23.644 1.00 26.96 ATOM 1698 N ASN 1092 3.631 29.207 25.413 1.00 25.03 ATOM 1699 CA ASN 1092 2.514 29.447 26.319 1.00 23.79 ATOM 1700 CB ASN 1092 2.668 28.611 27.579 1.00 22.47 ATOM 1701 CG ASN 1092 3.808 29.092 28.455 1.00 24.99 ATOM 1702 OD1 ASN 1092 4.676 29.873 28.021 1.00 25.87 ATOM 1703 ND2 ASN 1092 3.822 28.625 29.695 1.00 21.94 ATOM 1704 C ASN 1092 2.480 30.921 26.698 1.00 24.29 ATOM 1705 O ASN 1092 1.736 31.329 27.594 1.00 24.10 ATOM 1706 N HIS 1093 3.319 31.703 26.026 1.00 24.15 ATOM 1707 CA HIS 1093 3.387 33.146 26.231 1.00 25.70 ATOM 1708 CB HIS 1093 2.019 33.769 25.943 1.00 27.08 ATOM 1709 CG HIS 1093 1.703 33.844 24.484 1.00 27.45 ATOM 1710 CD2 HIS 1093 0.603 34.280 23.828 1.00 29.81 ATOM 1711 ND1 HIS 1093 2.604 33.463 23.514 1.00 28.03 ATOM 1712 CE1 HIS 1093 2.074 33.662 22.320 1.00 27.38 ATOM 1713 NE2 HIS 1093 0.860 34.158 22.483 1.00 28.82 ATOM 1714 C HIS 1093 3.909 33.630 27.577 1.00 23.83 ATOM 1715 O HIS 1093 3.659 34.766 27.993 1.00 21.91 ATOM 1716 N TYR 1094 4.636 32.757 28.253 1.00 22.71 ATOM 1717 CA TYR 1094 5.237 33.109 29.522 1.00 20.61 ATOM 1718 CB TYR 1094 4.935 32.050 30.579 1.00 18.87 ATOM 1719 CG TYR 1094 3.589 32.223 31.238 1.00 19.49 ATOM 1720 CD1 TYR 1094 3.389 33.222 32.183 1.00 19.68 ATOM 1721 CE1 TYR 1094 2.140 33.416 32.762 1.00 17.88 ATOM 1722 CD2 TYR 1094 2.497 31.416 30.887 1.00 15.85 ATOM 1723 CE2 TYR 1094 1.252 31.607 31.455 1.00 9.43 ATOM 1724 CZ TYR 1094 1.081 32.603 32.390 1.00 14.46 ATOM 1725 OH TYR 1094 −0.140 32.793 32.988 1.00 17.63 ATOM 1726 C TYR 1094 6.729 33.163 29.268 1.00 20.82 ATOM 1727 O TYR 1094 7.210 32.712 28.221 1.00 18.07 ATOM 1728 N ASN 1095 7.455 33.739 30.219 1.00 20.89 ATOM 1729 CA ASN 1095 8.900 33.820 30.118 1.00 20.72 ATOM 1730 CB ASN 1095 9.412 35.212 30.487 1.00 21.40 ATOM 1731 CG ASN 1095 9.470 36.143 29.302 1.00 23.13 ATOM 1732 OD1 ASN 1095 9.331 35.708 28.152 1.00 22.83 ATOM 1733 ND2 ASN 1095 9.690 37.434 29.567 1.00 16.97 ATOM 1734 C ASN 1095 9.494 32.835 31.091 1.00 19.44 ATOM 1735 O ASH 1095 8.893 32.530 32.129 1.00 17.11 ATOM 1736 N THR 1096 10.666 32.326 30.738 1.00 17.55 ATOM 1737 CA THR 1096 11.389 31.419 31.610 1.00 17.03 ATOM 1738 CB THR 1096 11.308 29.941 31.161 1.00 15.71 ATOM 1739 OG1 THR 1096 11.824 29.804 29.829 1.00 16.36 ATOM 1740 CG2 THR 1096 9.875 29.444 31.243 1.00 13.45 ATOM 1741 C THR 1096 12.832 31.870 31.561 1.00 18.27 ATOM 1742 O THR 1096 13.339 32.275 30.512 1.00 16.38 ATOM 1743 N TYR 1097 13.490 31.816 32.708 1.00 21.55 ATOM 1744 CA TYR 1097 14.880 32.223 32.780 1.00 23.69 ATOM 1745 CB TYR 1097 15.000 33.436 33.703 1.00 22.27 ATOM 1746 CG TYR 1097 14.243 34.642 33.181 1.00 23.09 ATOM 1747 CD1 TYR 1097 14.825 35.505 32.247 1.00 22.94 ATOM 1748 CE1 TYR 1097 14.135 36.604 31.756 1.00 22.15 ATOM 1749 CD2 TYR 1097 12.940 34.912 33.607 1.00 21.24 ATOM 1750 CE2 TYR 1097 12.241 36.003 33.122 1.00 22.31 ATOM 1751 CZ TYR 1097 12.844 36.850 32.196 1.00 24.38 ATOM 1752 OH TYR 1097 12.159 37.945 31.715 1.00 23.23 ATOM 1753 C TYR 1097 15.730 31.058 33.273 1.00 25.03 ATOM 1754 O TYR 1097 15.580 30.599 34.408 1.00 26.08 ATOM 1755 N ILE 1098 16.601 30.566 32.399 1.00 24.39 ATOM 1756 CA ILE 1098 17.478 29.459 32.736 1.00 25.51 ATOM 1757 CB ILE 1098 17.591 28.452 31.553 1.00 27.69 ATOM 1758 CG2 ILE 1098 18.784 27.513 31.761 1.00 26.48 ATOM 1759 CG1 ILE 1098 16.283 27.664 31.422 1.00 29.30 ATOM 1760 CD1 ILE 1098 16.250 26.691 30.265 1.00 30.50 ATOM 1761 C ILE 1098 18.864 29.971 33.070 1.00 25.47 ATOM 1762 O ILE 1098 19.371 30.864 32.397 1.00 26.03 ATOM 1763 N SER 1099 19.471 29.411 34.115 1.00 27.10 ATOM 1764 CA SER 1099 20.831 29.792 34.505 1.00 26.84 ATOM 1765 CB SER 1099 21.329 28.937 35.672 1.00 25.96 ATOM 1766 OG SER 1099 22.744 28.831 35.633 1.00 23.92 ATOM 1767 C SER 1099 21.751 29.565 33.311 1.00 27.38 ATOM 1768 O SER 1099 21.845 28.449 32.791 1.00 25.65 ATOM 1769 N LYS 1100 22.423 30.627 32.881 1.00 28.81 ATOM 1770 CA LYS 1100 23.329 30.556 31.746 1.00 27.88 ATOM 1771 CB LYS 1100 23.814 31.958 31.381 1.00 25.82 ATOM 1772 CG LYS 1100 24.366 32.105 29.973 1.00 23.03 ATOM 1773 CD LYS 1100 25.670 31.382 29.798 1.00 21.49 ATOM 1774 CE LYS 1100 26.291 31.684 28.444 1.00 27.52 ATOM 1775 NZ LYS 1100 26.639 33.123 28.259 1.00 31.05 ATOM 1776 C LYS 1100 24.510 29.664 32.095 1.00 29.65 ATOM 1777 O LYS 1100 25.001 28.927 31.247 1.00 30.86 ATOM 1778 N LYS 1101 24.952 29.722 33.347 1.00 33.14 ATOM 1779 CA LYS 1101 26.081 28.916 33.799 1.00 36.59 ATOM 1780 CB LYS 1101 26.655 29.498 35.090 1.00 39.16 ATOM 1781 CG LYS 1101 27.824 28.710 35.665 1.00 40.87 ATOM 1782 CD LYS 1101 28.258 29.283 37.004 1.00 43.27 ATOM 1783 CE LYS 1101 29.356 28.445 37.645 1.00 43.89 ATOM 1784 NZ LYS 1101 29.730 28.963 38.999 1.00 45.78 ATOM 1785 C LYS 1101 25.703 27.451 34.030 1.00 38.74 ATOM 1786 O LYS 1101 26.517 26.552 33.831 1.00 40.28 ATOM 1787 N HIS 1102 24.473 27.203 34.452 1.00 39.44 ATOM 1788 CA HIS 1102 24.056 25.831 34.700 1.00 42.07 ATOM 1789 CB HIS 1102 23.574 25.706 36.149 1.00 46.14 ATOM 1790 CG HIS 1102 24.667 25.893 37.156 1.00 50.07 ATOM 1791 CD2 HIS 1102 25.043 26.978 37.877 1.00 52.28 ATOM 1792 ND1 HIS 1102 25.564 24.895 37.474 1.00 53.13 ATOM 1793 CE1 HIS 1102 26.444 25.357 38.346 1.00 54.05 ATOM 1794 NE2 HIS 1102 26.151 26.620 38.606 1.00 52.81 ATOM 1795 C HIS 1102 22.982 25.375 33.711 1.00 41.28 ATOM 1796 O HIS 1102 22.063 24.619 34.061 1.00 37.39 ATOM 1797 N ALA 1103 23.130 25.834 32.469 1.00 40.59 ATOM 1798 CA ALA 1103 22.202 25.512 31.390 1.00 40.36 ATOM 1799 CB ALA 1103 22.635 26.200 30.123 1.00 37.23 ATOM 1800 C ALA 1103 22.096 24.014 31.149 1.00 42.23 ATOM 1801 O ALA 1103 20.997 23.452 31.168 1.00 44.36 ATOM 1802 N GLU 1104 23.238 23.375 30.912 1.00 43.40 ATOM 1803 CA GLU 1104 23.292 21.937 30.665 1.00 42.56 ATOM 1804 CB GLU 1104 24.719 21.447 30.890 1.00 43.94 ATOM 1805 CG GLU 1104 24.823 19.969 31.196 1.00 50.47 ATOM 1806 CD GLU 1104 25.984 19.649 32.132 1.00 53.87 ATOM 1807 OE1 GLU 1104 26.065 18.492 32.608 1.00 53.33 ATOM 1808 OE2 GLU 1104 26.815 20.555 32.389 1.00 56.91 ATOM 1809 C GLU 1104 22.315 21.144 31.548 1.00 40.65 ATOM 1810 O GLU 1104 21.601 20.270 31.071 1.00 40.37 ATOM 1811 N LYS 1105 22.280 21.461 32.836 1.00 39.78 ATOM 1812 CA LYS 1105 21.403 20.764 33.769 1.00 39.91 ATOM 1813 CB LYS 1105 21.907 20.951 35.202 1.00 37.94 ATOM 1814 CG LYS 1105 23.417 21.052 35.304 1.00 39.12 ATOM 1815 CD LYS 1105 23.848 21.809 36.556 1.00 39.21 ATOM 1816 CE LYS 1105 25.327 22.126 36.492 1.00 37.65 ATOM 1817 NZ LYS 1105 25.661 22.762 35.185 1.00 38.50 ATOM 1818 C LYS 1105 19.979 21.296 33.685 1.00 40.75 ATOM 1819 O LYS 1105 19.071 20.742 34.297 1.00 41.96 ATOM 1820 N ASN 1106 19.784 22.376 32.937 1.00 41.18 ATOM 1821 CA ASN 1106 18.462 22.981 32.820 1.00 41.14 ATOM 1822 CB ASN 1106 17.475 21.971 32.234 1.00 44.79 ATOM 1823 CG ASN 1106 17.528 21.926 30.715 1.00 49.01 ATOM 1824 OD1 ASN 1106 17.201 20.907 30.096 1.00 49.41 ATOM 1825 ND2 ASN 1106 17.930 23.044 30.102 1.00 48.31 ATOM 1826 C ASN 1106 17.978 23.480 34.179 1.00 39.12 ATOM 1827 O ASN 1106 16.973 23.021 34.711 1.00 36.06 ATOM 1828 N TRP 1107 18.722 24.429 34.732 1.00 39.99 ATOM 1829 CA TRP 1107 18.415 25.027 36.025 1.00 40.08 ATOM 1830 CB TRP 1107 19.722 25.324 36.770 1.00 44.16 ATOM 1831 CG TRP 1107 20.270 24.147 37.514 1.00 48.80 ATOM 1832 CD2 TRP 1107 21.283 24.171 38.527 1.00 52.38 ATOM 1833 CE2 TRP 1107 21.471 22.836 38.961 1.00 54.23 ATOM 1834 CE3 TRP 1107 22.050 25.188 39.115 1.00 50.87 ATOM 1835 CD1 TRP 1107 19.899 22.839 37.373 1.00 50.05 ATOM 1836 NE1 TRP 1107 20.614 22.045 38.239 1.00 51.58 ATOM 1837 CZ2 TRP 1107 22.402 22.494 39.959 1.00 53.29 ATOM 1838 CZ3 TRP 1107 22.974 24.846 40.106 1.00 50.44 ATOM 1839 CH2 TRP 1107 23.139 23.510 40.517 1.00 50.09 ATOM 1840 C TRP 1107 17.612 26.312 35.836 1.00 36.90 ATOM 1841 O TRP 1107 18.133 27.313 35.345 1.00 35.09 ATOM 1842 N PHE 1108 16.346 26.283 36.234 1.00 34.05 ATOM 1843 CA PHE 1108 15.482 27.447 36.071 1.00 32.57 ATOM 1844 CB PHE 1108 14.032 27.035 35.789 1.00 29.87 ATOM 1845 CG PHE 1108 13.851 26.207 34.556 1.00 31.30 ATOM 1846 CD1 PHE 1108 13.946 24.813 34.617 1.00 29.28 ATOM 1847 CD2 PHE 1108 13.563 26.812 33.333 1.00 30.16 ATOM 1848 CE1 PHE 1108 13.755 24.037 33.483 1.00 27.25 ATOM 1849 CE2 PHE 1108 13.370 26.042 32.189 1.00 27.77 ATOM 1850 CZ PHE 1108 13.466 24.653 32.266 1.00 29.18 ATOM 1851 C PHE 1108 15.426 28.371 37.270 1.00 32.28 ATOM 1852 O PHE 1108 15.757 27.988 38.395 1.00 32.12 ATOM 1853 N VAL 1109 14.993 29.599 36.993 1.00 30.24 ATOM 1854 CA VAL 1109 14.771 30.608 38.009 1.00 28.78 ATOM 1855 CB VAL 1109 14.916 32.040 37.455 1.00 27.91 ATOM 1856 CG1 VAL 1109 14.061 32.986 38.269 1.00 28.52 ATOM 1857 CG2 VAL 1109 16.369 32.493 37.506 1.00 26.43 ATOM 1858 C VAL 1109 13.296 30.341 38.267 1.00 30.90 ATOM 1859 O VAL 1109 12.478 30.445 37.348 1.00 34.02 ATOM 1860 N GLY 1110 12.950 29.968 39.492 1.00 30.71 ATOM 1861 CA GLY 1110 11.561 29.679 39.776 1.00 28.19 ATOM 1862 C GLY 1110 11.182 30.147 41.153 1.00 27.88 ATOM 1863 O GLY 1110 11.994 30.723 41.857 1.00 29.05 ATOM 1864 N LEU 1111 9.939 29.899 41.537 1.00 27.28 ATOM 1865 CA LEU 1111 9.455 30.294 42.841 1.00 25.79 ATOM 1866 CB LEU 1111 8.924 31.720 42.780 1.00 26.52 ATOM 1867 CG LEU 1111 9.968 32.830 42.641 1.00 26.50 ATOM 1868 OD1 LEU 1111 9.340 34.076 42.009 1.00 24.70 ATOM 1869 CD2 LEU 1111 10.546 33.151 44.029 1.00 26.77 ATOM 1870 C LEU 1111 8.364 29.317 43.251 1.00 27.97 ATOM 1871 O LEU 1111 7.591 28.842 42.415 1.00 26.75 ATOM 1872 N LYS 1112 8.311 29.019 44.544 1.00 30.13 ATOM 1873 CA LYS 1112 7.350 28.065 45.075 1.00 31.69 ATOM 1874 CB LYS 1112 7.971 27.331 46.261 1.00 33.89 ATOM 1875 CG LYS 1112 9.118 26.417 45.886 1.00 34.68 ATOM 1876 CD LYS 1112 9.628 25.686 47.115 1.00 40.38 ATOM 1877 CE LYS 1112 9.748 24.186 46.863 1.00 43.55 ATOM 1878 NZ LYS 1112 10.244 23.444 48.060 1.00 47.64 ATOM 1879 C LYS 1112 6.008 28.650 45.487 1.00 30.45 ATOM 1880 O LYS 1112 5.893 29.841 45.709 1.00 30.59 ATOM 1881 N LYS 1113 5.001 27.788 45.588 1.00 30.55 ATOM 1882 CA LYS 1113 3.656 28.182 45.980 1.00 33.46 ATOM 1883 CB LYS 1113 2.889 26.972 46.503 1.00 36.18 ATOM 1884 CG LYS 1113 2.420 26.035 45.415 1.00 40.68 ATOM 1885 CD LYS 1113 1.253 26.630 44.633 1.00 41.87 ATOM 1886 CE LYS 1113 1.340 26.277 43.145 1.00 44.15 ATOM 1887 NZ LYS 1113 1.559 24.825 42.892 1.00 42.02 ATOM 1888 C LYS 1113 3.604 29.276 47.033 1.00 34.24 ATOM 1889 O LYS 1113 2.659 30.056 47.071 1.00 34.86 ATOM 1890 N ASN 1114 4.607 29.334 47.900 1.00 36.89 ATOM 1891 CA ASN 1114 4.621 30.358 48.945 1.00 37.34 ATOM 1892 CB ASN 1114 4.949 29.733 50.303 1.00 38.37 ATOM 1893 CG ASN 1114 6.331 29.136 50.336 1.00 39.19 ATOM 1894 OD1 ASN 1114 7.310 29.793 49.984 1.00 40.59 ATOM 1895 ND2 ASN 1114 6.424 27.885 50.761 1.00 39.86 ATOM 1896 C ASN 1114 5.619 31.472 48.652 1.00 35.57 ATOM 1897 O ASN 1114 5.874 32.311 49.504 1.00 36.04 ATOM 1898 N GLY 1115 6.200 31.458 47.459 1.00 34.06 ATOM 1899 CA GLY 1115 7.134 32.502 47.080 1.00 36.04 ATOM 1900 C GLY 1115 8.564 32.339 47.543 1.00 37.79 ATOM 1901 O GLY 1115 9.403 33.217 47.340 1.00 36.95 ATOM 1902 N SER 1116 8.852 31.213 48.171 1.00 40.51 ATOM 1903 CA SER 1116 10.197 30.966 48.644 1.00 41.68 ATOM 1904 CB SER 1116 10.181 29.933 49.772 1.00 41.90 ATOM 1905 OG SER 1116 11.496 29.620 50.190 1.00 44.49 ATOM 1906 C SER 1116 11.054 30.465 47.494 1.00 42.89 ATOM 1907 O SER 1116 10.576 29.757 46.605 1.00 42.23 ATOM 1908 N CYS 1117 12.323 30.855 47.523 1.00 45.02 ATOM 1909 CA CYS 1117 13.295 30.453 46.519 1.00 46.88 ATOM 1910 CB CYS 1117 14.695 30.722 47.075 1.00 43.60 ATOM 1911 SC CYS 1117 16.032 29.895 46.216 1.00 48.25 ATOM 1912 C CYS 1117 13.134 28.960 46.178 1.00 49.41 ATOM 1913 O CYS 1117 13.038 28.134 47.084 1.00 52.69 ATOM 1914 N LYS 1118 13.071 28.610 44.893 1.00 49.61 ATOM 1915 CA LYS 1118 12.957 27.199 44.509 1.00 49.20 ATOM 1916 CB LYS 1118 11.799 26.982 43.522 1.00 49.31 ATOM 1917 CG LYS 1118 11.683 25.533 43.011 1.00 49.85 ATOM 1918 CD LYS 1118 10.225 25.069 42.854 1.00 50.35 ATOM 1919 CE LYS 1118 10.148 23.575 42.477 1.00 51.22 ATOM 1920 NZ LYS 1118 8.760 22.996 42.520 1.00 51.56 ATOM 1921 C LYS 1118 14.279 26.699 43.904 1.00 49.92 ATOM 1922 O LYS 1118 14.640 27.045 42.777 1.00 50.66 ATOM 1923 N ARG 1119 14.998 25.890 44.673 1.00 50.19 ATOM 1924 CA ARG 1119 16.281 25.343 44.253 1.00 50.36 ATOM 1925 CB ARG 1119 16.624 24.114 45.096 1.00 52.65 ATOM 1926 CG ARG 1119 16.160 24.207 46.545 1.00 56.80 ATOM 1927 CD ARG 1119 16.685 23.048 47.391 1.00 59.18 ATOM 1928 NE ARG 1119 18.143 23.025 47.393 1.00 59.69 ATOM 1929 CZ ARG 1119 18.880 22.090 46.802 1.00 61.21 ATOM 1930 NH1 ARG 1119 18.298 21.084 46.162 1.00 59.96 ATOM 1931 NH2 ARG 1119 20.204 22.171 46.838 1.00 61.64 ATOM 1932 C ARG 1119 16.273 24.956 42.779 1.00 50.59 ATOM 1933 O ARG 1119 15.477 24.124 42.349 1.00 49.28 ATOM 1934 N GLY 1120 17.169 25.563 42.010 1.00 51.51 ATOM 1935 CA GLY 1120 17.259 25.270 40.590 1.00 51.80 ATOM 1936 C GLY 1120 17.227 23.796 40.210 1.00 52.28 ATOM 1937 O GLY 1120 16.583 23.433 39.228 1.00 52.78 ATOM 1938 N PRO 1121 17.912 22.914 40.954 1.00 52.45 ATOM 1939 CD PRO 1121 18.817 23.151 42.088 1.00 52.24 ATOM 1940 CA PRO 1121 17.897 21.492 40.607 1.00 52.16 ATOM 1941 CB PRO 1121 19.020 20.926 41.463 1.00 51.38 ATOM 1942 CG PRO 1121 18.929 21.770 42.682 1.00 51.92 ATOM 1943 C PRO 1121 16.571 20.774 40.847 1.00 51.27 ATOM 1944 O PRO 1121 16.486 19.565 40.648 1.00 51.20 ATOM 1945 N ARG 1122 15.545 21.504 41.279 1.00 51.52 ATOM 1946 CA ARG 1122 14.231 20.898 41.519 1.00 51.08 ATOM 1947 CB ARG 1122 13.789 21.088 42.977 1.00 55.21 ATOM 1948 CG ARG 1122 14.904 21.394 43.970 1.00 60.91 ATOM 1949 CD ARG 1122 15.931 20.274 44.078 1.00 65.86 ATOM 1950 NE ARG 1122 15.424 19.078 44.751 1.00 68.18 ATOM 1951 CZ ARG 1122 16.174 18.016 45.044 1.00 70.69 ATOM 1952 NH1 ARG 1122 17.466 17.993 44.726 1.00 70.77 ATOM 1953 NH2 ARG 1122 15.635 16.975 45.663 1.00 72.96 ATOM 1954 C ARG 1122 13.184 21.532 40.594 1.00 49.22 ATOM 1955 O ARG 1122 11.973 21.357 40.784 1.00 47.14 ATOM 1956 N THR 1123 13.665 22.271 39.596 1.00 46.78 ATOM 1957 CA THR 1123 12.798 22.937 38.638 1.00 44.43 ATOM 1958 CB THR 1123 13.306 24.351 38.326 1.00 40.55 ATOM 1959 OG1 THR 1123 14.431 24.279 37.447 1.00 31.85 ATOM 1960 CG2 THR 1123 13.727 25.048 39.613 1.00 40.32 ATOM 1961 C THR 1123 12.710 22.137 37.339 1.00 47.64 ATOM 1962 O THR 1123 13.731 21.753 36.754 1.00 45.66 ATOM 1963 N HIS 1124 11.479 21.895 36.896 1.00 50.67 ATOM 1964 CA HIS 1124 11.224 21.130 35.678 1.00 54.16 ATOM 1965 CB HIS 1124 10.338 19.916 36.009 1.00 58.09 ATOM 1966 CG HIS 1124 10.131 18.975 34.860 1.00 62.09 ATOM 1967 CD2 HIS 1124 10.504 17.684 34.686 1.00 62.98 ATOM 1968 ND1 HIS 1124 9.467 19.338 33.707 1.00 65.77 ATOM 1969 CE1 HIS 1124 9.439 18.313 32.873 1.00 65.18 ATOM 1970 NE2 HIS 1124 10.062 17.296 33.445 1.00 64.99 ATOM 1971 C HIS 1124 10.549 21.986 34.609 1.00 54.27 ATOM 1972 O HIS 1124 9.888 22.980 34.918 1.00 54.50 ATOM 1973 N TYR 1125 10.722 21.584 33.354 1.00 54.63 ATOM 1974 CA TYR 1125 10.137 22.277 32.214 1.00 54.24 ATOM 1975 CB TYR 1125 10.423 21.496 30.929 1.00 59.36 ATOM 1976 CG TYR 1125 9.671 22.015 29.722 1.00 66.87 ATOM 1977 CD1 TYR 1125 9.981 23.259 29.155 1.00 69.31 ATOM 1978 CE1 TYR 1125 9.269 23.750 28.052 1.00 71.83 ATOM 1979 CD2 TYR 1125 8.630 21.273 29.156 1.00 69.80 ATOM 1980 CE2 TYR 1125 7.912 21.753 28.054 1.00 71.60 ATOM 1981 CZ TYR 1125 8.235 22.988 27.508 1.00 72.61 ATOM 1982 OH TYR 1125 7.527 23.451 26.420 1.00 73.01 ATOM 1983 C TYR 1125 8.628 22.483 32.344 1.00 51.31 ATOM 1984 O TYR 1125 8.091 23.494 31.894 1.00 52.27 ATOM 1985 N GLY 1126 7.941 21.532 32.961 1.00 47.56 ATOM 1986 CA GLY 1126 6.502 21.652 33.087 1.00 43.88 ATOM 1987 C GLY 1126 5.985 22.296 34.354 1.00 42.13 ATOM 1988 O GLY 1126 4.796 22.194 34.664 1.00 42.63 ATOM 1989 N GLN 1127 6.853 22.974 35.090 1.00 39.48 ATOM 1990 CA GLN 1127 6.416 23.601 36.330 1.00 36.35 ATOM 1991 CB GLN 1127 7.569 23.611 37.332 1.00 36.34 ATOM 1992 CG GLN 1127 8.169 22.237 37.592 1.00 39.71 ATOM 1993 CD GLN 1127 9.057 22.204 38.832 1.00 42.52 ATOM 1994 OE1 GLN 1127 10.011 22.983 38.952 1.00 42.90 ATOM 1995 NE2 GLN 1127 8.745 21.297 39.763 1.00 42.62 ATOM 1996 C GLN 1127 5.855 25.019 36.172 1.00 34.79 ATOM 1997 O GLN 1127 6.207 25.751 35.246 1.00 35.39 ATOM 1998 N LYS 1128 4.959 25.388 37.081 1.00 31.56 ATOM 1999 CA LYS 1128 4.362 26.713 37.092 1.00 29.98 ATOM 2000 CB LYS 1128 3.039 26.692 37.860 1.00 30.28 ATOM 2001 CG LYS 1128 1.809 26.365 37.033 1.00 32.79 ATOM 2002 CD LYS 1128 0.595 26.130 37.937 1.00 36.26 ATOM 2003 CE LYS 1128 −0.648 26.865 37.452 1.00 34.75 ATOM 2004 NZ LYS 1128 −0.529 28.348 37.611 1.00 37.92 ATOM 2005 C LYS 1128 5.341 27.630 37.815 1.00 29.54 ATOM 2006 O LYS 1128 5.296 28.852 37.675 1.00 28.37 ATOM 2007 N ALA 1129 6.227 27.020 38.593 1.00 28.70 ATOM 2008 CA ALA 1129 7.209 27.763 39.361 1.00 29.70 ATOM 2009 CB ALA 1129 7.946 26.817 40.300 1.00 31.85 ATOM 2010 C ALA 1129 8.212 28.537 38.501 1.00 28.04 ATOM 2011 O ALA 1129 8.671 29.614 38.897 1.00 24.95 ATOM 2012 N ILE 1130 8.548 27.997 37.331 1.00 25.55 ATOM 2013 CA ILE 1130 9.512 28.668 36.460 1.00 25.84 ATOM 2014 CB ILE 1130 10.408 27.648 35.730 1.00 24.07 ATOM 2015 CG2 ILE 1130 11.103 26.771 36.743 1.00 25.87 ATOM 2016 CG1 ILE 1130 9.576 26.785 34.783 1.00 22.30 ATOM 2017 CD1 ILE 1130 10.421 25.886 33.896 1.00 18.90 ATOM 2018 C ILE 1130 8.901 29.619 35.417 1.00 25.23 ATOM 2019 O ILE 1130 9.620 30.188 34.585 1.00 23.60 ATOM 2020 N LEU 1131 7.582 29.796 35.474 1.00 22.59 ATOM 2021 CA LEU 1131 6.885 30.672 34.542 1.00 21.21 ATOM 2022 CB LEU 1131 5.493 30.115 34.227 1.00 15.60 ATOM 2023 CG LEU 1131 5.505 28.801 33.432 1.00 11.10 ATOM 2024 CD1 LEU 1131 4.108 28.233 33.361 1.00 7.19 ATOM 2025 CD2 LEU 1131 6.082 29.033 32.038 1.00 4.00 ATOM 2026 C LEU 1131 6.774 32.086 35.086 1.00 23.55 ATOM 2027 O LEU 1131 6.251 32.309 36.191 1.00 23.78 ATOM 2028 N PHE 1132 7.265 33.042 34.298 1.00 23.72 ATOM 2029 C APHE 1132 7.249 34.438 34.708 1.00 24.86 ATOM 2030 CB PHE 1132 8.685 34.916 34.968 1.00 28.80 ATOM 2031 CG PHE 1132 9.291 34.355 36.229 1.00 29.89 ATOM 2032 CD1 PHE 1132 9.078 34.978 37.458 1.00 29.52 ATOM 2033 CD2 PHE 1132 10.028 33.176 36.193 1.00 30.41 ATOM 2034 CE1 PHE 1132 9.591 34.429 38.629 1.00 33.18 ATOM 2035 CE2 PHE 1132 10.544 32.616 37.364 1.00 32.28 ATOM 2036 CZ PHE 1132 10.328 33.240 38.582 1.00 32.37 ATOM 2037 C PHE 1132 6.577 35.341 33.697 1.00 24.19 ATOM 2038 O PHE 1132 6.553 35.050 32.505 1.00 28.10 ATOM 2039 N LEU 1133 6.048 36.451 34.186 1.00 22.19 ATOM 2040 CA LEU 1133 5.365 37.404 33.339 1.00 20.42 ATOM 2041 CB LEU 1133 3.875 37.313 33.627 1.00 18.98 ATOM 2042 CG LEU 1133 2.869 37.744 32.573 1.00 17.32 ATOM 2043 CD1 LEU 1133 3.125 36.981 31.292 1.00 17.67 ATOM 2044 CD2 LEU 1133 1.458 37.454 33.091 1.00 17.57 ATOM 2045 C LEU 1133 5.872 38.816 33.636 1.00 21.21 ATOM 2046 O LEU 1133 5.916 39.230 34.790 1.00 21.22 ATOM 2047 N PRO 1134 6.298 39.558 32.602 1.00 22.31 ATOM 2048 CD PRO 1134 6.657 39.079 31.256 1.00 21.79 ATOM 2049 CA PRO 1134 6.788 40.928 32.810 1.00 21.91 ATOM 2050 CB PRO 1134 7.495 41.248 31.496 1.00 22.07 ATOM 2051 CG PRO 1134 7.868 39.892 30.954 1.00 20.81 ATOM 2052 C PRO 1134 5.603 41.874 33.046 1.00 21.75 ATOM 2053 O PRO 1134 4.594 41.786 32.353 1.00 22.26 ATOM 2054 N LEU 1135 5.710 42.761 34.028 1.00 22.32 ATOM 2055 CA LEU 1135 4.632 43.708 34.297 1.00 21.76 ATOM 2056 CB LEU 1135 3.785 43.304 35.512 1.00 17.50 ATOM 2057 CG LEU 1135 2.990 41.993 35.546 1.00 14.52 ATOM 2058 CD1 LEU 1135 1.923 42.095 36.624 1.00 4.60 ATOM 2059 CD2 LEU 1135 2.341 41.732 34.208 1.00 10.88 ATOM 2060 C LEU 1135 5.198 45.072 34.571 1.00 23.53 ATOM 2061 O LEU 1135 6.331 45.199 35.037 1.00 24.94 ATOM 2062 N PRO 1136 4.419 46.121 34.262 1.00 27.53 ATOM 2063 CD PRO 1136 3.196 46.068 33.441 1.00 26.33 ATOM 2064 CA PRO 1136 4.822 47.515 34.482 1.00 28.25 ATOM 2065 CB PRO 1136 3.726 48.305 33.770 1.00 27.06 ATOM 2066 CG PRO 1136 3.281 47.370 32.695 1.00 26.26 ATOM 2067 C PRO 1136 4.805 47.742 35.993 1.00 28.67 ATOM 2068 O PRO 1136 4.103 47.039 36.720 1.00 30.06 ATOM 2069 N VAL 1137 5.560 48.713 36.480 1.00 29.29 ATOM 2070 GA VAL 1137 5.580 48.936 37.916 1.00 27.70 ATOM 2071 CB VAL 1137 6.458 50.136 38.273 1.00 25.31 ATOM 2072 CG1 VAL 1137 6.339 50.425 39.749 1.00 26.58 ATOM 2073 CG2 VAL 1137 7.921 49.830 37.914 1.00 23.39 ATOM 2074 C VAL 1137 4.192 49.130 38.514 1.00 28.47 ATOM 2075 O VAL 1137 3.862 48.516 39.536 1.00 27.14 ATOM 2076 N SER 1138 3.385 49.970 37.863 1.00 32.03 ATOM 2077 CA SER 1138 2.020 50.289 38.314 1.00 32.04 ATOM 2078 CB SER 1138 1.746 51.789 38.143 1.00 30.10 ATOM 2079 C SER 1138 0.918 49.500 37.613 1.00 31.47 ATOM 2080 O SER 1138 −0.213 49.518 38.157 1.00 33.77 ATOM 2081 CB ASN 2147 26.814 102.975 10.017 1.00 45.18 ATOM 2082 CG ASN 2147 28.252 103.343 9.748 1.00 51.54 ATOM 2083 OD1 ASN 2147 28.630 103.582 8.603 1.00 53.81 ATOM 2084 ND2 ASN 2147 29.060 103.421 10.803 1.00 52.12 ATOM 2085 C ASN 2147 24.804 104.423 9.509 1.00 39.76 ATOM 2086 O ASN 2147 24.748 105.461 8.872 1.00 42.25 ATOM 2087 N ASN 2147 25.555 104.031 11.860 1.00 43.01 ATOM 2088 CA ASN 2147 25.973 104.190 10.443 1.00 42.82 ATOM 2089 N ARG 2148 23.848 103.510 9.442 1.00 35.64 ATOM 2090 CA ARG 2148 22.695 103.737 8.568 1.00 33.55 ATOM 2091 CB ARG 2148 22.484 102.544 7.640 1.00 33.03 ATOM 2092 C ARG 2148 21.380 104.083 9.268 1.00 31.68 ATOM 2093 O ARG 2148 21.238 103.902 10.481 1.00 31.50 ATOM 2094 N MET 2149 20.425 104.579 8.485 1.00 29.10 ATOM 2095 CA MET 2149 19.110 104.959 8.982 1.00 26.25 ATOM 2096 CB MET 2149 18.219 105.397 7.824 1.00 27.33 ATOM 2097 CG MET 2149 16.823 105.852 8.235 1.00 28.42 ATOM 2098 SD MET 2149 16.815 107.525 8.910 1.00 36.58 ATOM 2099 CE MET 2149 15.404 107.453 9.968 1.00 29.53 ATOM 2100 C MET 2149 18.426 103.810 9.714 1.00 24.81 ATOM 2101 O MET 2149 18.116 102.777 9.129 1.00 23.83 ATOM 2102 N PRO 2150 18.161 103.987 11.015 1.00 23.19 ATOM 2103 CD PRO 2150 18.459 105.161 11.850 1.00 22.29 ATOM 2104 CA PRO 2150 17.503 102.942 11.807 1.00 21.50 ATOM 2105 CB PRO 2150 17.247 103.630 13.143 1.00 20.73 ATOM 2106 CG PRO 2150 18.411 104.582 13.242 1.00 20.31 ATOM 2107 G PRO 2150 16.222 102.392 11.182 1.00 21.16 ATOM 2108 O PRO 2150 15.409 103.138 10.618 1.00 19.67 ATOM 2109 N VAL 2151 16.056 101.071 11.279 1.00 21.55 ATOM 2110 GA VAL 2151 14.874 100.379 10.751 1.00 16.77 ATOM 2111 CB VAL 2151 15.089 99.899 9.290 1.00 13.02 ATOM 2112 CG1 VAL 2151 13.887 99.086 8.836 1.00 10.15 ATOM 2113 CG2 VAL 2151 15.285 101.091 8.368 1.00 10.43 ATOM 2114 C VAL 2151 14.537 99.164 11.606 1.00 15.22 ATOM 2115 O VAL 2151 15.310 98.206 11.676 1.00 14.27 ATOM 2116 N ALA 2152 13.388 99.207 12.268 1.00 14.49 ATOM 2117 CA ALA 2152 12.980 98.083 13.104 1.00 15.15 ATOM 2118 CB ALA 2152 11.655 98.394 13.793 1.00 11.10 ATOM 2119 C ALA 2152 12.852 96.823 12.234 1.00 15.46 ATOM 2120 O ALA 2152 12.463 96.896 11.064 1.00 14.12 ATOM 2121 N PRO 2153 13.174 95.649 12.799 1.00 16.43 ATOM 2122 CD PRO 2153 13.559 95.410 14.200 1.00 15.40 ATOM 2123 GA PRO 2153 13.093 94.387 12.055 1.00 16.27 ATOM 2124 CB PRO 2153 13.605 93.366 13.064 1.00 16.36 ATOM 2125 CG PRO 2153 13.205 93.968 14.379 1.00 16.80 ATOM 2126 G PRO 2153 11.709 94.043 11.516 1.00 15.96 ATOM 2127 O PRO 2153 10.705 94.176 12.204 1.00 15.23 ATOM 2128 N TYR 2154 11.675 93.596 10.268 1.00 19.71 ATOM 2129 GA TYR 2154 10.424 93.224 9.606 1.00 21.43 ATOM 2130 CB TYR 2154 9.933 94.369 8.743 1.00 18.91 ATOM 2131 CG TYR 2154 10.926 94.732 7.678 1.00 16.22 ATOM 2132 CD1 TYR 2154 12.161 95.274 8.011 1.00 14.25 ATOM 2133 CE1 TYR 2154 13.087 95.600 7.029 1.00 17.02 ATOM 2134 CD2 TYR 2154 10.638 94.521 6.332 1.00 17.27 ATOM 2135 CE2 TYR 2154 11.559 94.842 5.340 1.00 14.79 ATOM 2136 CZ TYR 2154 12.776 95.383 5.696 1.00 15.43 ATOM 2137 OH TYR 2154 13.676 95.728 4.723 1.00 16.67 ATOM 2138 C TYR 2154 10.571 91.995 8.711 1.00 22.61 ATOM 2139 O TYR 2154 11.657 91.687 8.203 1.00 23.08 ATOM 2140 N TRP 2155 9.452 91.316 8.502 1.00 24.53 ATOM 2141 CA TRP 2155 9.404 90.115 7.677 1.00 25.22 ATOM 2142 CB TRP 2155 8.017 89.493 7.786 1.00 20.66 ATOM 2143 CG TRP 2155 7.600 89.146 9.194 1.00 16.41 ATOM 2144 CD2 TRP 2155 8.402 88.535 10.208 1.00 12.68 ATOM 2145 CE2 TRP 2155 7.571 88.351 11.344 1.00 14.74 ATOM 2146 CE3 TRP 2155 9.737 88.123 10.273 1.00 13.09 ATOM 2147 CD1 TRP 2155 6.352 89.305 9.741 1.00 18.18 ATOM 2148 NE1 TRP 2155 6.328 88.829 11.029 1.00 14.03 ATOM 2149 CZ2 TRP 2155 8.040 87.769 12.532 1.00 11.48 ATOM 2150 CZ3 TRP 2155 10.203 87.541 11.459 1.00 12.94 ATOM 2151 CH2 TRP 2155 9.353 87.373 12.569 1.00 14.66 ATOM 2152 C TRP 2155 9.722 90.419 6.210 1.00 27.64 ATOM 2153 O TRP 2155 9.326 91.454 5.679 1.00 27.23 ATOM 2154 N THR 2156 10.433 89.503 5.560 1.00 30.07 ATOM 2155 CA THR 2156 10.810 89.663 4.162 1.00 32.68 ATOM 2156 CB THR 2156 12.334 89.496 3.996 1.00 33.62 ATOM 2157 OG1 THR 2156 12.998 90.564 4.675 1.00 36.23 ATOM 2158 CG2 THR 2156 12.737 89.532 2.531 1.00 40.06 ATOM 2159 C THR 2156 10.083 88.642 3.289 1.00 34.34 ATOM 2160 O THR 2156 10.241 88.617 2.069 1.00 34.49 ATOM 2161 N SER 2157 9.272 87.803 3.918 1.00 35.53 ATOM 2162 CA SER 2157 8.542 86.788 3.181 1.00 36.03 ATOM 2163 CB SER 2157 9.490 85.632 2.860 1.00 37.70 ATOM 2164 OG SER 2157 8.833 84.616 2.133 1.00 43.05 ATOM 2165 C SER 2157 7.375 86.303 4.026 1.00 36.23 ATOM 2166 O SER 2157 7.117 85.106 4.120 1.00 36.84 ATOM 2167 N PRO 2158 6.639 87.242 4.639 1.00 36.88 ATOM 2168 CD PRO 2158 6.668 88.673 4.292 1.00 35.23 ATOM 2169 CA PRO 2158 5.487 86.950 5.498 1.00 37.16 ATOM 2170 CB PRO 2158 4.713 88.262 5.489 1.00 36.26 ATOM 2171 CG PRO 2158 5.790 89.271 5.347 1.00 36.76 ATOM 2172 C PRO 2158 4.653 85.793 4.985 1.00 38.08 ATOM 2173 O PRO 2158 4.120 84.997 5.759 1.00 37.13 ATOM 2174 N ALA 2159 4.536 85.721 3.666 1.00 40.74 ATOM 2175 CA ALA 2159 3.771 84.669 3.020 1.00 41.35 ATOM 2176 CB ALA 2159 3.976 84.737 1.512 1.00 42.33 ATOM 2177 C ALA 2159 4.214 83.310 3.549 1.00 41.99 ATOM 2178 O ALA 2159 3.465 82.636 4.271 1.00 41.46 ATOM 2179 N ALA 2160 5.439 82.922 3.196 1.00 40.06 ATOM 2180 GA ALA 2160 5.992 81.640 3.615 1.00 41.70 ATOM 2181 CB ALA 2160 7.505 81.629 3.395 1.00 40.83 ATOM 2182 C ALA 2160 5.670 81.281 5.072 1.00 42.86 ATOM 2183 O ALA 2160 5.556 80.101 5.418 1.00 45.81 ATOM 2184 N MET 2161 5.505 82.292 5.919 1.00 41.09 ATOM 2185 CA MET 2161 5.223 82.062 7.335 1.00 36.97 ATOM 2186 CB MET 2161 5.658 83.287 8.152 1.00 35.45 ATOM 2187 CG MET 2161 7.028 83.838 7.748 1.00 33.71 ATOM 2188 SD MET 2161 7.574 85.241 8.737 1.00 28.89 ATOM 2189 CE MET 2161 9.301 85.166 8.486 1.00 33.50 ATOM 2190 C MET 2161 3.765 81.725 7.653 1.00 35.46 ATOM 2191 O MET 2161 3.456 81.336 8.775 1.00 33.94 ATOM 2192 N ALA 2162 2.871 81.866 6.677 1.00 35.20 ATOM 2193 CA ALA 2162 1.449 81.575 6.900 1.00 34.67 ATOM 2194 CB ALA 2162 0.669 81.773 5.601 1.00 37.06 ATOM 2195 C ALA 2162 1.243 80.151 7.429 1.00 33.41 ATOM 2196 O ALA 2162 0.459 79.922 8.353 1.00 29.20 ATOM 2197 N LYS 2163 1.953 79.201 6.820 1.00 32.69 ATOM 2198 CA LYS 2163 1.901 77.793 7.208 1.00 30.42 ATOM 2199 CB LYS 2163 2.709 76.972 6.196 1.00 28.48 ATOM 2200 CG LYS 2163 2.830 75.496 6.493 1.00 26.64 ATOM 2201 CD LYS 2163 3.823 74.841 5.536 1.00 27.91 ATOM 2202 CE LYS 2163 4.166 73.406 5.979 1.00 32.58 ATOM 2203 NZ LYS 2163 5.262 72.761 5.179 1.00 29.98 ATOM 2204 C LYS 2163 2.521 77.698 8.605 1.00 30.84 ATOM 2205 O LYS 2163 3.747 77.594 8.744 1.00 29.90 ATOM 2206 N ALA 2164 1.674 77.740 9.634 1.00 29.63 ATOM 2207 CA ALA 2164 2.140 77.705 11.017 1.00 30.27 ATOM 2208 CB ALA 2164 1.104 78.355 11.925 1.00 30.69 ATOM 2209 C ALA 2164 2.503 76.329 11.550 1.00 31.68 ATOM 2210 O ALA 2164 3.525 76.161 12.219 1.00 31.11 ATOM 2211 N LW 2165 1.673 75.337 11.265 1.00 33.60 ATOM 2212 CA LEU 2165 1.949 73.990 11.752 1.00 33.41 ATOM 2213 CB LEU 2165 0.640 73.264 12.060 1.00 30.23 ATOM 2214 CG LEU 2165 0.754 71.790 12.430 1.00 30.51 ATOM 2215 CD1 LEU 2165 1.605 71.634 13.678 1.00 31.21 ATOM 2216 CD2 LEU 2165 −0.631 71.230 12.660 1.00 31.48 ATOM 2217 C LEU 2165 2.782 73.149 10.788 1.00 34.43 ATOM 2218 O LEU 2165 2.491 73.070 9.593 1.00 36.36 ATOM 2219 N HIS 2166 3.831 72.532 11.316 1.00 33.16 ATOM 2220 CA HIS 2166 4.678 71.669 10.517 1.00 32.38 ATOM 2221 CB HIS 2166 6.144 72.100 10.596 1.00 32.21 ATOM 2222 CG HIS 2166 6.515 73.170 9.620 1.00 32.42 ATOM 2223 CD2 HIS 2166 7.354 73.155 8.558 1.00 31.95 ATOM 2224 ND1 HIS 2166 6.009 74.451 9.690 1.00 33.80 ATOM 2225 CE1 HIS 2166 6.521 75.178 8.712 1.00 32.14 ATOM 2226 NE2 HIS 2166 7.340 74.416 8.012 1.00 31.06 ATOM 2227 C HIS 2166 4.540 70.242 11.027 1.00 32.81 ATOM 2228 O HIS 2166 5.107 69.874 12.059 1.00 33.23 ATOM 2229 N ALA 2167 3.761 69.441 10.313 1.00 31.73 ATOM 2230 CA ALA 2167 3.593 68.053 10.695 1.00 29.93 ATOM 2231 CB ALA 2167 2.159 67.602 10.440 1.00 28.39 ATOM 2232 C ALA 2167 4.584 67.267 9.842 1.00 27.89 ATOM 2233 O ALA 2167 4.592 67.373 8.616 1.00 29.00 ATOM 2234 N VAL 2168 5.433 66.490 10.495 1.00 26.21 ATOM 2235 CA VAL 2168 6.442 65.720 9.782 1.00 24.32 ATOM 2236 CB VAL 2168 7.831 66.432 9.911 1.00 22.47 ATOM 2237 CG1 VAL 2168 8.943 65.438 10.278 1.00 21.29 ATOM 2238 CG2 VAL 2168 8.157 67.140 8.617 1.00 15.49 ATOM 2239 C VAL 2168 6.554 64.267 10.250 1.00 24.60 ATOM 2240 O VAL 2168 6.384 63.948 11.436 1.00 23.00 ATOM 2241 N PRO 2169 6.811 63.353 9.311 1.00 23.98 ATOM 2242 CD PRO 2169 6.899 63.436 7.843 1.00 22.43 ATOM 2243 CA PRO 2169 6.931 61.973 9.786 1.00 24.42 ATOM 2244 CB PRO 2169 6.794 61.153 8.500 1.00 21.59 ATOM 2245 CG PRO 2169 7.418 62.052 7.466 1.00 22.42 ATOM 2246 C PRO 2169 8.316 61.854 10.450 1.00 23.60 ATOM 2247 O PRO 2169 9.302 62.438 9.974 1.00 22.30 ATOM 2248 N ALA 2170 8.378 61.129 11.564 1.00 20.63 ATOM 2249 CA ALA 2170 9.627 60.950 12.281 1.00 16.73 ATOM 2250 CB ALA 2170 9.474 59.839 13.294 1.00 16.46 ATOM 2251 C ALA 2170 10.785 60.645 11.343 1.00 15.08 ATOM 2252 O ALA 2170 10.613 59.952 10.340 1.00 14.72 ATOM 2253 N ALA 2171 11.957 61.191 11.670 1.00 16.41 ATOM 2254 CA ALA 2171 13.192 60.979 10.905 1.00 15.01 ATOM 2255 CB ALA 2171 13.190 59.591 10.258 1.00 13.99 ATOM 2256 C ALA 2171 13.491 62.022 9.854 1.00 14.60 ATOM 2257 O ALA 2171 14.598 62.084 9.339 1.00 17.74 ATOM 2258 N ALA 2172 12.519 62.847 9.519 1.00 17.17 ATOM 2259 CA ALA 2172 12.768 63.859 8.509 1.00 18.37 ATOM 2260 CB ALA 2172 11.451 64.297 7.866 1.00 16.27 ATOM 2261 C ALA 2172 13.483 65.060 9.132 1.00 19.13 ATOM 2262 O ALA 2172 13.337 65.338 10.322 1.00 16.21 ATOM 2263 N THR 2173 14.290 65.739 8.320 1.00 21.04 ATOM 2264 CA THR 2173 14.994 66.943 8.748 1.00 18.95 ATOM 2265 CB THR 2173 16.176 67.288 7.801 1.00 18.71 ATOM 2266 CG1 THR 2173 17.276 66.402 8.054 1.00 16.70 ATOM 2267 CG2 TER 2173 16.629 68.736 7.998 1.00 16.01 ATOM 2268 C THR 2173 13.956 68.055 8.655 1.00 20.09 ATOM 2269 O THR 2173 13.250 68.178 7.651 1.00 18.76 ATOM 2270 N VAL 2174 13.851 68.855 9.707 1.00 19.40 ATOM 2271 CA VAL 2174 12.890 69.945 9.732 1.00 15.32 ATOM 2272 CB VAL 2174 12.004 69.821 10.965 1.00 12.17 ATOM 2273 CG1 VAL 2174 11.331 71.134 11.264 1.00 12.60 ATOM 2274 CG2 VAL 2174 10.995 68.736 10.746 1.00 7.68 ATOM 2275 C VAL 2174 13.585 71.297 9.768 1.00 16.49 ATOM 2276 O VAL 2174 14.447 71.517 10.616 1.00 19.77 ATOM 2277 N ALA 2175 13.223 72.195 8.854 1.00 15.74 ATOM 2278 CA ALA 2175 13.807 73.542 8.845 1.00 17.01 ATOM 2279 CB ALA 2175 14.499 73.798 7.524 1.00 14.10 ATOM 2280 C ALA 2175 12.722 74.609 9.091 1.00 18.28 ATOM 2281 O ALA 2175 11.594 74.452 8.638 1.00 21.48 ATOM 2282 N PHE 2176 13.054 75.665 9.840 1.00 20.02 ATOM 2283 CA PHE 2176 12.122 76.774 10.125 1.00 18.22 ATOM 2284 CB PHE 2176 11.761 76.856 11.611 1.00 16.80 ATOM 2285 CG PHE 2176 10.820 75.785 12.061 1.00 17.78 ATOM 2286 CD1 PHE 2176 9.781 75.368 11.236 1.00 16.51 ATOM 2287 CD2 PHE 2176 10.974 75.177 13.307 1.00 20.55 ATOM 2288 CE1 PHE 2176 8.905 74.358 11.634 1.00 18.12 ATOM 2289 CE2 PEE 2176 10.097 74.156 13.723 1.00 22.23 ATOM 2290 CZ PHE 2176 9.058 73.746 12.880 1.00 18.85 ATOM 2291 C PHE 2176 12.750 78.090 9.697 1.00 19.21 ATOM 2292 O PHE 2176 13.904 78.371 9.998 1.00 19.63 ATOM 2293 N ALA 2177 11.987 78.913 9.002 1.00 20.79 ATOM 2294 CA ALA 2177 12.541 80.158 8.518 1.00 22.37 ATOM 2295 CB ALA 2177 12.675 80.099 6.988 1.00 23.14 ATOM 2296 C ALA 2177 11.750 81.385 8.930 1.00 23.63 ATOM 2297 O ALA 2177 10.525 81.357 9.070 1.00 22.68 ATOM 2298 N CYS 2178 12.487 82.465 9.130 1.00 24.40 ATOM 2299 CA CYS 2178 11.920 83.740 9.505 1.00 25.73 ATOM 2300 C CYS 2178 12.706 84.783 8.736 1.00 27.05 ATOM 2301 O CYS 2178 13.464 85.557 9.313 1.00 27.60 ATOM 2302 CB CYS 2178 12.055 83.971 11.013 1.00 26.41 ATOM 2303 SG CYS 2178 10.976 82.891 12.010 1.00 35.82 ATOM 2304 N PRO 2179 12.581 84.781 7.403 1.00 28.11 ATOM 2305 CD PRO 2179 11.929 83.798 6.519 1.00 26.95 ATOM 2306 CA PRO 2179 13.321 85.781 6.629 1.00 28.50 ATOM 2307 CB PRO 2179 12.798 85.570 5.212 1.00 27.84 ATOM 2308 CG PRO 2179 12.599 84.078 5.179 1.00 28.66 ATOM 2309 C PRO 2179 12.988 87.160 7.188 1.00 28.64 ATOM 2310 O PRO 2179 11.820 87.479 7.441 1.00 29.06 ATOM 2311 N SER 2180 14.013 87.971 7.404 1.00 27.60 ATOM 2312 CA SER 2180 13.784 89.287 7.961 1.00 27.62 ATOM 2313 CB SER 2180 13.687 89.208 9.481 1.00 29.43 ATOM 2314 OG SER 2180 12.714 88.260 9.868 1.00 34.19 ATOM 2315 C SER 2180 14.880 90.243 7.600 1.00 25.26 ATOM 2316 O SER 2180 15.938 89.859 7.128 1.00 24.71 ATOM 2317 N SER 2181 14.612 91.508 7.844 1.00 25.59 ATOM 2318 CA SER 2181 15.577 92.537 7.561 1.00 26.24 ATOM 2319 CB SER 2181 15.329 93.100 6.163 1.00 29.28 ATOM 2320 OG SER 2181 16.357 93.995 5.787 1.00 35.09 ATOM 2321 C SER 2181 15.392 93.613 8.620 1.00 25.20 ATOM 2322 O SER 2181 14.482 93.534 9.456 1.00 21.16 ATOM 2323 N GLY 2182 16.260 94.612 8.577 1.00 25.62 ATOM 2324 CA GLY 2182 16.198 95.701 9.529 1.00 25.11 ATOM 2325 C GLY 2182 17.596 96.234 9.718 1.00 26.42 ATOM 2326 O GLY 2182 18.577 95.509 9.504 1.00 26.03 ATOM 2327 N THR 2183 17.701 97.502 10.102 1.00 27.07 ATOM 2328 CA THR 2183 19.007 98.105 10.317 1.00 26.58 ATOM 2329 CB THR 2183 19.416 99.018 9.125 1.00 25.81 ATOM 2330 OG1 THR 2183 19.415 100.390 9.532 1.00 27.66 ATOM 2331 CG2 THR 2183 18.450 98.843 7.967 1.00 26.30 ATOM 2332 C THR 2183 19.039 98.892 11.621 1.00 25.95 ATOM 2333 O THR 2183 18.092 99.604 11.948 1.00 26.68 ATOM 2334 N PRO 2184 20.117 98.723 12.408 1.00 25.59 ATOM 2335 CD PRO 2184 20.357 99.372 13.708 1.00 25.84 ATOM 2336 CA PRO 2184 21.225 97.825 12.066 1.00 23.93 ATOM 2337 CB PRO 2184 22.212 98.037 13.214 1.00 21.04 ATOM 2338 CG PRO 2184 21.329 98.425 14.352 1.00 24.26 ATOM 2339 C PRO 2184 20.711 96.390 11.954 1.00 22.28 ATOM 2340 O PRO 2184 19.664 96.056 12.514 1.00 17.59 ATOM 2341 N ASN 2185 21.437 95.563 11.210 1.00 24.05 ATOM 2342 CA ASN 2185 21.041 94.184 10.981 1.00 25.57 ATOM 2343 CB ASN 2185 22.129 93.439 10.223 1.00 30.66 ATOM 2344 CG ASN 2185 21.560 92.367 9.317 1.00 38.00 ATOM 2345 OD1 ASN 2185 21.167 91.285 9.771 1.00 40.23 ATOM 2346 ND2 ASN 2185 21.490 92.672 8.022 1.00 41.44 ATOM 2347 C ASN 2185 20.708 93.454 12.264 1.00 24.39 ATOM 2348 O ASN 2185 21.550 93.300 13.142 1.00 24.40 ATOM 2349 N PRO 2186 19.462 92.982 12.376 1.00 23.14 ATOM 2350 CD PRO 2186 18.424 93.174 11.349 1.00 24.07 ATOM 2351 CA PRO 2186 18.924 92.256 13.526 1.00 23.24 ATOM 2352 CB PRO 2186 17.424 92.246 13.245 1.00 23.79 ATOM 2353 CG PRO 2186 17.371 92.180 11.766 1.00 25.15 ATOM 2354 C PRO 2186 19.477 90.856 13.838 1.00 25.08 ATOM 2355 O PRO 2186 20.077 90.168 12.996 1.00 24.16 ATOM 2356 N THR 2187 19.236 90.465 15.084 1.00 23.61 ATOM 2357 CA THR 2187 19.658 89.208 15.665 1.00 21.54 ATOM 2358 CB THR 2187 20.002 89.451 17.146 1.00 22.80 ATOM 2359 OG1 THR 2187 21.405 89.687 17.244 1.00 23.78 ATOM 2360 CG2 THR 2187 19.582 88.284 18.041 1.00 22.31 ATOM 2361 C THR 2187 18.605 88.114 15.540 1.00 21.64 ATOM 2362 O THR 2187 17.405 88.396 15.442 1.00 20.29 ATOM 2363 N LEU 2188 19.069 86.863 15.556 1.00 19.99 ATOM 2364 CA LEU 2188 18.183 85.711 15.439 1.00 15.85 ATOM 2365 CB LEU 2188 18.385 85.017 14.085 1.00 10.64 ATOM 2366 CG LEU 2188 17.236 84.247 13.404 1.00 8.83 ATOM 2367 CD1 LEU 2188 17.850 83.322 12.369 1.00 3.96 ATOM 2368 CD2 LEU 2188 16.401 83.443 14.407 1.00 5.07 ATOM 2369 C LEU 2188 18.421 84.697 16.558 1.00 15.07 ATOM 2370 O LEU 2188 19.482 84.086 16.652 1.00 12.76 ATOM 2371 N ALA 2189 17.408 84.520 17.392 1.00 14.83 ATOM 2372 CA ALA 2189 17.462 83.573 18.483 1.00 11.93 ATOM 2373 CB ALA 2189 17.443 84.314 19.819 1.00 8.30 ATOM 2374 C ALA 2189 16.230 82.667 18.340 1.00 13.71 ATOM 2375 O ALA 2189 15.225 83.040 17.726 1.00 12.23 ATOM 2376 N TRP 2190 16.308 81.476 18.915 1.00 14.95 ATOM 2377 CA TRP 2190 15.213 80.538 18.839 1.00 15.29 ATOM 2378 CB TRP 2190 15.593 79.413 17.888 1.00 17.24 ATOM 2379 CG TRP 2190 15.495 79.760 16.430 1.00 16.08 ATOM 2380 CD2 TRP 2190 14.320 79.682 15.622 1.00 13.35 ATOM 2381 CE2 TRP 2190 14.696 80.029 14.305 1.00 12.00 ATOM 2382 CE3 TRP 2190 12.985 79.347 15.883 1.00 14.59 ATOM 2383 CD1 TRP 2190 16.511 80.151 15.597 1.00 13.49 ATOM 2384 NE1 TRP 2190 16.036 80.310 14.320 1.00 11.50 ATOM 2385 CZ2 TRP 2190 13.782 80.048 13.245 1.00 13.72 ATOM 2386 CZ3 TRP 2190 12.073 79.362 14.827 1.00 19.35 ATOM 2387 CH2 TRP 2190 12.480 79.712 13.521 1.00 15.59 ATOM 2388 C TRP 2190 14.792 79.945 20.187 1.00 18.85 ATOM 2389 O TRP 2190 15.628 79.608 21.032 1.00 20.20 ATOM 2390 N LEU 2191 13.484 79.802 20.371 1.00 20.34 ATOM 2391 CA LEU 2191 12.927 79.254 21.601 1.00 23.09 ATOM 2392 CB LEU 2191 12.041 80.305 22.275 1.00 20.62 ATOM 2393 CG LEU 2191 12.626 81.677 22.645 1.00 23.79 ATOM 2394 CD1 LEU 2191 11.612 82.415 23.512 1.00 24.02 ATOM 2395 CD2 LEU 2191 13.935 81.535 23.403 1.00 22.37 ATOM 2396 C LEU 2191 12.100 77.972 21.377 1.00 27.29 ATOM 2397 O LEU 2191 11.570 77.731 20.286 1.00 28.27 ATOM 2398 N LYS 2192 12.002 77.144 22.412 1.00 28.16 ATOM 2399 CA LYS 2192 11.206 75.926 22.335 1.00 29.20 ATOM 2400 CB LYS 2192 12.098 74.678 22.406 1.00 29.35 ATOM 2401 CG LYS 2192 11.347 73.338 22.326 1.00 26.72 ATOM 2402 CD LYS 2192 12.309 72.213 21.933 1.00 31.20 ATOM 2403 CE LYS 2192 11.843 70.819 22.387 1.00 34.93 ATOM 2404 NZ LYS 2192 10.538 70.386 21.818 1.00 36.82 ATOM 2405 C LYS 2192 10.247 75.981 23.517 1.00 29.33 ATOM 2406 O LYS 2192 10.665 75.925 24.671 1.00 27.86 ATOM 2407 N ASN 2193 8.963 76.120 23.220 1.00 30.20 ATOM 2408 CA ASN 2193 7.938 76.210 24.252 1.00 33.58 ATOM 2409 CB ASN 2193 7.739 74.852 24.930 1.00 34.59 ATOM 2410 CG ASN 2193 7.488 73.738 23.940 1.00 38.32 ATOM 2411 OD1 ASN 2193 6.630 73.849 23.072 1.00 39.46 ATOM 2412 ND2 ASN 2193 8.239 72.648 24.070 1.00 42.12 ATOM 2413 C ASN 2193 8.270 77.281 25.310 1.00 33.79 ATOM 2414 O ASN 2193 8.216 77.023 26.512 1.00 34.33 ATOM 2415 N GLY 2194 8.625 78.479 24.859 1.00 31.89 ATOM 2416 CA GLY 2194 8.924 79.548 25.790 1.00 33.29 ATOM 2417 C GLY 2194 10.344 79.649 26.322 1.00 34.90 ATOM 2418 O GLY 2194 10.887 80.745 26.426 1.00 36.26 ATOM 2419 N ALA 2195 10.951 78.523 26.674 1.00 34.28 ATOM 2420 CA ALA 2195 12.304 78.546 27.206 1.00 33.63 ATOM 2421 CB ALA 2195 12.550 77.298 28.049 1.00 31.67 ATOM 2422 C ALA 2195 13.339 78.644 26.091 1.00 33.30 ATOM 2423 O ALA 2195 13.018 78.470 24.917 1.00 32.47 ATOM 2424 N ALA 2196 14.579 78.935 26.469 1.00 32.73 ATOM 2425 CA ALA 2196 15.675 79.038 25.516 1.00 33.36 ATOM 2426 CB ALA 2196 16.934 79.580 26.205 1.00 32.26 ATOM 2427 C ALA 2196 15.926 77.638 24.982 1.00 33.13 ATOM 2428 O ALA 2196 15.685 76.660 25.681 1.00 31.98 ATOM 2429 N PHE 2197 16.409 77.545 23.747 1.00 35.16 ATOM 2430 CA PHE 2197 16.671 76.254 23.116 1.00 36.83 ATOM 2431 CB PHE 2197 15.835 76.118 21.838 1.00 38.27 ATOM 2432 CG PHE 2197 15.884 74.751 21.211 1.00 40.02 ATOM 2433 CD1 PHE 2197 15.880 74.610 19.821 1.00 41.65 ATOM 2434 CD2 PHE 2197 15.881 73.601 22.000 1.00 41.91 ATOM 2435 CE1 PHE 2197 15.867 73.341 19.218 1.00 42.05 ATOM 2436 CE2 PHE 2197 15.869 72.327 21.413 1.00 41.84 ATOM 2437 CZ PHE 2197 15.862 72.198 20.017 1.00 43.55 ATOM 2438 C PHE 2197 18.139 76.103 22.755 1.00 37.43 ATOM 2439 O PHE 2197 18.578 76.608 21.727 1.00 36.20 ATOM 2440 N ALA 2198 18.903 75.415 23.595 1.00 37.88 ATOM 2441 CA ALA 2198 20.315 75.205 23.301 1.00 38.43 ATOM 2442 CB ALA 2198 21.125 75.160 24.598 1.00 39.27 ATOM 2443 C ALA 2198 20.438 73.885 22.541 1.00 38.16 ATOM 2444 O ALA 2198 19.693 72.942 22.804 1.00 37.17 ATOM 2445 N PRO 2199 21.376 73.803 21.584 1.00 38.70 ATOM 2446 CD PRO 2199 22.362 74.829 21.223 1.00 38.08 ATOM 2447 CA PRO 2199 21.584 72.584 20.785 1.00 40.01 ATOM 2448 CB PRO 2199 22.841 72.906 19.964 1.00 37.42 ATOM 2449 CG PRO 2199 23.507 73.982 20.747 1.00 40.90 ATOM 2450 C PRO 2199 21.708 71.275 21.560 1.00 39.78 ATOM 2451 P PRO 2199 21.372 70.209 21.049 1.00 41.63 ATOM 2452 N ASP 2200 22.170 71.358 22.797 1.00 40.44 ATOM 2453 CA ASP 2200 22.333 70.172 23.625 1.00 40.38 ATOM 2454 CG ASP 2200 23.300 70.493 24.760 1.00 44.62 ATOM 2455 CG ASP 2200 24.196 71.674 24.428 1.00 48.63 ATOM 2456 OD1 ASP 2200 24.973 71.579 23.448 1.00 49.39 ATOM 2457 OD2 ASP 2200 24.107 72.703 25.137 1.00 52.60 ATOM 2458 C ASP 2200 20.981 69.736 24.177 1.00 38.45 ATOM 2459 O ASP 2200 20.864 68.689 24.811 1.00 37.39 ATOM 2460 N HIS 2201 19.959 70.549 23.930 1.00 36.35 ATOM 2461 CA HIS 2201 18.609 70.249 24.393 1.00 35.10 ATOM 2462 CB HIS 2201 17.700 71.449 24.176 1.00 36.45 ATOM 2463 CG HIS 2201 17.861 72.521 25.201 1.00 39.01 ATOM 2464 CD2 HIS 2201 16.946 73.275 25.852 1.00 38.88 ATOM 2465 ND1 HIS 2201 19.095 72.937 25.651 1.00 39.27 ATOM 2466 CE1 HIS 2201 18.933 73.902 26.537 1.00 40.23 ATOM 2467 NE2 HIS 2201 17.638 74.127 26.676 1.00 42.05 ATOM 2468 C HIS 2201 18.004 69.064 23.665 1.00 34.79 ATOM 2469 O HIS 2201 16.942 68.573 24.045 1.00 34.44 ATOM 2470 N ARG 2202 18.665 68.615 22.605 1.00 34.15 ATOM 2471 CA ARG 2202 18.151 67.499 21.831 1.00 32.50 ATOM 2472 CB ARG 2202 17.194 68.004 20.752 1.00 30.12 ATOM 2473 CG ARG 2202 17.869 68.809 19.654 1.00 28.46 ATOM 2474 CD ARG 2202 16.895 69.065 18.525 1.00 27.89 ATOM 2475 NE ARG 2202 16.329 67.818 18.025 1.00 25.16 ATOM 2476 GZ ARG 2202 16.687 67.243 16.885 1.00 25.99 ATOM 2477 NH1 ARG 2202 17.613 67.811 16.123 1.00 26.37 ATOM 2478 NH2 ARG 2202 16.117 66.104 16.505 1.00 25.18 ATOM 2479 C ARG 2202 19.268 66.726 21.162 1.00 33.59 ATOM 2480 O ARG 2202 20.315 67.292 20.835 1.00 34.52 ATOM 2481 N ILE 2203 19.041 65.432 20.954 1.00 31.54 ATOM 2482 CA ILE 2203 20.036 64.613 20.292 1.00 29.88 ATOM 2483 CB ILE 2203 19.659 63.133 20.330 1.00 28.99 ATOM 2484 CG2 ILE 2203 20.840 62.288 19.849 1.00 27.29 ATOM 2485 CG1 ILE 2203 19.263 62.747 21.759 1.00 27.78 ATOM 2486 CD1 ILE 2203 18.829 61.320 21.917 1.00 25.32 ATOM 2487 C ILE 2203 20.069 65.093 18.851 1.00 30.87 ATOM 2488 O ILE 2203 19.024 65.374 18.258 1.00 30.90 ATOM 2489 N GLY 2204 21.270 65.204 18.297 1.00 29.89 ATOM 2490 CA GLY 2204 21.406 65.671 16.935 1.00 28.63 ATOM 2491 C GLY 2204 21.812 67.129 16.955 1.00 29.63 ATOM 2492 O GLY 2204 22.605 67.575 16.127 1.00 30.51 ATOM 2493 N GLY 2205 21.279 67.875 17.917 1.00 28.98 ATOM 2494 CA GLY 2205 21.604 69.285 18.023 1.00 30.12 ATOM 2495 C GLY 2205 20.769 70.074 17.043 1.00 31.55 ATOM 2496 O GLY 2205 19.588 69.777 16.862 1.00 34.37 ATOM 2497 N TYR 2206 21.359 71.089 16.420 1.00 30.73 ATOM 2498 CA TYR 2206 20.630 71.872 15.431 1.00 30.91 ATOM 2499 CB TYR 2206 19.278 72.343 15.997 1.00 29.68 ATOM 2500 CG TYR 2206 19.336 73.512 16.967 1.00 33.76 ATOM 2501 CD1 TYR 2206 19.676 74.803 16.524 1.00 33.73 ATOM 2502 CE1 TYR 2206 19.678 75.887 17.387 1.00 31.86 ATOM 2503 CD2 TYR 2206 18.999 73.346 18.315 1.00 33.58 ATOM 2504 CE2 TYR 2206 18.995 74.431 19.189 1.00 35.07 ATOM 2505 CZ TYR 2206 19.334 75.697 18.710 1.00 36.17 ATOM 2506 OH TYR 2206 19.325 76.779 19.546 1.00 38.63 ATOM 2507 C TYR 2206 21.441 73.058 14.924 1.00 31.29 ATOM 2508 O TYR 2206 22.090 73.752 15.692 1.00 32.10 ATOM 2509 N ALA 2207 21.409 73.280 13.617 1.00 31.83 ATOM 2510 CA ALA 2207 22.130 74.396 13.033 1.00 32.22 ATOM 2511 CB ALA 2207 22.808 73.960 11.735 1.00 28.87 ATOM 2512 C ALA 2207 21.188 75.580 12.771 1.00 33.96 ATOM 2513 O ALA 2207 19.976 75.419 12.606 1.00 35.78 ATOM 2514 N VAL 2208 21.758 76.777 12.756 1.00 34.58 ATOM 2515 CA VAL 2208 21.004 77.992 12.493 1.00 33.03 ATOM 2516 CB VAL 2208 20.940 78.912 13.745 1.00 31.00 ATOM 2517 CG1 VAL 2208 20.155 80.170 13.427 1.00 31.63 ATOM 2518 CG2 VAL 2208 20.300 78.173 14.905 1.00 29.43 ATOM 2519 C VAL 2208 21.740 78.726 11.383 1.00 32.68 ATOM 2520 O VAL 2208 22.846 79.210 11.589 1.00 36.08 ATOM 2521 N ALA 2209 21.154 78.779 10.197 1.00 32.38 ATOM 2522 CA ALA 2209 21.787 79.490 9.097 1.00 32.76 ATOM 2523 CB ALA 2209 21.364 78.886 7.761 1.00 32.64 ATOM 2524 C ALA 2209 21.350 80.952 9.196 1.00 32.21 ATOM 2525 O ALA 2209 20.282 81.332 8.733 1.00 29.99 ATOM 2526 N TYR 2210 22.181 81.768 9.824 1.00 35.12 ATOM 2527 CA TYR 2210 21.858 83.178 9.992 1.00 39.15 ATOM 2528 CB TYR 2210 22.958 83.874 10.808 1.00 38.97 ATOM 2529 CG TYR 2210 23.195 83.199 12.135 1.00 42.16 ATOM 2530 CD1 TYR 2210 24.109 82.145 12.254 1.00 43.86 ATOM 2531 CE1 TYR 2210 24.281 81.469 13.466 1.00 44.27 ATOM 2532 CD2 TYR 2210 22.460 83.566 13.263 1.00 43.66 ATOM 2533 CE2 TYR 2210 22.624 82.899 14.483 1.00 46.54 ATOM 2534 CZ TYR 2210 23.535 81.850 14.576 1.00 46.10 ATOM 2535 OH TYR 2210 23.687 81.178 15.772 1.00 48.07 ATOM 2536 C TYR 2210 21.644 83.883 8.650 1.00 38.16 ATOM 2537 O TYR 2210 20.886 84.854 8.549 1.00 38.75 ATOM 2538 N ALA 2211 22.294 83.385 7.610 1.00 36.97 ATOM 2539 CA ALA 2211 22.137 83.998 6.308 1.00 34.88 ATOM 2540 CB ALA 2211 23.155 83.417 5.344 1.00 34.58 ATOM 2541 C ALA 2211 20.718 83.772 5.788 1.00 34.25 ATOM 2542 O ALA 2211 20.147 84.624 5.120 1.00 35.50 ATOM 2543 N THR 2212 20.140 82.627 6.127 1.00 33.86 ATOM 2544 CA THR 2212 18.811 82.265 5.658 1.00 30.60 ATOM 2545 CB THR 2212 18.827 80.848 5.114 1.00 32.70 ATOM 2546 OG1 THR 2212 20.091 80.614 4.491 1.00 37.44 ATOM 2547 CG2 THR 2212 17.732 80.651 4.086 1.00 34.56 ATOM 2548 C THR 2212 17.730 82.334 6.710 1.00 28.90 ATOM 2549 O THR 2212 16.688 81.712 6.556 1.00 27.43 ATOM 2550 N TRP 2213 17.987 83.065 7.787 1.00 29.76 ATOM 2551 CA TRP 2213 17.021 83.240 8.874 1.00 27.80 ATOM 2552 CB TRP 2213 16.019 84.348 8.493 1.00 26.89 ATOM 2553 CG TRP 2213 16.703 85.655 8.204 1.00 27.67 ATOM 2554 CD2 TRP 2213 17.136 86.628 9.167 1.00 29.11 ATOM 2555 CE2 TRP 2213 17.801 87.649 8.457 1.00 29.63 ATOM 2556 CE3 TRP 2213 17.029 86.733 10.561 1.00 29.05 ATOM 2557 CD1 TRP 2213 17.109 86.115 6.991 1.00 27.28 ATOM 2558 NE1 TRP 2213 17.770 87.311 7.132 1.00 29.13 ATOM 2559 CZ2 TRP 2213 18.357 88.764 9.093 1.00 31.44 ATOM 2560 CZ3 TRP 2213 17.581 87.839 11.194 1.00 30.07 ATOM 2561 CH2 TRP 2213 18.238 88.841 10.458 1.00 31.81 ATOM 2562 C TRP 2213 16.287 81.961 9.264 1.00 24.83 ATOM 2563 O TRP 2213 15.090 81.961 9.551 1.00 22.52 ATOM 2564 N SER 2214 17.020 80.861 9.302 1.00 27.35 ATOM 2565 CA SER 2214 16.394 79.591 9.642 1.00 29.71 ATOM 2566 CB SER 2214 16.088 78.819 8.354 1.00 27.02 ATOM 2567 OG SER 2214 17.209 78.851 7.494 1.00 27.71 ATOM 2568 C SER 2214 17.195 78.710 10.601 1.00 28.94 ATOM 2569 O SER 2214 18.374 78.960 10.877 1.00 28.56 ATOM 2570 N ILE 2215 16.514 77.698 11.127 1.00 27.21 ATOM 2571 CA ILE 2215 17.106 76.732 12.040 1.00 28.54 ATOM 2572 CB ILE 2215 16.427 76.730 13.419 1.00 27.61 ATOM 2573 CG2 ILE 2215 14.908 76.803 13.260 1.00 26.81 ATOM 2574 CG1 ILE 2215 16.844 75.461 14.172 1.00 27.42 ATOM 2575 CD1 ILE 2215 16.230 75.302 15.532 1.00 26.34 ATOM 2576 C ILE 2215 16.891 75.362 11.410 1.00 29.14 ATOM 2577 O ILE 2215 15.828 75.079 10.853 1.00 30.48 ATOM 2578 N ILE 2216 17.885 74.499 11.510 1.00 26.76 ATOM 2579 CA ILE 2216 17.747 73.206 10.892 1.00 27.79 ATOM 2580 CB ILE 2216 18.734 73.078 9.715 1.00 27.12 ATOM 2581 CG2 ILE 2216 18.621 71.708 9.083 1.00 28.89 ATOM 2582 CG1 ILE 2216 18.418 74.153 8.671 1.00 27.77 ATOM 2583 CD1 ILE 2216 19.258 74.069 7.413 1.00 28.95 ATOM 2584 C ILE 2216 17.940 72.055 11.853 1.00 28.07 ATOM 2585 O ILE 2216 19.017 71.907 12.441 1.00 29.76 ATOM 2586 N MET 2217 16.891 71.241 12.004 1.00 25.11 ATOM 2587 CA MET 2217 16.931 70.075 12.885 1.00 25.02 ATOM 2588 CB MET 2217 15.785 70.111 13.897 1.00 25.93 ATOM 2589 CG MET 2217 15.711 71.336 14.777 1.00 30.67 ATOM 2590 SD MET 2217 14.404 71.152 16.030 1.00 37.94 ATOM 2591 CE MET 2217 12.915 71.200 15.008 1.00 32.03 ATOM 2592 C MET 2217 16.840 68.748 12.127 1.00 23.05 ATOM 2593 O MET 2217 15.772 68.382 11.618 1.00 23.87 ATOM 2594 N ASP 2218 17.952 68.027 12.057 1.00 19.07 ATOM 2595 CA ASP 2218 17.967 66.734 11.395 1.00 17.04 ATOM 2596 CB ASP 2218 19.408 66.293 11.096 1.00 19.60 ATOM 2597 CG ASP 2218 19.938 66.862 9.781 1.00 26.60 ATOM 2598 OD1 ASP 2218 19.482 67.956 9.391 1.00 30.39 ATOM 2599 OD2 ASP 2218 20.818 66.232 9.137 1.00 29.07 ATOM 2600 C ASP 2218 17.266 65.682 12.266 1.00 15.55 ATOM 2601 O ASP 2218 17.126 65.829 13.480 1.00 9.21 ATOM 2602 N SER 2219 16.791 64.632 11.614 1.00 18.32 ATOM 2603 CA SER 2219 16.131 63.533 12.295 1.00 19.16 ATOM 2604 CB SER 2219 17.168 62.498 12.722 1.00 20.74 ATOM 2605 CG SER 2219 16.575 61.532 13.563 1.00 29.39 ATOM 2606 C SER 2219 15.305 63.939 13.497 1.00 17.12 ATOM 2607 O SER 2219 15.735 63.836 14.643 1.00 17.72 ATOM 2608 N VAL 2220 14.103 64.400 13.222 1.00 17.02 ATOM 2609 CA VAL 2220 13.202 64.799 14.276 1.00 18.02 ATOM 2610 CB VAL 2220 12.095 65.705 13.731 1.00 19.17 ATOM 2611 CG1 VAL 2220 12.692 66.990 13.189 1.00 19.80 ATOM 2612 CG2 VAL 2220 11.328 64.961 12.630 1.00 22.22 ATOM 2613 C VAL 2220 12.550 63.535 14.814 1.00 18.57 ATOM 2614 O VAL 2220 12.417 62.532 14.103 1.00 18.14 ATOM 2615 N VAL 2221 12.132 63.593 16.067 1.00 18.04 ATOM 2616 CA VAL 2221 11.463 62.469 16.704 1.00 18.22 ATOM 2617 CB VAL 2221 12.460 61.595 17.490 1.00 19.68 ATOM 2618 CG1 VAL 2221 13.130 60.596 16.551 1.00 15.48 ATOM 2619 CG2 VAL 2221 13.519 62.495 18.157 1.00 19.19 ATOM 2620 C VAL 2221 10.474 63.097 17.661 1.00 18.71 ATOM 2621 O VAL 2221 10.654 64.248 18.069 1.00 18.32 ATOM 2622 N PRO 2222 9.423 62.352 18.039 1.00 18.55 ATOM 2623 CD PRO 2222 9.259 60.918 17.752 1.00 17.61 ATOM 2624 CA PRO 2222 8.371 62.819 18.957 1.00 19.07 ATOM 2625 CB PRO 2222 7.801 61.515 19.508 1.00 16.37 ATOM 2626 CG PRO 2222 7.871 60.619 18.325 1.00 15.33 ATOM 2627 C PRO 2222 8.823 63.781 20.062 1.00 19.36 ATOM 2628 O PRO 2222 8.175 64.794 20.305 1.00 21.25 ATOM 2629 N SER 2223 9.933 63.475 20.721 1.00 20.13 ATOM 2630 CA SER 2223 10.429 64.341 21.782 1.00 20.49 ATOM 2631 CB SER 2223 11.736 63.787 22.364 1.00 16.62 ATOM 2632 OG SER 2223 12.840 64.105 21.535 1.00 16.05 ATOM 2633 C SER 2223 10.660 65.767 21.256 1.00 22.58 ATOM 2634 O SER 2223 10.679 66.725 22.036 1.00 23.81 ATOM 2635 N ASP 2224 10.830 65.905 19.941 1.00 21.50 ATOM 2636 CA ASP 2224 11.063 67.210 19.348 1.00 20.08 ATOM 2637 CB ASP 2224 11.709 67.073 17.970 1.00 22.89 ATOM 2638 CG ASP 2224 13.157 66.627 18.044 1.00 24.95 ATOM 2639 OD1 ASP 2224 13.891 67.184 18.886 1.00 24.92 ATOM 2640 OD2 ASP 2224 13.557 65.738 17.252 1.00 23.39 ATOM 2641 C ASP 2224 9.785 68.027 19.224 1.00 20.98 ATOM 2642 O ASP 2224 9.839 69.251 19.123 1.00 22.98 ATOM 2643 N ALA 2225 8.635 67.365 19.237 1.00 21.09 ATOM 2644 CA ALA 2225 7.356 68.071 19.115 1.00 22.05 ATOM 2645 CB ALA 2225 6.186 67.105 19.384 1.00 17.67 ATOM 2646 C ALA 2225 7.264 69.273 20.060 1.00 23.32 ATOM 2647 O ALA 2225 7.629 69.181 21.233 1.00 23.49 ATOM 2648 N GLY 2226 6.780 70.400 19.539 1.00 24.74 ATOM 2649 CA GLY 2226 6.620 71.594 20.354 1.00 24.38 ATOM 2650 C GLY 2226 6.560 72.886 19.554 1.00 26.79 ATOM 2651 O GLY 2226 6.673 72.886 18.323 1.00 27.32 ATOM 2652 N ASN 2227 6.382 74.001 20.258 1.00 26.78 ATOM 2653 CA ASN 2227 6.339 75.313 19.619 1.00 25.96 ATOM 2654 CB ASN 2227 5.554 76.310 20.466 1.00 24.91 ATOM 2655 CG ASN 2227 4.164 75.831 20.774 1.00 28.61 ATOM 2656 OD1 ASN 2227 3.433 75.420 19.874 1.00 30.98 ATOM 2657 ND2 ASN 2227 3.781 75.877 22.050 1.00 26.89 ATOM 2658 C ASN 2227 7.755 75.836 19.471 1.00 24.70 ATOM 2659 O ASM 2227 8.550 75.732 20.401 1.00 29.55 ATOM 2660 N TYR 2228 8.073 76.387 18.307 1.00 20.57 ATOM 2661 CA TYR 2228 9.386 76.947 18.075 1.00 18.55 ATOM 2662 CB TYR 2228 10.118 76.171 17.005 1.00 14.84 ATOM 2663 CG TYR 2228 10.521 74.819 17.498 1.00 18.09 ATOM 2664 CD1 TYR 2228 9.564 73.807 17.684 1.00 16.76 ATOM 2665 CE1 TYR 2228 9.934 72.535 18.143 1.00 18.01 ATOM 2666 CD2 TYR 2228 11.862 74.537 17.787 1.00 17.90 ATOM 2667 CE2 TYR 2228 12.248 73.273 18.245 1.00 21.76 ATOM 2668 CZ TYR 2228 11.281 72.273 18.418 1.00 19.94 ATOM 2669 OH TYR 2228 11.681 71.023 18.830 1.00 17.62 ATOM 2670 C TYR 2228 9.227 78.396 17.679 1.00 21.31 ATOM 2671 O TYR 2228 8.512 78.722 16.719 1.00 21.45 ATOM 2672 N THR 2229 9.891 79.269 18.430 1.00 18.76 ATOM 2673 CA THR 2229 9.777 80.681 18.177 1.00 18.04 ATOM 2674 CB THR 2229 9.240 81.411 19.402 1.00 16.54 ATOM 2675 OG1 THR 2229 7.945 80.894 19.727 1.00 15.07 ATOM 2676 CG2 THR 2229 9.134 82.906 19.123 1.00 14.42 ATOM 2677 C THR 2229 11.059 81.340 17.782 1.00 20.77 ATOM 2678 O THR 2229 12.065 81.227 18.476 1.00 25.59 ATOM 2679 N CYS 2230 11.033 82.030 16.653 1.00 21.16 ATOM 2680 CA GYS 2230 12.218 82.746 16.246 1.00 21.18 ATOM 2681 C CYS 2230 12.018 84.144 16.811 1.00 18.33 ATOM 2682 O CYS 2230 10.890 84.620 16.942 1.00 15.60 ATOM 2683 CB GYS 2230 12.348 82.797 14.723 1.00 21.87 ATOM 2684 SG CYS 2230 10.999 83.670 13.892 1.00 30.17 ATOM 2685 N ILE 2231 13.112 84.785 17.187 1.00 18.41 ATOM 2686 CA ILE 2231 13.028 86.128 17.712 1.00 18.07 ATOM 2687 CB ILE 2231 13.222 86.138 19.221 1.00 19.30 ATOM 2688 CG2 ILE 2231 13.386 87.558 19.718 1.00 20.15 ATOM 2689 CG1 ILE 2231 11.996 85.483 19.871 1.00 21.87 ATOM 2690 CD1 ILE 2231 12.043 85.418 21.373 1.00 20.48 ATOM 2691 C ILE 2231 14.063 86.988 17.037 1.00 17.55 ATOM 2692 O ILE 2231 15.263 86.760 17.180 1.00 20.34 ATOM 2693 N VAL 2232 13.576 87.960 16.274 1.00 16.63 ATOM 2694 CA VAL 2232 14.417 88.888 15.536 1.00 16.78 ATOM 2695 CB VAL 2232 13.937 89.017 14.075 1.00 16.85 ATOM 2696 CG1 VAL 2232 14.824 89.995 13.316 1.00 14.47 ATOM 2697 CG2 VAL 2232 13.936 87.644 13.408 1.00 12.11 ATOM 2698 C VAL 2232 14.334 90.244 16.206 1.00 19.10 ATOM 2699 O VAL 2232 13.240 90.736 16.512 1.00 18.37 ATOM 2700 N GLU 2233 15.489 90.855 16.434 1.00 23.01 ATOM 2701 CA GLU 2233 15.521 92.157 17.096 1.00 28.37 ATOM 2702 CB GLU 2233 15.256 91.989 18.596 1.00 33.71 ATOM 2703 CG GLU 2233 16.105 90.891 19.238 1.00 44.29 ATOM 2704 CD GLU 2233 15.834 90.711 20.730 1.00 50.75 ATOM 2705 OE1 GLU 2233 14.653 90.778 21.149 1.00 53.52 ATOM 2706 OE2 GLU 2233 16.807 90.486 21.486 1.00 55.00 ATOM 2707 C GLU 2233 16.834 92.902 16.932 1.00 27.80 ATOM 2708 O GLU 2233 17.892 92.294 16.725 1.00 26.70 ATOM 2709 N ASN 2234 16.741 94.228 17.021 1.00 25.44 ATOM 2710 GA ASN 2234 17.898 95.111 16.954 1.00 23.06 ATOM 2711 CB ASN 2234 18.136 95.666 15.536 1.00 20.37 ATOM 2712 CG ASN 2234 16.960 96.474 14.996 1.00 19.88 ATOM 2713 OD1 ASN 2234 16.098 96.928 15.744 1.00 17.91 ATOM 2714 ND2 ASN 2234 16.939 96.672 13.677 1.00 18.95 ATOM 2715 C ASN 2234 17.614 96.238 17.935 1.00 23.81 ATOM 2716 O ASN 2234 16.611 96.192 18.662 1.00 18.78 ATOM 2717 N ALA 2235 18.486 97.245 17.957 1.00 25.64 ATOM 2718 GA ALA 2235 18.330 98.370 18.875 1.00 25.56 ATOM 2719 CB ALA 2235 19.504 99.358 18.709 1.00 22.70 ATOM 2720 C ALA 2235 17.005 99.099 18.684 1.00 25.28 ATOM 2721 O ALA 2235 16.627 99.933 19.511 1.00 28.40 ATOM 2722 N TYR 2236 16.279 98.773 17.619 1.00 23.67 ATOM 2723 CA TYR 2236 15.031 99.472 17.364 1.00 22.28 ATOM 2724 CB TYR 2236 15.168 100.255 16.073 1.00 23.73 ATOM 2725 CG TYR 2236 16.263 101.272 16.171 1.00 27.43 ATOM 2726 CD1 TYR 2236 17.591 100.918 15.944 1.00 31.32 ATOM 2727 CE1 TYR 2236 18.616 101.851 16.106 1.00 35.39 ATOM 2728 CD2 TYR 2236 15.982 102.579 16.562 1.00 28.54 ATOM 2729 CE2 TYR 2236 16.989 103.513 16.728 1.00 32.14 ATOM 2730 CZ TYR 2236 18.303 103.147 16.501 1.00 34.04 ATOM 2731 OH TYR 2236 19.298 104.076 16.671 1.00 35.11 ATOM 2732 C TYR 2236 13.734 98.691 17.354 1.00 20.69 ATOM 2733 O TYR 2236 12.683 99.240 17.027 1.00 22.13 ATOM 2734 N GLY 2237 13.791 97.420 17.713 1.00 18.34 ATOM 2735 CA GLY 2237 12.579 96.641 17.735 1.00 18.42 ATOM 2736 C GLY 2237 12.819 95.154 17.719 1.00 20.66 ATOM 2737 O GLY 2237 13.910 94.685 17.397 1.00 22.88 ATOM 2738 N SER 2238 11.779 94.410 18.069 1.00 21.30 ATOM 2739 CA SER 2238 11.855 92.967 18.091 1.00 24.16 ATOM 2740 CB SER 2238 12.138 92.473 19.503 1.00 27.04 ATOM 2741 OG SER 2238 12.004 91.061 19.554 1.00 33.65 ATOM 2742 C SER 2238 10.549 92.368 17.619 1.00 24.16 ATOM 2743 O SER 2238 9.478 92.735 18.094 1.00 24.16 ATOM 2744 N ILE 2239 10.636 91.443 16.679 1.00 25.17 ATOM 2745 CA ILE 2239 9.438 90.793 16.174 1.00 25.95 ATOM 2746 CB ILE 2239 9.250 91.054 14.643 1.00 23.90 ATOM 2747 CG2 ILE 2239 9.041 92.538 14.405 1.00 22.25 ATOM 2748 CG1 ILE 2239 10.477 90.591 13.845 1.00 22.27 ATOM 2749 CD1 ILE 2239 10.375 90.865 12.338 1.00 15.87 ATOM 2750 C ILE 2239 9.606 89.314 16.463 1.00 26.02 ATOM 2751 O ILE 2239 10.711 88.860 16.730 1.00 26.85 ATOM 2752 N ASN 2240 8.515 88.566 16.440 1.00 27.54 ATOM 2753 CA ASN 2240 8.599 87.137 16.708 1.00 28.36 ATOM 2754 CB ASN 2240 8.358 86.858 18.184 1.00 31.11 ATOM 2755 CG ASN 2240 7.026 87.392 18.654 1.00 34.41 ATOM 2756 OD1 ASN 2240 6.017 87.293 17.950 1.00 39.95 ATOM 2757 ND2 ASN 2240 7.008 87.958 19.852 1.00 36.18 ATOM 2758 C ASN 2240 7.577 86.360 15.898 1.00 27.32 ATOM 2759 O ASN 2240 6.670 86.931 15.289 1.00 26.19 ATOM 2760 N HIS 2241 7.728 85.045 15.909 1.00 26.23 ATOM 2761 CA HIS 2241 6.823 84.174 15.183 1.00 24.63 ATOM 2762 CB HIS 2241 7.191 84.145 13.698 1.00 27.93 ATOM 2763 CG HIS 2241 6.198 83.418 12.851 1.00 29.56 ATOM 2764 CD2 HIS 2241 6.302 82.271 12.141 1.00 30.41 ATOM 2765 ND1 HIS 2241 4.894 83.840 12.708 1.00 28.42 ATOM 2766 CE1 HIS 2241 4.237 82.984 11.950 1.00 28.77 ATOM 2767 NE2 HIS 2241 5.069 82.021 11.593 1.00 30.81 ATOM 2768 C HIS 2241 6.977 82.798 15.775 1.00 20.79 ATOM 2769 O HIS 2241 8.080 82.406 16.124 1.00 23.73 ATOM 2770 N THR 2242 5.883 82.068 15.905 1.00 18.57 ATOM 2771 CA THR 2242 5.967 80.732 16.469 1.00 19.34 ATOM 2772 CB THR 2242 5.175 80.606 17.786 1.00 18.92 ATOM 2773 OG1 THR 2242 5.654 81.569 18.737 1.00 19.94 ATOM 2774 CG2 THR 2242 5.351 79.197 18.370 1.00 16.55 ATOM 2775 C THR 2242 5.441 79.678 15.515 1.00 19.37 ATOM 2776 O THR 2242 4.439 79.889 14.846 1.00 19.56 ATOM 2777 N TYR 2243 6.131 78.545 15.467 1.00 19.59 ATOM 2778 CA TYR 2243 5.744 77.426 14.626 1.00 18.65 ATOM 2779 CB TYR 2243 6.871 77.032 13.671 1.00 18.22 ATOM 2780 CG TYR 2243 7.181 78.003 12.559 1.00 21.98 ATOM 2781 CD1 TYR 2243 8.262 78.879 12.653 1.00 26.03 ATOM 2782 CE1 TYR 2243 8.585 79.749 11.605 1.00 27.45 ATOM 2783 CD2 TYR 2243 6.421 78.020 11.392 1.00 22.51 ATOM 2784 CE2 TYR 2243 6.728 78.879 10.336 1.00 23.43 ATOM 2785 CZ TYR 2243 7.808 79.745 10.445 1.00 27.97 ATOM 2786 OH TYR 2243 8.102 80.614 9.403 1.00 26.48 ATOM 2787 C TYR 2243 5.439 76.206 15.489 1.00 20.69 ATOM 2788 O TYR 2243 6.165 75.904 16.432 1.00 20.77 ATOM 2789 N ALA 2244 4.364 75.494 15.171 1.00 24.28 ATOM 2790 CA ALA 2244 4.044 74.268 15.904 1.00 24.29 ATOM 2791 CB ALA 2244 2.528 74.036 15.923 1.00 21.88 ATOM 2792 C ALA 2244 4.749 73.145 15.132 1.00 23.11 ATOM 2793 O ALA 2244 4.847 73.204 13.903 1.00 22.54 ATOM 2794 N LEU 2245 5.286 72.155 15.831 1.00 21.86 ATOM 2795 CA LEU 2245 5.922 71.053 15.122 1.00 22.62 ATOM 2796 CB LEU 2Z45 7.443 71.051 15.287 1.00 18.99 ATOM 2797 CG LEU 2245 8.147 70.207 14.204 1.00 17.70 ATOM 2798 CD1 LEU 2245 9.642 70.451 14.227 1.00 21.67 ATOM 2799 CD2 LEU 2245 7.870 68.761 14.398 1.00 12.29 ATOM 2800 C LEU 2245 5.362 69.730 15.612 1.00 24.97 ATOM 2801 O LEU 2245 5.443 69.393 16.801 1.00 26.93 ATOM 2802 N ASP 2246 4.769 68.982 14.698 1.00 23.77 ATOM 2803 CA ASP 2246 4.244 67.695 15.080 1.00 26.78 ATOM 2804 CB ASP 2246 2.742 67.632 14.827 1.00 32.54 ATOM 2805 CG ASP 2246 2.116 66.391 15.412 1.00 38.06 ATOM 2806 OD1 ASP 2246 2.401 66.068 16.586 1.00 43.40 ATOM 2807 OD2 ASP 2246 1.334 65.733 14.700 1.00 43.40 ATOM 2808 C ASP 2246 4.989 66.639 14.283 1.00 24.87 ATOM 2809 O ASP 2246 5.301 66.843 13.109 1.00 24.14 ATOM 2810 N VAL 2247 5.289 65.523 14.939 1.00 23.50 ATOM 2811 CA VAL 2247 6.026 64.419 14.326 1.00 22.60 ATOM 2812 CB VAL 2247 7.394 64.245 15.014 1.00 24.33 ATOM 2813 CG1 VAL 2247 8.164 63.064 14.404 1.00 22.90 ATOM 2814 CG2 VAL 2247 8.190 65.548 14.897 1.00 25.31 ATOM 2815 C VAL 2247 5.250 63.123 14.457 1.00 20.96 ATOM 2816 O VAL 2247 4.716 62.831 15.518 1.00 23.24 ATOM 2817 N VAL 2248 5.185 62.342 13.385 1.00 21.02 ATOM 2818 CA VAL 2248 4.459 61.071 13.428 1.00 20.10 ATOM 2819 CB VAL 2248 3.209 61.096 12.523 1.00 22.52 ATOM 2820 CG1 VAL 2248 2.433 59.817 12.680 1.00 24.17 ATOM 2821 CG2 VAL 2248 2.337 62.271 12.875 1.00 24.94 ATOM 2822 C VAL 2248 5.336 59.929 12.960 1.00 18.71 ATOM 2823 O VAL 2248 5.854 59.952 11.843 1.00 17.85 ATOM 2824 N GLU 2249 5.499 58.931 13.821 1.00 19.07 ATOM 2825 CA GLU 2249 6.306 57.763 13.491 1.00 20.26 ATOM 2826 CB GLU 2249 6.647 56.980 14.764 1.00 23.63 ATOM 2827 CG GLU 2249 7.421 57.804 15.789 1.00 29.31 ATOM 2828 CD GLU 2249 7.621 57.095 17.110 1.00 30.62 ATOM 2829 OE1 GLU 2249 6.622 56.608 17.688 1.00 31.42 ATOM 2830 OE2 GLU 2249 8.783 57.043 17.573 1.00 35.73 ATOM 2831 C GLU 2249 5.478 56.904 12.553 1.00 20.02 ATOM 2832 O GLU 2249 4.380 56.483 12.910 1.00 21.25 ATOM 2833 N ARG 2250 5.991 56.667 11.348 1.00 19.31 ATOM 2834 CA ARG 2250 5.282 55.855 10.358 1.00 19.27 ATOM 2835 CB ARG 2250 5.516 56.389 8.929 1.00 14.30 ATOM 2836 CG ARG 2250 5.039 57.822 8.660 1.00 12.43 ATOM 2837 CD ARG 2250 3.621 58.089 9.162 1.00 12.56 ATOM 2838 NE ARG 2250 2.601 57.339 8.431 1.00 16.48 ATOM 2839 CZ ARG 2250 2.203 57.609 7.189 1.00 18.36 ATOM 2840 NH1 ARG 2250 2.729 58.622 6.501 1.00 14.94 ATOM 2841 NH2 ARG 2250 1.277 56.851 6.627 1.00 18.04 ATOM 2842 C ARG 2250 5.732 54.396 10.443 1.00 20.00 ATOM 2843 O ARG 2250 6.919 54.122 10.617 1.00 21.86 ATOM 2844 N ALA 2251 4.788 53.464 10.309 1.00 19.84 ATOM 2845 CA ALA 2251 5.104 52.039 10.388 1.00 17.49 ATOM 2846 CB ALA 2251 4.314 51.415 11.554 1.00 15.22 ATOM 2847 C ALA 2251 4.814 51.289 9.076 1.00 17.93 ATOM 2848 O ALA 2251 3.702 50.785 8.898 1.00 19.93 ATOM 2849 N PRO 2252 5.806 51.225 8.132 1.00 19.12 ATOM 2850 CD PRO 2252 7.021 52.074 8.124 1.00 16.50 ATOM 2851 CA PRO 2252 5.671 50.538 6.829 1.00 17.21 ATOM 2852 CB PRO 2252 6.666 51.290 5.945 1.00 16.08 ATOM 2853 CG PRO 2252 7.780 51.571 6.901 1.00 13.86 ATOM 2854 C PRO 2252 5.948 49.025 6.834 1.00 17.45 ATOM 2855 O PRO 2252 6.942 48.554 6.280 1.00 17.02 ATOM 2856 N HIS 2253 5.056 48.272 7.463 1.00 18.62 ATOM 2857 CA HIS 2253 5.165 46.822 7.543 1.00 20.04 ATOM 2858 CB HIS 2253 5.589 46.388 8.951 1.00 24.45 ATOM 2859 CG HIS 2253 6.666 47.238 9.545 1.00 29.28 ATOM 2860 CD2 HIS 2253 6.641 48.105 10.585 1.00 28.96 ATOM 2861 ND1 HIS 2253 7.938 47.313 9.010 1.00 30.02 ATOM 2862 CE1 HIS 2253 8.646 48.197 9.691 1.00 29.21 ATOM 2863 NE2 HIS 2253 7.884 48.693 10.650 1.00 32.56 ATOM 2864 C HIS 2253 3.749 46.333 7.291 1.00 21.36 ATOM 2865 O HIS 2253 2.817 47.138 7.261 1.00 20.08 ATOM 2866 N ARG 2254 3.572 45.026 7.109 1.00 22.26 ATOM 2867 CA ARG 2254 2.232 44.505 6.891 1.00 20.97 ATOM 2868 CB ARG 2254 2.268 43.046 6.396 1.00 24.88 ATOM 2869 CG ARG 2254 2.584 41.956 7.436 1.00 25.31 ATOM 2870 CD ARG 2254 4.068 41.905 7.797 1.00 31.05 ATOM 2871 NE ARG 2254 4.655 40.568 7.641 1.00 33.67 ATOM 2872 CZ ARG 2254 4.229 39.466 8.258 1.00 32.88 ATOM 2873 NH1 ARG 2254 3.201 39.509 9.089 1.00 35.12 ATOM 2874 NH2 ARG 2254 4.846 38.315 8.053 1.00 31.58 ATOM 2875 C ARG 2254 1.547 44.599 8.246 1.00 19.97 ATOM 2876 O ARG 2254 2.181 44.920 9.247 1.00 19.38 ATOM 2877 N PRO 2255 0.245 44.334 8.302 1.00 18.97 ATOM 2878 CD PRO 2255 −0.704 43.973 7.236 1.00 17.39 ATOM 2879 CA PRO 2255 −0.423 44.424 9.604 1.00 17.68 ATOM 2880 CB PRO 2255 −1.884 44.080 9.266 1.00 19.06 ATOM 2881 CG PRO 2255 −2.003 44.461 7.810 1.00 17.45 ATOM 2882 C PRO 2255 0.175 43.451 10.635 1.00 16.18 ATOM 2883 O PRO 2255 0.819 42.465 10.266 1.00 10.22 ATOM 2884 N ILE 2256 −0.063 43.738 11.917 1.00 17.71 ATOM 2885 CA ILE 2256 0.401 42.905 13.031 1.00 20.17 ATOM 2886 CB ILE 2256 1.310 43.684 14.007 1.00 21.84 ATOM 2887 CG2 ILE 2256 1.579 42.836 15.244 1.00 22.63 ATOM 2888 CG1 ILE 2256 2.624 44.084 13.329 1.00 25.56 ATOM 2889 CD1 ILE 2256 3.525 44.970 14.209 1.00 24.01 ATOM 2890 C ILE 2256 −0.812 42.465 13.842 1.00 21.08 ATOM 2891 O ILE 2256 −1.599 43.304 14.280 1.00 22.25 ATOM 2892 N LEU 2257 −0.972 41.162 14.046 1.00 21.14 ATOM 2893 CA LEU 2257 −2.099 40.673 14.836 1.00 23.57 ATOM 2894 CB LEU 2257 −2.692 39.399 14.227 1.00 22.98 ATOM 2895 CG LEU 2257 −3.161 39.361 12.773 1.00 20.53 ATOM 2896 CD1 LEU 2257 −4.123 38.185 12.587 1.00 18.03 ATOM 2897 CD2 LEU 2257 −3.859 40.645 12.429 1.00 20.37 ATOM 2898 C LEU 2257 −1.620 40.356 16.250 1.00 26.64 ATOM 2899 O LEU 2257 −0.462 39.973 16.451 1.00 30.59 ATOM 2900 N GLN 2258 −2.499 40.508 17.235 1.00 27.95 ATOM 2901 CA GLN 2258 −2.114 40.217 18.609 1.00 26.66 ATOM 2902 CB GLN 2258 −3.163 40.734 19.587 1.00 27.37 ATOM 2903 CG GLN 2258 −2.854 40.381 21.026 1.00 31.81 ATOM 2904 CD GLN 2258 −1.476 40.870 21.458 1.00 36.00 ATOM 2905 OE1 GLN 2258 −1.223 42.080 21.521 1.00 36.76 ATOM 2906 NE2 GLN 2258 −0.574 39.929 21.751 1.00 35.05 ATOM 2907 C GLN 2258 −1.969 38.720 18.770 1.00 25.32 ATOM 2908 O GLN 2258 −2.907 37.978 18.506 1.00 28.43 ATOM 2909 N ALA 2259 −0.790 38.278 19.192 1.00 25.30 ATOM 2910 CA ALA 2259 −0.520 36.853 19.390 1.00 24.71 ATOM 2911 CB ALA 2259 0.883 36.670 19.940 1.00 23.59 ATOM 2912 C ALA 2259 −1.544 36.230 20.342 1.00 25.40 ATOM 2913 O ALA 2259 −1.919 36.836 21.351 1.00 28.18 ATOM 2914 N GLY 2260 −2.001 35.023 20.022 1.00 23.57 ATOM 2915 CA GLY 2260 −2.987 34.372 20.867 1.00 22.17 ATOM 2916 C GLY 2260 −4.408 34.591 20.373 1.00 21.74 ATOM 2917 O GLY 2260 −5.311 33.807 20.682 1.00 21.27 ATOM 2918 N LEU 2261 −4.616 35.656 19.604 1.00 20.57 ATOM 2919 CA LEU 2261 −5.943 35.958 19.078 1.00 21.16 ATOM 2920 CB LEU 2261 −6.304 37.416 19.373 1.00 21.27 ATOM 2921 CG LEU 2261 −6.347 37.757 20.865 1.00 22.44 ATOM 2922 CD1 LEU 2261 −6.741 39.215 21.078 1.00 20.50 ATOM 2923 CD2 LEU 2261 −7.346 36.837 21.545 1.00 22.48 ATOM 2924 C LEU 2261 −6.034 35.674 17.574 1.00 19.70 ATOM 2925 O LEU 2261 −5.152 36.057 16.805 1.00 20.74 ATOM 2926 N PRO 2262 −7.111 34.998 17.139 1.00 17.08 ATOM 2927 CD PRO 2262 −7.354 34.649 15.729 1.00 16.05 ATOM 2928 CA PRO 2262 −8.192 34.503 17.999 1.00 16.51 ATOM 2929 CB PRO 2262 −9.293 34.169 17.001 1.00 14.07 ATOM 2930 CG PRO 2262 −8.508 33.673 15.828 1.00 16.76 ATOM 2931 C PRO 2262 −7.704 33.285 18.762 1.00 17.26 ATOM 2932 O PRO 2262 −6.675 32.708 18.415 1.00 20.94 ATOM 2933 N ALA 2263 −8.426 32.893 19.800 1.00 15.69 ATOM 2934 CA ALA 2263 −8.027 31.734 20.592 1.00 14.01 ATOM 2935 CB ALA 2263 −7.831 32.151 22.060 1.00 7.68 ATOM 2936 C ALA 2263 −9.059 30.602 20.496 1.00 13.49 ATOM 2937 O ALA 2263 −10.267 30.852 20.374 1.00 11.10 ATOM 2938 N ASN 2264 −8.579 29.364 20.547 1.00 13.00 ATOM 2939 CA ASN 2264 −9.467 28.212 20.492 1.00 15.21 ATOM 2940 CB ASN 2264 −8.732 26.932 20.806 1.00 9.73 ATOM 2941 CG ASN 2264 −7.559 26.746 19.947 1.00 13.05 ATOM 2942 OD1 ASN 2264 −7.503 27.281 18.833 1.00 18.74 ATOM 2943 ND2 ASN 2264 −6.598 25.977 20.428 1.00 12.71 ATOM 2944 C ASN 2264 −10.583 28.339 21.495 1.00 19.33 ATOM 2945 O ASN 2264 −10.459 29.022 22.503 1.00 19.67 ATOM 2946 N LYS 2265 −11.674 27.649 21.212 1.00 24.50 ATOM 2947 CA LYS 2265 −12.814 27.669 22.085 1.00 27.32 ATOM 2948 CB LYS 2265 −13.738 28.819 21.721 1.00 28.46 ATOM 2949 CG LYS 2265 −13.241 30.174 22.150 1.00 32.13 ATOM 2950 CD LYS 2265 −14.378 30.948 22.789 1.00 36.02 ATOM 2951 CE LYS 2265 −14.977 30.158 23.950 1.00 36.92 ATOM 2952 NZ LYS 2265 −16.151 30.833 24.580 1.00 40.08 ATOM 2953 C LYS 2265 −13.553 26.367 21.930 1.00 30.50 ATOM 2954 O LYS 2265 −13.573 25.776 20.848 1.00 31.20 ATOM 2955 N THR 2266 −14.133 25.915 23.035 1.00 33.40 ATOM 2956 CA THR 2266 −14.928 24.699 23.073 1.00 32.79 ATOM 2957 CB THR 2266 −14.324 23.639 24.013 1.00 31.95 ATOM 2958 OG1 THR 2266 −13.009 23.280 23.567 1.00 30.70 ATOM 2959 CG2 THR 2266 −15.182 22.396 24.019 1.00 34.16 ATOM 2960 C THR 2266 −16.248 25.197 23.642 1.00 34.06 ATOM 2961 O THR 2266 −16.261 25.945 24.619 1.00 33.77 ATOM 2962 N VAL 2267 −17.354 24.816 23.012 1.00 35.60 ATOM 2963 CA VAL 2267 −18.670 25.249 23.463 1.00 35.90 ATOM 2964 CB VAL 2267 −19.141 26.520 22.704 1.00 38.17 ATOM 2965 CG1 VAL 2267 −18.149 27.657 22.924 1.00 38.27 ATOM 2966 CG2 VAL 2267 −19.279 26.218 21.210 1.00 36.88 ATOM 2967 C VAL 2267 −19.700 24.150 23.250 1.00 35.89 ATOM 2968 O VAL 2267 −19.446 23.163 22.553 1.00 36.10 ATOM 2969 N ALA 2268 −20.869 24.338 23.850 1.00 34.73 ATOM 2970 CA ALA 2268 −21.946 23.369 23.751 1.00 33.00 ATOM 2971 CB ALA 2268 −22.767 23.370 25.025 1.00 27.28 ATOM 2972 C ALA 2268 −22.827 23.708 22.574 1.00 34.99 ATOM 2973 O ALA 2268 −22.923 24.879 22.179 1.00 34.44 ATOM 2974 N LEU 2269 −23.457 22.681 22.006 1.00 35.47 ATOM 2975 CA LEU 2269 −24.357 22.882 20.883 1.00 35.90 ATOM 2976 CB LEU 2269 −25.110 21.584 20.564 1.00 39.22 ATOM 2977 CG LEU 2269 −24.353 20.443 19.867 1.00 42.42 ATOM 2978 CD1 LEU 2269 −25.140 19.154 20.022 1.00 42.54 ATOM 2979 CD2 LEU 2269 −24.136 20.771 18.386 1.00 41.55 ATOM 2980 C LEU 2269 −25.352 23.967 21.280 1.00 34.29 ATOM 2981 O LEU 2269 −25.940 23.905 22.357 1.00 32.80 ATOM 2982 N GLY 2270 −25.517 24.968 20.419 1.00 34.69 ATOM 2983 CA GLY 2270 −26.459 26.037 20.699 1.00 38.43 ATOM 2984 C GLY 2270 −25.838 27.301 21.254 1.00 41.50 ATOM 2985 O GLY 2270 −26.441 28.376 21.184 1.00 41.72 ATOM 2986 N SER 2271 −24.632 27.173 21.805 1.00 43.37 ATOM 2987 CA SER 2271 −23.918 28.305 22.380 1.00 43.17 ATOM 2988 CB SER 2271 −22.628 27.834 23.067 1.00 47.15 ATOM 2989 OG SER 2271 −22.855 26.791 23.999 1.00 54.22 ATOM 2990 C SER 2271 −23.528 29.297 21.292 1.00 42.24 ATOM 2991 O SER 2271 −23.167 28.902 20.179 1.00 41.28 ATOM 2992 N ASN 2272 −23.600 30.583 21.611 1.00 39.22 ATOM 2993 CA ASN 2272 −23.181 31.593 20.654 1.00 36.32 ATOM 2994 CB ASN 2272 −23.903 32.906 20.906 1.00 38.38 ATOM 2995 CG ASN 2272 −25.394 32.722 20.967 1.00 43.80 ATOM 2996 OD1 ASN 2272 −25.965 31.944 20.193 1.00 43.87 ATOM 2997 ND2 ASN 2272 −26.046 33.435 21.887 1.00 48.37 ATOM 2998 C ASN 2272 −21.694 31.736 20.924 1.00 32.84 ATOM 2999 O ASN 2272 −21.222 31.390 22.007 1.00 30.83 ATOM 3000 N VAL 2273 −20.944 32.228 19.951 1.00 28.07 ATOM 3001 CA VAL 2273 −19.515 32.351 20.153 1.00 23.37 ATOM 3002 CB VAL 2273 −18.776 31.080 19.666 1.00 19.24 ATOM 3003 CG1 VAL 2273 −19.577 30.396 18.614 1.00 20.51 ATOM 3004 CG2 VAL 2273 −17.415 31.434 19.115 1.00 19.81 ATOM 3005 C VAL 2273 −18.950 33.569 19.478 1.00 23.80 ATOM 3006 O VAL 2273 −19.504 34.065 18.502 1.00 25.04 ATOM 3007 N GLU 2274 −17.844 34.058 20.026 1.00 23.55 ATOM 3008 CA GLU 2274 −17.179 35.231 19.496 1.00 23.82 ATOM 3009 CB GLU 2274 −17.520 36.465 20.340 1.00 26.77 ATOM 3010 CG GLU 2274 −18.990 36.883 20.323 1.00 31.02 ATOM 3011 CD GLU 2274 −19.278 38.065 21.256 1.00 36.36 ATOM 3012 OE1 GLU 2274 −19.314 37.871 22.493 1.00 38.44 ATOM 3013 CE2 GLU 2274 −19.461 39.196 20.754 1.00 38.11 ATOM 3014 C GLU 2274 −15.677 35.019 19.500 1.00 23.04 ATOM 3015 O GLU 2274 −15.092 34.559 20.481 1.00 23.32 ATOM 3016 N PHE 2275 −15.056 35.334 18.379 1.00 22.12 ATOM 3017 CA PHE 2275 −13.617 35.228 18.266 1.00 23.08 ATOM 3018 CB PHE 2275 −13.227 34.497 16.989 1.00 23.46 ATOM 3019 CG PHE 2275 −13.513 33.025 17.016 1.00 24.47 ATOM 3020 CD1 PHE 2275 −12.814 32.188 17.876 1.00 20.25 ATOM 3021 CD2 PHE 2275 −14.462 32.469 16.155 1.00 22.69 ATOM 3022 CE1 PHE 2275 −13.046 30.814 17.881 1.00 22.65 ATOM 3023 CE2 PHE 2275 −14.704 31.095 16.151 1.00 23.25 ATOM 3024 CZ PHE 2275 −13.994 30.264 17.017 1.00 22.55 ATOM 3025 C PHE 2275 −13.152 36.678 18.192 1.00 24.50 ATOM 3026 O PHE 2275 −13.847 37.518 17.612 1.00 22.70 ATOM 3027 N MET 2276 −11.996 36.972 18.792 1.00 23.05 ATOM 3028 CA MET 2276 −11.450 38.323 18.783 1.00 19.92 ATOM 3029 CB MET 2276 −11.051 38.767 20.188 1.00 23.46 ATOM 3030 CG MET 2276 −12.105 38.548 21.248 1.00 28.97 ATOM 3031 SD MET 2276 −11.548 39.133 22.847 1.00 35.29 ATOM 3032 CE MET 2276 −12.366 40.757 22.877 1.00 35.62 ATOM 3033 C MET 2276 −10.224 38.352 17.914 1.00 17.93 ATOM 3034 O MET 2276 −9.613 37.330 17.644 1.00 17.08 ATOM 3035 N CYS 2277 −9.857 39.541 17.486 1.00 19.16 ATOM 3036 CA CYS 2277 −8.693 39.705 16.647 1.00 21.43 ATOM 3037 C CYS 2277 −8.246 41.148 16.852 1.00 22.01 ATOM 3038 O CYS 2277 −9.059 42.072 16.737 1.00 21.65 ATOM 3039 CB CYS 2277 −9.080 39.461 15.189 1.00 23.00 ATOM 3040 SG CYS 2277 −7.702 39.378 13.994 1.00 33.53 ATOM 3041 N LYS 2278 −6.969 41.334 17.178 1.00 20.12 ATOM 3042 CA LYS 2278 −6.420 42.663 17.398 1.00 21.75 ATOM 3043 CB LYS 2278 −5.748 42.736 18.772 1.00 23.93 ATOM 3044 CG LYS 2278 −6.257 43.847 19.688 1.00 26.77 ATOM 3045 CD LYS 2278 −5.526 45.177 19.459 1.00 32.15 ATOM 3046 CE LYS 2278 −5.866 46.236 20.538 1.00 35.30 ATOM 3047 NZ LYS 2278 −5.502 45.849 21.953 1.00 36.06 ATOM 3048 C LYS 2278 −5.411 42.951 16.299 1.00 22.73 ATOM 3049 O LYS 2278 −4.437 42.218 16.122 1.00 24.81 ATOM 3050 N VAL 2279 −5.648 44.031 15.565 1.00 22.86 ATOM 3051 CA VAL 2279 −4.785 44.410 14.453 1.00 20.11 ATOM 3052 CB VAL 2279 −5.608 44.423 13.123 1.00 17.48 ATOM 3053 CG1 VAL 2279 −4.723 44.767 11.954 1.00 18.12 ATOM 3054 CG2 VAL 2279 −6.274 43.093 12.909 1.00 12.42 ATOM 3055 C VAL 2279 −4.478 45.800 14.657 1.00 20.73 ATOM 3056 O VAL 2279 −4.820 46.684 15.235 1.00 19.88 ATOM 3057 N TYR 2280 −2.931 45.971 14.214 1.00 19.94 ATOM 3058 CA TYR 2280 −2.259 47.266 14.260 1.00 20.90 ATOM 3059 CB TYR 2280 −1.065 47.313 15.211 1.00 22.44 ATOM 3060 CG TYR 2280 −0.219 48.575 14.960 1.00 24.80 ATOM 3061 CD1 TYR 2280 −0.544 49.802 15.568 1.00 24.50 ATOM 3062 CE1 TYR 2280 0.139 50.979 15.239 1.00 21.31 ATOM 3063 CD2 TYR 2280 0.826 48.569 14.021 1.00 21.65 ATOM 3064 CE2 TYR 2280 1.509 49.746 13.686 1.00 19.85 ATOM 3065 CZ TYR 2280 1.161 50.939 14.296 1.00 21.86 ATOM 3066 OH TYR 2280 1.823 52.097 13.945 1.00 25.77 ATOM 3067 C TYR 2280 −1.724 47.475 12.858 1.00 20.64 ATOM 3068 O TYR 2280 −1.089 46.585 12.295 1.00 23.29 ATOM 3069 N SER 2281 −1.930 48.656 12.303 1.00 18.64 ATOM 3070 CA SER 2281 −1.466 48.882 10.954 1.00 21.14 ATOM 3071 CB SER 2281 −2.374 48.077 10.001 1.00 22.58 ATOM 3072 OG SER 2281 −2.013 48.208 8.639 1.00 23.27 ATOM 3073 C SER 2281 −1.501 50.367 10.616 1.00 21.23 ATOM 3074 O SER 2281 −2.566 50.977 10.658 1.00 23.17 ATOM 3075 N ASP 2282 −0.346 50.952 10.301 1.00 20.96 ATOM 3076 CA ASP 2282 −0.310 52.366 9.941 1.00 19.46 ATOM 3077 CB ASP 2282 1.125 52.806 9.624 1.00 20.53 ATOM 3078 CG ASP 2282 1.201 54.230 9.109 1.00 20.83 ATOM 3079 OD1 ASP 2282 2.319 54.780 9.011 1.00 18.07 ATOM 3080 OD2 ASP 2282 0.143 54.799 8.792 1.00 23.14 ATOM 3081 C ASP 2282 −1.249 52.531 8.736 1.00 18.46 ATOM 3082 O ASP 2282 −2.273 53.217 8.841 1.00 19.78 ATOM 3083 N PRO 2283 −0.930 51.912 7.577 1.00 17.09 ATOM 3084 CD PRO 2283 0.299 51.262 7.094 1.00 15.57 ATOM 3085 CA PRO 2283 −1.880 52.098 6.470 1.00 16.82 ATOM 3086 CB PRO 2283 −1.123 51.546 5.264 1.00 14.12 ATOM 3087 CG PRO 2283 −0.186 50.572 5.853 1.00 14.51 ATOM 3088 C PRO 2283 −3.164 51.333 6.777 1.00 17.33 ATOM 3089 O PRO 2283 −3.134 50.362 7.529 1.00 18.94 ATOM 3090 N GLN 2284 −4.292 51.773 6.228 1.00 18.73 ATOM 3091 CA GLN 2284 −5.568 51.100 6.494 1.00 21.43 ATOM 3092 CB GLN 2284 −6.696 51.736 5.689 1.00 24.32 ATOM 3093 CG GLN 2284 −7.175 53.030 6.274 1.00 30.25 ATOM 3094 CD GLN 2284 −7.677 52.849 7.685 1.00 33.16 ATOM 3095 OE1 GLN 2284 −7.553 53.749 8.518 1.00 39.37 ATOM 3096 NE2 GLN 2284 −8.255 51.685 7.963 1.00 29.48 ATOM 3097 C GLN 2284 −5.572 49.606 6.223 1.00 20.62 ATOM 3098 O GLN 2284 −5.324 49.161 5.109 1.00 21.34 ATOM 3099 N PRO 2285 −5.864 48.808 7.252 1.00 20.67 ATOM 3100 CD PRO 2285 −6.022 49.206 8.663 1.00 22.25 ATOM 3101 CA PRO 2285 −5.905 47.350 7.122 1.00 20.42 ATOM 3102 CB PRO 2285 −5.621 46.883 8.540 1.00 18.80 ATOM 3103 CG PRO 2285 −6.401 47.878 9.337 1.00 20.07 ATOM 3104 C PRO 2285 −7.275 46.875 6.647 1.00 21.35 ATOM 3105 O PRO 2285 −8.301 47.483 6.956 1.00 19.43 ATOM 3106 N HIS 2286 −7.288 45.788 5.887 1.00 22.52 ATOM 3107 CA HIS 2286 −8.536 45.227 5.414 1.00 23.32 ATOM 3108 CB HIS 2286 −8.481 45.010 3.903 1.00 27.49 ATOM 3109 CG HIS 2286 −9.756 44.476 3.334 1.00 32.81 ATOM 3110 CD2 HIS 2286 −10.924 45.094 3.037 1.00 35.44 ATOM 3111 ND1 HIS 2286 −9.956 43.137 3.081 1.00 33.65 ATOM 3112 CE1 HIS 2286 −11.192 42.952 2.654 1.00 34.94 ATOM 3113 NE2 HIS 2286 −11.800 44.124 2.619 1.00 35.76 ATOM 3114 C HIS 2286 −8.661 43.904 6.154 1.00 21.23 ATOM 3115 O HIS 2286 −7.826 43.026 5.987 1.00 20.31 ATOM 3116 N ILE 2287 −9.691 43.768 6.981 1.00 19.86 ATOM 3117 CA ILE 2287 −9.862 42.558 7.773 1.00 21.24 ATOM 3118 CB ILE 2287 −10.142 42.888 9.277 1.00 19.88 ATOM 3119 CG2 ILE 2287 −10.647 41.653 10.001 1.00 20.88 ATOM 3120 CG1 ILE 2287 −8.859 43.337 9.978 1.00 20.91 ATOM 3121 CD1 ILE 2287 −8.405 44.721 9.624 1.00 25.87 ATOM 3122 C ILE 2287 −10.959 41.622 7.286 1.00 23.20 ATOM 3123 O ILE 2287 −12.073 42.049 6.994 1.00 24.53 ATOM 3124 N GLN 2288 −10.630 40.336 7.221 1.00 24.44 ATOM 3125 CA GLN 2288 −11.574 39.314 6.793 1.00 27.20 ATOM 3126 CB GLN 2288 −11.244 38.800 5.394 1.00 28.49 ATOM 3127 CG GLN 2288 −11.553 39.714 4.245 1.00 30.33 ATOM 3128 CD GLN 2288 −11.346 39.004 2.927 1.00 33.65 ATOM 3129 OE1 GLN 2288 −11.402 39.611 1.858 1.00 37.86 ATOM 3130 NE2 GLN 2288 −11.106 37.699 2.997 1.00 34.58 ATOM 3131 C GLN 2288 −11.497 38.122 7.713 1.00 27.19 ATOM 3132 O GLN 2288 −10.430 37.806 8.234 1.00 28.06 ATOM 3133 N TRP 2289 −12.625 37.457 7.911 1.00 26.54 ATOM 3134 CA TRP 2289 −12.634 36.253 8.722 1.00 28.32 ATOM 3135 CB TRP 2289 −13.750 36.299 9.761 1.00 25.38 ATOM 3136 CG TRP 2289 −13.409 37.180 10.925 1.00 27.68 ATOM 3137 CD2 TRP 2289 −12.744 36.787 12.136 1.00 27.55 ATOM 3138 CE2 TRP 2289 −12.626 37.947 12.943 1.00 26.89 ATOM 3139 CE3 TRP 2289 −12.237 35.571 12.614 1.00 24.06 ATOM 3140 CD1 TRP 2289 −13.656 38.520 11.046 1.00 27.89 ATOM 3141 NE1 TRP 2289 −13.189 38.986 12.258 1.00 25.77 ATOM 3142 CZ2 TRP 2289 −12.024 37.920 14.205 1.00 25.28 ATOM 3143 CZ3 TRP 2289 −11.643 35.547 13.864 1.00 23.82 ATOM 3144 CH2 TRP 2289 −11.542 36.717 14.647 1.00 25.25 ATOM 3145 C TRP 2289 −12.843 35.102 7.738 1.00 30.49 ATOM 3146 O TRP 2289 −13.627 35.228 6.794 1.00 30.51 ATOM 3147 N LEU 2290 −12.135 33.994 7.935 1.00 28.70 ATOM 3148 CA LEU 2290 −12.269 32.872 7.020 1.00 30.74 ATOM 3149 CB LEU 2290 −11.000 32.722 6.167 1.00 29.89 ATOM 3150 CG LEU 2290 −10.212 33.935 5.669 1.00 29.52 ATOM 3151 CD1 LEU 2290 −8.980 33.448 4.918 1.00 28.48 ATOM 3152 CD2 LEU 2290 −11.073 34.800 4.774 1.00 29.20 ATOM 3153 C LEU 2290 −12.521 31.541 7.718 1.00 32.74 ATOM 3154 O LEU 2290 −11.876 31.218 8.711 1.00 35.23 ATOM 3155 N LYS 2291 −13.456 30.762 7.186 1.00 32.99 ATOM 3156 CA LYS 2291 −13.726 29.441 7.729 1.00 33.14 ATOM 3157 CB LYS 2291 −15.224 29.138 7.695 1.00 33.79 ATOM 3158 CG LYS 2291 −15.591 27.702 8.118 1.00 35.06 ATOM 3159 CD LYS 2291 −15.159 27.402 9.548 1.00 38.44 ATOM 3160 CE LYS 2291 −15.732 26.092 10.073 1.00 40.01 ATOM 3161 NZ LYS 2291 −15.085 24.893 9.476 1.00 42.04 ATOM 3162 C LYS 2291 −12.978 28.455 6.833 1.00 33.08 ATOM 3163 O LYS 2291 −12.884 28.653 5.626 1.00 33.86 ATOM 3164 N HIS 2292 −12.423 27.406 7.417 1.00 33.75 ATOM 3165 CA HIS 2292 −1.715 26.419 6.621 1.00 36.27 ATOM 3166 CB HIS 2292 −10.565 25.839 7.437 1.00 36.83 ATOM 3167 CC HIS 2292 −9.474 26.827 7.704 1.00 40.26 ATOM 3168 CD2 HIS 2292 −9.432 27.902 8.527 1.00 42.43 ATOM 3169 ND1 HIS 2292 −8.277 26.818 7.024 1.00 41.03 ATOM 3170 CE1 HIS 2292 −7.541 27.844 7.413 1.00 40.49 ATOM 3171 NE2 HIS 2292 −8.220 28.518 8.325 1.00 42.70 ATOM 3172 C HIS 2292 −12.696 25.334 6.196 1.00 38.08 ATOM 3173 O HIS 2292 −13.502 24.868 7.000 1.00 39.31 ATOM 3174 N ILE 2293 −12.652 24.950 4.925 1.00 39.67 ATOM 3175 CA ILE 2293 −13.561 23.920 4.432 1.00 41.05 ATOM 3176 CB ILE 2293 −14.479 24.454 3.322 1.00 41.60 ATOM 3177 CG2 ILE 2293 −15.592 23.439 3.057 1.00 44.08 ATOM 3178 CG1 ILE 2293 −15.087 25.792 3.740 1.00 41.91 ATOM 3179 CD1 ILE 2293 −15.889 26.455 2.640 1.00 43.30 ATOM 3180 C ILE 2293 −12.799 22.730 3.875 1.00 39.31 ATOM 3181 O ILE 2293 −11.990 22.886 2.968 1.00 39.37 ATOM 3182 N ASN 2304 −1.041 23.913 −2.561 1.00 62.05 ATOM 3183 CA ASN 2304 −0.699 23.331 −1.272 1.00 64.32 ATOM 3184 CB ASN 2304 0.817 23.290 −1.124 1.00 67.23 ATOM 3185 CG ASN 2304 1.255 22.401 0.024 1.00 70.61 ATOM 3186 OD1 ASN 2304 0.870 21.221 0.110 1.00 72.36 ATOM 3187 ND2 ASN 2304 2.089 22.962 0.911 1.00 71.52 ATOM 3188 C ASN 2304 −1.281 24.209 −0.165 1.00 64.20 ATOM 3189 O ASN 2304 −0.764 24.302 0.942 1.00 64.52 ATOM 3190 N LEU 2305 −2.389 24.872 −0.490 1.00 63.72 ATOM 3191 CA LEU 2305 −3.067 25.756 0.442 1.00 62.02 ATOM 3192 CB LEU 2305 −3.184 27.154 −0.152 1.00 62.74 ATOM 3193 CG LEU 2305 −1.908 27.883 −0.565 1.00 62.44 ATOM 3194 CD1 LEU 2305 −2.319 29.112 −1.312 1.00 61.35 ATOM 3195 CD2 LEU 2305 −1.025 28.247 0.650 1.00 62.84 ATOM 3196 C LEU 2305 −4.473 25.244 0.704 1.00 61.44 ATOM 3197 O LEU 2305 −5.041 24.551 −0.133 1.00 62.02 ATOM 3198 N PRO 2306 −5.073 25.623 1.836 1.00 60.02 ATOM 3199 CD PRO 2306 −4.615 26.411 2.990 1.00 59.73 ATOM 3200 CA PRO 2306 −6.431 25.139 2.106 1.00 57.82 ATOM 3201 CB PRO 2306 −6.466 25.124 3.595 1.00 59.06 ATOM 3202 CG PRO 2306 −5.874 26.399 3.869 1.00 60.01 ATOM 3203 C PRO 2306 −7.546 26.011 1.593 1.00 56.58 ATOM 3204 O PRO 2306 −7.399 27.228 1.445 1.00 58.04 ATOM 3205 N TYR 2307 −8.688 25.369 1.388 1.00 55.64 ATOM 3206 CA TYR 2307 −9.885 26.056 0.936 1.00 53.48 ATOM 3207 CB TYR 2307 −10.933 25.076 0.417 1.00 56.98 ATOM 3208 CG TYR 2307 −10.416 23.924 −0.405 1.00 62.03 ATOM 3209 CD1 TYR 2307 −9.967 22.753 0.209 1.00 65.31 ATOM 3210 CE1 TYR 2307 −9.517 21.669 −0.544 1.00 66.92 ATOM 3211 CD2 TYR 2307 −10.401 23.990 −1.800 1.00 63.17 ATOM 3212 CE2 TYR 2307 −9.952 22.915 −2.565 1.00 65.21 ATOM 3213 CZ TYR 2307 −9.511 21.758 −1.929 1.00 67.11 ATOM 3214 OH TYR 2307 −9.067 20.689 −2.671 1.00 67.96 ATOM 3215 C TYR 2307 −10.537 26.824 2.082 1.00 49.68 ATOM 3216 O TYR 2307 −10.633 26.335 3.207 1.00 49.15 ATOM 3217 N VAL 2308 −11.029 28.017 1.789 1.00 45.52 ATOM 3218 CA VAL 2308 −11.660 28.826 2.815 1.00 43.00 ATOM 3219 CB VAL 2308 −10.746 29.992 3.239 1.00 41.70 ATOM 3220 CG1 VAL 2308 −9.441 29.451 3.779 1.00 37.17 ATOM 3221 CG2 VAL 2308 −10.487 30.931 2.052 1.00 40.99 ATOM 3222 C VAL 2308 −12.978 29.390 2.331 1.00 41.87 ATOM 3223 O VAL 2308 −13.292 29.337 1.149 1.00 42.67 ATOM 3224 N GLN 2309 −13.739 29.935 3.264 1.00 41.93 ATOM 3225 CA GLN 2309 −15.021 30.520 2.963 1.00 42.91 ATOM 3226 CB GLN 2309 −16.127 29.659 3.562 1.00 44.89 ATOM 3227 CG GLN 2309 −7.516 30.053 3.136 1.00 52.27 ATOM 3228 CD GLN 2309 −18.587 29.456 4.026 1.00 56.02 ATOM 3229 OE1 GLN 2309 −18.606 28.247 4.283 1.00 57.05 ATOM 3230 NE2 GLN 2309 −19.491 30.305 4.503 1.00 58.93 ATOM 3231 C GLN 2309 −15.015 31.892 3.625 1.00 42.49 ATOM 3232 O GLN 2309 −14.979 31.989 4.851 1.00 43.27 ATOM 3233 N ILE 2310 −15.011 32.950 2.824 1.00 40.11 ATOM 3234 CA ILE 2310 −15.025 34.291 3.379 1.00 39.08 ATOM 3235 CB ILE 2310 −15.021 35.362 2.277 1.00 39.01 ATOM 3236 CG2 ILE 2310 −14.919 36.741 2.897 1.00 35.23 ATOM 3237 CG1 ILE 2310 −13.875 35.106 1.292 1.00 39.88 ATOM 3238 CD1 ILE 2310 −12.510 35.076 1.913 1.00 39.73 ATOM 3239 C ILE 2310 −16.323 34.424 4.170 1.00 41.83 ATOM 3240 O ILE 2310 −17.390 34.017 3.698 1.00 44.61 ATOM 3241 N LEU 2311 −16.233 34.982 5.372 1.00 41.88 ATOM 3242 CA LEU 2311 −17.402 35.159 6.216 1.00 41.44 ATOM 3243 CB LEU 2311 −17.148 34.545 7.594 1.00 42.77 ATOM 3244 CG LEU 2311 −16.996 33.022 7.590 1.00 42.18 ATOM 3245 CD1 LEU 2311 −16.751 32.506 8.990 1.00 39.93 ATOM 3246 CD2 LEU 2311 −18.259 32.408 7.018 1.00 42.17 ATOM 3247 C LEU 2311 −17.766 36.628 6.354 1.00 43.17 ATOM 3248 O LEU 2311 −18.897 37.024 6.061 1.00 44.43 ATOM 3249 N GLU 2324 −13.336 43.467 14.737 1.00 40.36 ATOM 3250 CA GLU 2324 −12.410 42.769 15.620 1.00 37.84 ATOM 3251 CB GLU 2324 −12.114 43.614 16.850 1.00 40.25 ATOM 3252 CG GLU 2324 −11.481 44.950 16.594 1.00 45.51 ATOM 3253 CD GLU 2324 −11.284 45.716 17.892 1.00 49.98 ATOM 3254 OE1 GLU 2324 −11.542 45.124 18.966 1.00 49.99 ATOM 3255 OE2 GLU 2324 −10.872 46.901 17.849 1.00 54.07 ATOM 3256 C GLU 2324 −12.970 41.428 16.095 1.00 35.83 ATOM 3257 O GLU 2324 −12.222 40.579 16.592 1.00 36.63 ATOM 3258 N VAL 2325 −14.281 41.238 15.975 1.00 30.19 ATOM 3259 CA VAL 2325 −14.858 39.985 16.421 1.00 27.54 ATOM 3260 CB VAL 2325 −15.710 40.181 17.717 1.00 25.42 ATOM 3261 CG1 VAL 2325 −15.364 41.502 18.371 1.00 22.35 ATOM 3262 CG2 VAL 2325 −17.187 40.080 17.419 1.00 22.54 ATOM 3263 C VAL 2325 −15.692 39.259 15.372 1.00 27.76 ATOM 3264 O VAL 2325 −16.371 39.875 14.553 1.00 28.36 ATOM 3265 N LEU 2326 −15.604 37.937 15.395 1.00 26.34 ATOM 3266 CA LEU 2326 −16.370 37.101 14.497 1.00 25.78 ATOM 3267 CB LEU 2326 −15.504 35.977 13.920 1.00 21.35 ATOM 3268 CG LEU 2326 −16.291 34.860 13.222 1.00 23.78 ATOM 3269 CD1 LEU 2326 −17.282 35.481 12.238 1.00 20.95 ATOM 3270 CD2 LEU 2326 −15.336 33.883 12.509 1.00 19.68 ATOM 3271 C LEU 2326 −17.458 36.534 15.389 1.00 26.83 ATOM 3272 O LEU 2326 −17.164 35.917 16.405 1.00 25.50 ATOM 3273 N HIS 2327 −18.717 36.761 15.032 1.00 30.43 ATOM 3274 CA HIS 2327 −19.802 36.256 15.861 1.00 33.90 ATOM 3275 CB HIS 2327 −20.720 37.416 16.252 1.00 36.22 ATOM 3276 CG HIS 2327 −21.558 37.140 17.460 1.00 42.95 ATOM 3277 CD2 HIS 2327 −21.860 35.978 18.092 1.00 46.12 ATOM 3278 ND1 HIS 2327 −22.221 38.131 18.151 1.00 45.91 ATOM 3279 CE1 HIS 2327 −22.897 37.596 19.153 1.00 46.22 ATOM 3280 NE2 HIS 2327 −22.694 36.289 19.137 1.00 48.55 ATOM 3281 C HIS 2327 −20.615 35.105 15.244 1.00 32.96 ATOM 3282 O HIS 2327 −21.250 35.257 14.204 1.00 33.14 ATOM 3283 N LEU 2328 −20.569 33.945 15.891 1.00 32.03 ATOM 3284 CA LEU 2328 −21.308 32.776 15.434 1.00 32.84 ATOM 3285 CB LEU 2328 −20.440 31.522 15.566 1.00 29.75 ATOM 3286 CG LEU 2328 −19.062 31.620 14.895 1.00 31.56 ATOM 3287 CD1 LEU 2328 −18.254 30.378 15.207 1.00 30.02 ATOM 3288 CD2 LEU 2328 −19.206 31.797 13.387 1.00 31.02 ATOM 3289 C LEU 2328 −22.551 32.653 16.311 1.00 35.89 ATOM 3290 O LEU 2328 −22.447 32.540 17.537 1.00 36.66 ATOM 3291 N ARG 2329 −23.725 32.687 15.686 1.00 38.78 ATOM 3292 CA ARG 2329 −24.986 32.598 16.420 1.00 41.21 ATOM 3293 CB ARG 2329 −26.162 32.878 15.486 1.00 40.21 ATOM 3294 C ARG 2329 −25.188 31.252 17.116 1.00 44.19 ATOM 3295 O ARG 2329 −24.309 30.783 17.841 1.00 49.35 ATOM 3296 N ASN 2330 −26.344 30.632 16.899 1.00 44.19 ATOM 3297 CA ASN 2330 −26.664 29.361 17.540 1.00 43.74 ATOM 3298 CB ASN 2330 −28.167 29.103 17.455 1.00 46.78 ATOM 3299 CG ASN 2330 −28.602 27.936 18.313 1.00 51.73 ATOM 3300 OD1 ASN 2330 −28.521 26.770 17.901 1.00 51.92 ATOM 3301 ND2 ASN 2330 −29.054 28.240 19.529 1.00 54.52 ATOM 3302 C ASN 2330 −25.894 28.185 16.957 1.00 43.06 ATOM 3303 O ASN 2330 −26.439 27.343 16.245 1.00 43.14 ATOM 3304 N VAL 2331 −24.615 28.133 17.302 1.00 42.22 ATOM 3305 CA VAL 2331 −23.690 27.107 16.848 1.00 39.36 ATOM 3306 CB VAL 2331 −22.356 27.279 17.583 1.00 37.88 ATOM 3307 CG1 VAL 2331 −21.465 26.056 17.394 1.00 37.62 ATOM 3308 CC2 VAL 2331 −21.674 28.527 17.065 1.00 34.34 ATOM 3309 C VAL 2331 −24.145 25.659 16.966 1.00 39.83 ATOM 3310 O VAL 2331 −24.868 25.297 17.888 1.00 39.78 ATOM 3311 N SER 2332 −23.692 24.845 16.012 1.00 41.07 ATOM 3312 CA SER 2332 −23.981 23.411 15.947 1.00 43.66 ATOM 3313 CB SER 2332 −24.966 23.123 14.815 1.00 44.86 ATOM 3314 OG SER 2332 −24.356 23.342 13.549 1.00 44.80 ATOM 3315 C SER 2332 −22.665 22.662 15.670 1.00 44.87 ATOM 3316 O SER 2332 −21.589 23.272 15.648 1.00 45.34 ATOM 3317 N PHE 2333 −22.743 21.350 15.452 1.00 44.28 ATOM 3318 CA PHE 2333 −21.537 20.575 15.173 1.00 44.85 ATOM 3319 CB PHE 2333 −21.860 19.081 15.028 1.00 44.97 ATOM 3320 CG PHE 2333 −22.125 18.392 16.333 1.00 47.08 ATOM 3321 CD1 PHE 2333 −23.358 17.794 16.585 1.00 46.75 ATOM 3322 CD2 PHE 2333 −21.152 18.374 17.332 1.00 47.17 ATOM 3323 CE1 PHE 2333 −23.620 17.188 17.814 1.00 46.53 ATOM 3324 CE2 PHE 2333 −21.403 17.772 18.563 1.00 46.90 ATOM 3325 CZ PHE 2333 −22.640 17.179 18.804 1.00 47.14 ATOM 3326 C PHE 2333 −20.857 21.067 13.906 1.00 45.07 ATOM 3327 O PHE 2333 −19.639 21.222 13.869 1.00 43.84 ATOM 3328 N GLU 2334 −21.651 21.320 12.870 1.00 46.28 ATOM 3329 CA GLU 2334 −21.106 21.782 11.602 1.00 46.39 ATOM 3330 CB GLU 2334 −22.228 22.071 10.608 1.00 51.24 ATOM 3331 CG GLU 2334 −21.710 22.359 9.207 1.00 56.82 ATOM 3332 CD GLU 2334 −22.639 23.253 8.414 1.00 60.09 ATOM 3333 OE1 GLU 2334 −23.818 22.871 8.232 1.00 63.25 ATOM 3334 OE2 GLU 2334 −22.186 24.337 7.975 1.00 60.77 ATOM 3335 C GLU 2334 −20.261 23.037 11.783 1.00 43.51 ATOM 3336 O GLU 2334 −19.326 23.285 11.017 1.00 42.01 ATOM 3337 N ASP 2335 −20.598 23.832 12.795 1.00 40.98 ATOM 3338 CA ASP 2335 −19.856 25.053 13.070 1.00 37.84 ATOM 3339 CB ASP 2335 −20.596 25.895 14.110 1.00 39.60 ATOM 3340 CG ASP 2335 −21.918 26.431 13.599 1.00 41.51 ATOM 3341 OD1 ASP 2335 −21.910 27.153 12.581 1.00 44.36 ATOM 3342 OD2 ASP 2335 −22.967 26.141 14.212 1.00 42.62 ATOM 3343 C ASP 2335 −18.447 24.728 13.574 1.00 34.92 ATOM 3344 O ASP 2335 −17.545 25.558 13.511 1.00 35.75 ATOM 3345 N ALA 2336 −18.251 23.519 14.079 1.00 31.20 ATOM 3346 CA ALA 2336 −16.937 23.151 14.576 1.00 31.00 ATOM 3347 CB ALA 2336 −16.948 21.725 15.111 1.00 33.17 ATOM 3348 C ALA 2336 −15.934 23.279 13.449 1.00 29.61 ATOM 3349 O ALA 2336 −16.298 23.187 12.280 1.00 28.64 ATOM 3350 N GLY 2337 −14.676 23.518 13.805 1.00 29.46 ATOM 3351 CA GLY 2337 −13.639 23.642 12.799 1.00 27.88 ATOM 3352 C GLY 2337 −12.708 24.812 13.019 1.00 27.32 ATOM 3353 O GLY 2337 −12.816 25.533 14.010 1.00 27.38 ATOM 3354 N GLU 2338 11.801 25.010 12.068 1.00 26.35 ATOM 3355 CA GLU 2338 10.817 26.077 12.145 1.00 25.16 ATOM 3356 CB GLU 2338 −9.500 25.587 11.544 1.00 25.02 ATOM 3357 CG GLU 2338 −8.417 26.640 11.439 1.00 29.90 ATOM 3358 CD GLU 2338 −7.099 26.060 10.960 1.00 32.40 ATOM 3359 OE1 GLU 2338 −7.125 25.240 10.023 1.00 36.76 ATOM 3360 OE2 GLU 2338 −6.036 26.427 11.507 1.00 35.28 ATOM 3361 C GLU 2338 −11.227 27.389 11.485 1.00 23.81 ATOM 3362 O GLU 2338 −11.734 27.402 10.369 1.00 21.60 ATOM 3363 N TYR 2339 −10.999 28.490 12.199 1.00 25.63 ATOM 3364 CA TYR 2339 −11.306 29.827 11.696 1.00 26.09 ATOM 3365 CB TYR 2339 −12.348 30.517 12.567 1.00 26.10 ATOM 3366 CC TYR 2339 −13.696 29.861 12.514 1.00 28.36 ATOM 3367 CD1 TYR 2339 −13.937 28.673 13.195 1.00 29.75 ATOM 3368 CE1 TYR 2339 −15.179 28.044 13.123 1.00 33.66 ATOM 3369 CD2 TYR 2339 −14.731 30.415 11.758 1.00 30.60 ATOM 3370 CE2 TYR 2339 −15.980 29.798 11.677 1.00 30.79 ATOM 3371 GZ TYR 2339 16.197 28.614 12.363 1.00 33.46 ATOM 3372 OH TYR 2339 17.431 28.002 12.296 1.00 36.17 ATOM 3373 C TYR 2339 −10.049 30.686 11.645 1.00 25.83 ATOM 3374 O TYR 2339 −9.108 30.482 12.412 1.00 25.51 ATOM 3375 N THR 2340 −10.056 31.653 10.735 1.00 26.17 ATOM 3376 CA THR 2340 −8.930 32.550 10.539 1.00 26.13 ATOM 3377 CB THR 2340 −8.130 32.164 9.279 1.00 25.51 ATOM 3378 OG1 THR 2340 −7.397 30.965 9.540 1.00 25.93 ATOM 3379 CG2 THR 2340 −7.157 33.281 8.882 1.00 24.93 ATOM 3380 C THR 2340 −9.311 34.018 10.406 1.00 26.93 ATOM 3381 O THR 2340 −10.294 34.377 9.752 1.00 26.98 ATOM 3382 N CYS 2341 −8.507 34.861 11.039 1.00 27.65 ATOM 3383 CA CYS 2341 −8.697 36.290 10.977 1.00 27.53 ATOM 3384 C GYS 2341 −7.557 36.754 10.096 1.00 26.55 ATOM 3385 O CYS 2341 −6.396 36.552 10.436 1.00 26.68 ATOM 3386 CB CYS 2341 −8.580 36.922 12.364 1.00 27.67 ATOM 3387 SG GYS 2341 −8.642 38.740 12.303 1.00 35.81 ATOM 3388 N LEU 2342 −7.890 37.346 8.952 1.00 25.54 ATOM 3389 CA LEU 2342 −6.879 37.834 8.029 1.00 23.02 ATOM 3390 CB LEU 2342 −7.046 37.168 6.658 1.00 24.73 ATOM 3391 CG LEU 2342 −5.942 37.381 5.610 1.00 27.71 ATOM 3392 CD1 LEU 2342 −6.063 36.329 4.503 1.00 28.36 ATOM 3393 CD2 LEU 2342 −6.025 38.789 5.026 1.00 27.29 ATOM 3394 C LEU 2342 −6.968 39.349 7.881 1.00 22.27 ATOM 3395 O LEU 2342 −8.052 39.917 7.752 1.00 20.43 ATOM 3396 N ALA 2343 −5.807 39.991 7.920 1.00 21.01 ATOM 3397 CA ALA 2343 −5.702 41.432 7.766 1.00 20.11 ATOM 3398 CB ALA 2343 −5.360 42.086 9.098 1.00 23.64 ATOM 3399 C ALA 2343 −4.588 41.685 6.762 1.00 19.39 ATOM 3400 O ALA 2343 −3.566 40.987 6.775 1.00 20.25 ATOM 3401 N GLY 2344 −4.781 42.676 5.896 1.00 15.98 ATOM 3402 CA GLY 2344 −3.770 42.979 4.907 1.00 14.20 ATOM 3403 C GLY 2344 −3.752 44.440 4.503 1.00 17.89 ATOM 3404 O GLY 2344 −4.788 45.127 4.517 1.00 16.24 ATOM 3405 N ASN 2345 −2.563 44.927 4.164 1.00 17.17 ATOM 3406 CA ASN 2345 −2.428 46.298 3.721 1.00 21.03 ATOM 3407 CB ASN 2345 −1.805 47.193 4.806 1.00 23.74 ATOM 3408 CG ASN 2345 −0.399 46.784 5.174 1.00 24.91 ATOM 3409 OD1 ASN 2345 −0.431 46.504 4.305 1.00 23.61 ATOM 3410 ND2 ASN 2345 −0.113 46.768 6.475 1.00 25.23 ATOM 3411 C ASN 2345 −1.567 46.284 2.474 1.00 22.00 ATOM 3412 O ASN 2345 −1.140 45.224 2.027 1.00 22.16 ATOM 3413 N SER 2346 −1.303 47.458 1.916 1.00 21.88 ATOM 3414 CA SER 2346 −0.518 47.541 0.699 1.00 21.21 ATOM 3415 CB SER 2346 −0.334 48.992 0.283 1.00 24.16 ATOM 3416 CG SER 2346 0.677 49.611 1.064 1.00 33.09 ATOM 3417 C SER 2346 0.846 46.888 0.779 1.00 20.93 ATOM 3418 O SER 2346 1.414 46.559 −0.252 1.00 24.76 ATOM 3419 N ILE 2347 1.393 46.706 1.977 1.00 19.77 ATOM 3420 CA ILE 2347 2.718 46.087 2.082 1.00 19.53 ATOM 3421 CB ILE 2347 3.476 46.527 3.386 1.00 19.85 ATOM 3422 CG2 ILE 2347 4.732 45.668 3.573 1.00 18.89 ATOM 3423 CG1 ILE 2347 3.948 47.985 3.286 1.00 14.77 ATOM 3424 CD1 ILE 2347 2.872 48.970 2.968 1.00 14.56 ATOM 3425 C ILE 2347 2.656 44.552 2.033 1.00 19.00 ATOM 3426 O ILE 2347 3.401 43.908 1.294 1.00 18.70 ATOM 3427 N GLY 2348 1.766 43.972 2.821 1.00 18.45 ATOM 3428 CA GLY 2348 1.630 42.533 2.846 1.00 16.84 ATOM 3429 C GLY 2348 0.423 42.154 3.673 1.00 19.06 ATOM 3430 O GLY 2348 −0.350 43.017 4.090 1.00 21.04 ATOM 3431 N LEU 2349 0.232 40.866 3.915 1.00 21.40 ATOM 3432 CA LEU 2349 −0.917 40.472 4.710 1.00 23.92 ATOM 3433 CB LEU 2349 −2.002 39.887 3.802 1.00 24.93 ATOM 3434 CG LEU 2349 −1.783 38.567 3.089 1.00 25.84 ATOM 3435 CD1 LEU 2349 −2.053 37.427 4.071 1.00 27.55 ATOM 3436 CD2 LEU 2349 −2.734 38.466 1.902 1.00 24.89 ATOM 3437 C LEU 2349 −0.519 39.508 5.819 1.00 23.81 ATOM 3438 O LEU 2349 0.536 38.881 5.752 1.00 22.86 ATOM 3439 N SER 2350 −1.353 39.411 6.849 1.00 25.20 ATOM 3440 CA SER 2350 −1.058 38.533 7.982 1.00 23.85 ATOM 3441 CB SER 2350 −0.478 39.356 9.129 1.00 26.37 ATOM 3442 OG SER 2350 0.066 40.585 8.661 1.00 27.48 ATOM 3443 C SER 2350 −2.327 37.858 8.481 1.00 22.50 ATOM 3444 O SER 2350 −3.431 38.326 8.222 1.00 22.48 ATOM 3445 N HIS 2351 −2.170 36.762 9.205 1.00 23.35 ATOM 3446 CA HIS 2351 −3.330 36.078 9.766 1.00 25.91 ATOM 3447 CB HIS 2351 −4.119 35.351 8.676 1.00 24.75 ATOM 3448 CG HIS 2351 −3.378 34.217 8.053 1.00 25.15 ATOM 3449 CD2 HIS 2351 −3.516 32.877 8.191 1.00 25.62 ATOM 3450 ND1 HIS 2351 −2.353 34.407 7.151 1.00 26.72 ATOM 3451 CE1 HIS 2351 −1.893 33.232 6.759 1.00 25.94 ATOM 3452 NE2 HIS 2351 −2.582 32.287 7.374 1.00 26.06 ATOM 3453 C HIS 2351 −2.990 35.093 10.880 1.00 26.62 ATOM 3454 O HIS 2351 −1.873 34.585 10.973 1.00 27.45 ATOM 3455 N HIS 2352 −3.980 34.849 11.728 1.00 27.46 ATOM 3456 CA HIS 2352 −3.879 33.923 12.848 1.00 25.59 ATOM 3457 CB HIS 2352 −3.870 34.669 14.184 1.00 26.72 ATOM 3458 CG HIS 2352 −2.614 35.436 14.453 1.00 27.99 ATOM 3459 GD2 HIS 2352 −1.546 35.715 13.669 1.00 28.60 ATOM 3460 ND1 HIS 2352 −2.357 36.022 15.674 1.00 25.34 ATOM 3461 CE1 HIS 2352 −1.185 36.630 15.630 1.00 25.94 ATOM 3462 NE2 HIS 2352 −0.673 36.459 14.425 1.00 28.21 ATOM 3463 C HIS 2352 −5.141 33.078 12.777 1.00 25.00 ATOM 3464 O HIS 2352 −6.189 33.545 12.318 1.00 23.02 ATOM 3465 N SER 2353 −5.049 31.837 13.231 1.00 25.48 ATOM 3466 CA SER 2353 −6.209 30.962 13.207 1.00 26.14 ATOM 3467 CB SER 2353 −5.983 29.830 12.216 1.00 25.97 ATOM 3468 OG SER 2353 −5.596 30.359 10.961 1.00 30.37 ATOM 3469 C SER 2353 −6.488 30.394 14.577 1.00 25.96 ATOM 3470 O SER 2353 −5.682 30.529 15.493 1.00 27.63 ATOM 3471 N ALA 2354 −7.648 29.769 14.716 1.00 28.26 ATOM 3472 CA ALA 2354 −8.039 29.151 15.981 1.00 28.99 ATOM 3473 CB ALA 2354 −8.682 30.180 16.906 1.00 26.00 ATOM 3474 C ALA 2354 −9.014 28.026 15.677 1.00 28.34 ATOM 3475 O ALA 2354 −9.589 27.992 14.591 1.00 25.64 ATOM 3476 N TRP 2355 −9.200 27.111 16.626 1.00 30.54 ATOM 3477 CA TRP 2355 −10.107 25.978 16.429 1.00 31.68 ATOM 3478 CB TRP 2355 −9.349 24.650 16.576 1.00 35.96 ATOM 3479 CG TRP 2355 −9.671 23.674 15.485 1.00 44.14 ATOM 3480 CD2 TRP 2355 −10.745 22.713 15.477 1.00 46.89 ATOM 3481 CE2 TRP 2355 −10.700 22.050 14.225 1.00 47.34 ATOM 3482 CE3 TRP 2355 −11.739 22.350 16.402 1.00 49.33 ATOM 3483 CD1 TRP 2355 −9.038 23.554 14.273 1.00 45.62 ATOM 3484 NE1 TRP 2355 −9.654 22.579 13.514 1.00 47.04 ATOM 3485 CZ2 TRP 2355 −11.616 21.041 13.877 1.00 49.67 ATOM 3486 CZ3 TRP 2355 −12.658 21.336 16.053 1.00 50.10 ATOM 3487 CH2 TRP 2355 −12.583 20.698 14.799 1.00 51.09 ATOM 3488 C TRP 2355 −11.286 26.007 17.394 1.00 30.19 ATOM 3489 O TRP 2355 −11.110 26.198 18.613 1.00 29.45 ATOM 3490 N LEU 2356 −12.480 25.839 16.848 1.00 28.20 ATOM 3491 CA LEU 2356 −13.696 25.852 17.645 1.00 27.77 ATOM 3492 CB LEU 2356 −14.800 26.608 16.918 1.00 26.93 ATOM 3493 CG LEU 2356 −16.128 26.552 17.675 1.00 29.22 ATOM 3494 CD1 LEU 2356 −16.026 27.451 18.915 1.00 29.55 ATOM 3495 CD2 LEU 2356 −17.289 27.011 16.778 1.00 26.35 ATOM 3496 C LEU 2356 −14.162 24.436 17.901 1.00 27.46 ATOM 3497 O LEU 2356 −14.468 23.702 16.957 1.00 28.35 ATOM 3498 N THR 2357 −14.260 24.053 19.167 1.00 28.12 ATOM 3499 CA THR 2357 −14.697 22.710 19.490 1.00 28.42 ATOM 3500 CB THR 2357 −13.766 22.070 20.539 1.00 29.97 ATOM 3501 OG1 THR 2357 −12.397 22.232 20.124 1.00 34.87 ATOM 3502 CG2 THR 2357 −14.085 20.602 20.675 1.00 28.93 ATOM 3503 C THR 2357 −16.128 22.755 19.990 1.00 27.28 ATOM 3504 O THR 2357 −16.493 23.594 20.821 1.00 25.21 ATOM 3505 N VAL 2358 −16.948 21.853 19.473 1.00 26.50 ATOM 3506 CA VAL 2358 −18.345 21.841 19.880 1.00 27.27 ATOM 3507 CB VAL 2358 −19.239 22.101 18.692 1.00 28.10 ATOM 3508 CG1 VAL 2358 −20.639 22.433 19.174 1.00 31.58 ATOM 3509 CG2 VAL 2358 −18.646 23.239 17.861 1.00 27.73 ATOM 3510 C VAL 2358 −18.769 20.553 20.577 1.00 27.76 ATOM 3511 O VAL 2358 −18.437 19.453 20.141 1.00 27.86 ATOM 3512 N LEU 2359 −19.524 20.709 21.661 1.00 29.50 ATOM 3513 CA LEU 2359 −19.960 19.576 22.466 1.00 29.73 ATOM 3514 CB LEU 2359 −19.235 19.650 23.817 1.00 28.52 ATOM 3515 CG LEU 2359 −17.709 19.655 23.682 1.00 24.43 ATOM 3516 CD1 LEU 2359 −17.073 19.819 25.063 1.00 22.37 ATOM 3517 CD2 LEU 2359 −17.264 18.353 22.992 1.00 18.11 ATOM 3518 C LEU 2359 −21.480 19.460 22.670 1.00 30.02 ATOM 3519 O LEU 2359 −22.142 20.532 22.683 1.00 29.26 ATOM 3520 CB ASN 3147 −34.933 22.064 55.418 1.00 44.07 ATOM 3521 CG ASN 3147 −36.079 21.137 55.075 1.00 49.07 ATOM 3522 OD1 ASN 3147 −35.963 19.925 55.207 1.00 51.17 ATOM 3523 ND2 ASN 3147 −37.193 21.708 54.646 1.00 49.27 ATOM 3524 C ASN 3147 −33.835 22.292 57.692 1.00 40.45 ATOM 3525 O ASN 3147 −33.964 21.572 58.683 1.00 40.68 ATOM 3526 N ASN 3147 −35.269 24.112 56.758 1.00 42.01 ATOM 3527 CA ASN 3147 −35.056 22.641 56.832 1.00 42.43 ATOM 3528 N ARG 3148 −32.658 22.799 57.342 1.00 37.62 ATOM 3529 CA ARG 3148 −31.470 22.483 58.148 1.00 36.21 ATOM 3530 CB ARG 3148 −30.346 21.952 57.257 1.00 34.96 ATOM 3531 C ARG 3148 −30.943 23.632 59.017 1.00 35.42 ATOM 3532 O ARG 3148 −31.315 24.798 58.836 1.00 36.26 ATOM 3533 N MET 3149 −30.101 23.277 59.987 1.00 31.28 ATOM 3534 CA MET 3149 −29.501 24.245 60.908 1.00 27.15 ATOM 3535 CB MET 3149 −28.481 23.554 61.808 1.00 28.45 ATOM 3536 CG MET 3149 −27.849 24.460 62.865 1.00 27.74 ATOM 3537 D MET 3149 −28.961 24.797 64.250 1.00 29.90 ATOM 3538 CE MET 3149 −28.319 26.362 64.772 1.00 26.73 ATOM 3539 C MET 3149 −28.806 25.378 60.171 1.00 23.68 ATOM 3540 O MET 3149 −27.832 25.153 59.462 1.00 24.57 ATOM 3541 N PRO 3150 −29.275 26.619 60.360 1.00 21.74 ATOM 3542 CD PRO 3150 −30.432 27.035 61.174 1.00 19.77 ATOM 3543 CA PRO 3150 −28.667 27.770 59.684 1.00 17.93 ATOM 3544 CE PRO 3150 −29.414 28.956 60.293 1.00 20.02 ATOM 3545 CG PRO 3150 −30.789 28.377 60.555 1.00 17.09 ATOM 3546 C PRO 3150 −27.163 27.877 59.863 1.00 13.71 ATOM 3547 O PRO 3150 −26.635 27.611 60.938 1.00 17.01 ATOM 3548 N VAL 3151 −26.474 28.248 58.791 1.00 12.06 ATOM 3549 CA VAL 3151 −25.019 28.410 58.810 1.00 11.74 ATOM 3550 CB VAL 3151 −24.276 27.099 58.419 1.00 9.82 ATOM 3551 CG1 VAL 3151 −22.767 27.358 58.290 1.00 2.10 ATOM 3552 CG2 VAL 3151 −24.539 26.019 59.467 1.00 7.23 ATOM 3553 C VAL 3151 −24.582 29.501 57.840 1.00 13.11 ATOM 3554 O VAL 3151 −24.724 29.355 56.622 1.00 12.79 ATOM 3555 N ALA 3152 −24.052 30.597 58.374 1.00 13.16 ATOM 3556 CA ALA 3152 −23.599 31.686 57.507 1.00 14.26 ATOM 3557 CB ALA 3152 −23.067 32.847 58.340 1.00 7.04 ATOM 3558 C ALA 3152 −22.519 31.170 56.535 1.00 13.45 ATOM 3559 O ALA 3152 −21.733 30.291 56.869 1.00 12.84 ATOM 3560 N PRO 3153 −22.481 31.717 55.315 1.00 15.40 ATOM 3561 CD PRO 3153 −23.320 32.814 54.796 1.00 14.82 ATOM 3562 CA PRO 3153 −21.498 31.292 54.318 1.00 16.14 ATOM 3563 CB PRO 3153 −21.883 32.114 53.089 1.00 16.95 ATOM 3564 CG PRO 3153 −22.470 33.360 53.690 1.00 17.38 ATOM 3565 C PRO 3153 −20.051 31.491 54.733 1.00 17.05 ATOM 3566 O PRO 3153 −19.689 32.528 55.275 1.00 16.99 ATOM 3567 N TYR 3154 −19.227 30.485 54.456 1.00 21.23 ATOM 3568 CA TYR 3154 −17.807 30.516 54.797 1.00 20.93 ATOM 3569 CB TYR 3154 −17.579 29.793 56.105 1.00 19.47 ATOM 3570 CG TYR 3154 −17.999 28.351 56.035 1.00 17.48 ATOM 3571 CD1 TYR 3154 −19.340 28.006 55.910 1.00 14.81 ATOM 3572 CE1 TYR 3154 −19.732 26.680 55.837 1.00 18.14 ATOM 3573 CD2 TYR 3154 −17.051 27.327 56.082 1.00 18.77 ATOM 3574 CE2 TYR 3154 −17.432 25.987 56.010 1.00 17.16 ATOM 3575 GZ TYR 3154 −18.770 25.672 55.888 1.00 19.28 ATOM 3576 OH TYR 3154 −19.146 24.352 55.828 1.00 21.94 ATOM 3577 C TYR 3154 −16.947 29.848 53.737 1.00 22.24 ATOM 3578 O TYR 3154 −17.401 28.963 53.015 1.00 24.32 ATOM 3579 N TRP 3155 −15.689 30.267 53.683 1.00 24.77 ATOM 3580 CA TRP 3155 −14.713 29.744 52.732 1.00 27.11 ATOM 3581 CB TRP 3155 −13.418 30.548 52.845 1.00 26.23 ATOM 3582 CG TRP 3155 −13.586 32.029 52.627 1.00 24.87 ATOM 3583 CD2 TRP 3155 −14.384 32.670 51.622 1.00 23.22 ATOM 3584 CE2 TRP 3155 −14.193 34.067 51.763 1.00 23.69 ATOM 3585 CE3 TRP 3155 −15.240 32.204 50.617 1.00 21.94 ATOM 3586 CD1 TRP 3155 −12.962 33.035 53.318 1.00 24.48 ATOM 3587 NE1 TRP 3155 −13.321 34.260 52.804 1.00 22.81 ATOM 3588 CZ2 TRP 3155 −14.830 35.003 50.932 1.00 21.14 ATOM 3589 CZ3 TRP 3155 −15.872 33.135 49.789 1.00 21.61 ATOM 3590 CH2 TRP 3155 −15.661 34.519 49.954 1.00 22.70 ATOM 3591 C TRP 3155 −14.415 28.261 52.970 1.00 28.81 ATOM 3592 O TRP 3155 −14.352 27.804 54.108 1.00 29.07 ATOM 3593 N THR 3156 −14.221 27.520 51.886 1.00 31.49 ATOM 3594 CA THR 3156 −13.937 26.093 51.968 1.00 34.42 ATOM 3595 CB THR 3156 −14.935 25.292 51.097 1.00 36.07 ATOM 3596 OG1 THR 3156 −16.258 25.446 51.628 1.00 37.52 ATOM 3597 CG2 THR 3156 −14.574 23.812 51.068 1.00 38.45 ATOM 3598 C THR 3156 −12.515 25.811 51.496 1.00 36.62 ATOM 3599 O THR 3156 −12.059 24.672 51.493 1.00 38.31 ATOM 3600 N SER 3157 −11.809 26.859 51.100 1.00 38.06 ATOM 3601 CA SER 3157 −10.448 26.691 50.627 1.00 39.63 ATOM 3602 CB SER 3157 −10.474 26.163 49.192 1.00 42.04 ATOM 3603 OG SER 3157 −9.165 25.975 48.686 1.00 48.25 ATOM 3604 C SER 3157 −9.732 28.027 50.687 1.00 39.53 ATOM 3605 O SER 3157 −9.023 28.406 49.756 1.00 39.53 ATOM 3606 N PRO 3158 −9.894 28.750 51.807 1.00 40.33 ATOM 3607 CD PRO 3158 −10.415 28.203 53.072 1.00 38.84 ATOM 3608 CA PRO 3158 −9.283 30.066 52.031 1.00 41.05 ATOM 3609 CB PRO 3158 −9.298 30.193 53.552 1.00 39.82 ATOM 3610 CG PRO 3158 −10.514 29.428 53.933 1.00 39.18 ATOM 3611 C PRO 3158 −7.873 30.157 51.463 1.00 41.84 ATOM 3612 O PRO 3158 −7.460 31.194 50.938 1.00 40.53 ATOM 3613 N ALA 3159 −7.144 29.055 51.577 1.00 42.89 ATOM 3614 CA ALA 3159 −5.783 28.990 51.084 1.00 44.47 ATOM 3615 CB ALA 3159 −5.269 27.557 51.180 1.00 46.15 ATOM 3616 C ALA 3159 −5.727 29.475 49.641 1.00 44.76 ATOM 3617 O ALA 3159 −5.175 30.545 49.353 1.00 44.96 ATOM 3618 N ALA 3160 −6.312 28.685 48.743 1.00 42.87 ATOM 3619 CA ALA 3160 −6.328 29.011 47.324 1.00 42.85 ATOM 3620 CB ALA 3160 −7.370 28.152 46.607 1.00 41.03 ATOM 3621 C ALA 3160 −6.592 30.493 47.050 1.00 43.30 ATOM 3622 O ALA 3160 −6.115 31.035 46.050 1.00 46.42 ATOM 3623 N MET 3161 −7.328 31.153 47.942 1.00 41.04 ATOM 3624 CA MET 3161 −7.666 32.560 47.756 1.00 38.29 ATOM 3625 CB MET 3161 −8.936 32.890 48.545 1.00 36.52 ATOM 3626 CG MET 3161 −10.049 31.857 48.369 1.00 34.13 ATOM 3627 SD MET 3161 −11.553 32.242 49.278 1.00 30.96 ATOM 3628 CE MET 3161 −12.721 31.294 48.415 1.00 36.88 ATOM 3629 C MET 3161 −6.557 33.548 48.119 1.00 38.60 ATOM 3630 O MET 3161 −6.658 34.733 47.804 1.00 38.63 ATOM 3631 N ALA 3162 −5.499 33.066 48.766 1.00 38.98 ATOM 3632 CA ALA 3162 −4.386 33.932 49.166 1.00 37.98 ATOM 3633 CB ALA 3162 −3.288 33.097 49.821 1.00 40.89 ATOM 3634 C ALA 3162 −3.816 34.711 47.978 1.00 36.26 ATOM 3635 O ALA 3162 −3.553 35.911 48.081 1.00 34.15 ATOM 3636 N LYS 3163 −3.619 34.011 46.860 1.00 34.79 ATOM 3637 CA LYS 3163 −3.105 34.602 45.621 1.00 32.71 ATOM 3638 CB LYS 3163 −2.867 33.483 44.608 1.00 29.79 ATOM 3639 CG LYS 3163 −2.416 33.927 43.247 1.00 30.82 ATOM 3640 CD LYS 3163 −2.410 32.742 42.276 1.00 33.00 ATOM 3641 CE LYS 3163 −2.244 33.211 40.818 1.00 36.76 ATOM 3642 NZ LYS 3163 −2.375 32.119 39.797 1.00 33.68 ATOM 3643 C LYS 3163 −4.181 35.574 45.109 1.00 33.81 ATOM 3644 O LYS 3163 −5.115 35.165 44.407 1.00 32.40 ATOM 3645 N ALA 3164 −4.045 36.855 45.467 1.00 32.72 ATOM 3646 CA ALA 3164 −5.022 37.877 45.099 1.00 30.74 ATOM 3647 CB ALA 3164 −4.965 39.035 46.094 1.00 28.25 ATOM 3648 C ALA 3164 −4.900 38.409 43.680 1.00 31.97 ATOM 3649 O ALA 3164 −5.902 38.594 42.977 1.00 31.00 ATOM 3650 N LEU 3165 −3.678 38.659 43.244 1.00 32.83 ATOM 3651 CA LEU 3165 −3.494 39.182 41.895 1.00 34.12 ATOM 3652 CB LEU 3165 −2.321 40.164 41.864 1.00 31.66 ATOM 3653 CG LEU 3165 −1.902 40.675 40.489 1.00 29.85 ATOM 3654 CD1 LEU 3165 −3.047 41.426 39.852 1.00 28.92 ATOM 3655 CD2 LEU 3165 −0.692 41.575 40.636 1.00 32.73 ATOM 3656 C LEU 3165 −3.274 38.098 40.838 1.00 35.09 ATOM 3657 O LEU 3165 −2.440 37.200 40.994 1.00 35.48 ATOM 3658 N HIS 3166 −4.040 38.190 39.758 1.00 35.16 ATOM 3659 CA HIS 3166 −3.915 37.254 38.655 1.00 33.65 ATOM 3660 CB HIS 3166 −5.265 36.610 38.323 1.00 33.18 ATOM 3661 CG HIS 3166 −5.591 35.420 39.168 1.00 33.75 ATOM 3662 CD2 HIS 3166 −5.711 34.109 38.849 1.00 34.10 ATOM 3663 ND1 HIS 3166 −5.840 35.509 40.520 1.00 34.52 ATOM 3664 CE1 HIS 3166 −6.100 34.305 41.000 1.00 33.44 ATOM 3665 NE2 HIS 3166 −6.028 33.439 40.007 1.00 33.69 ATOM 3666 C HIS 3166 −3.387 37.992 37.434 1.00 32.45 ATOM 3667 O HIS 3166 −4.116 38.715 36.750 1.00 31.98 ATOM 3668 N ALA 3167 −2.101 37.833 37.175 1.00 30.77 ATOM 3669 CA ALA 3167 −1.513 38.471 36.016 1.00 30.62 ATOM 3670 CB ALA 3167 −0.104 38.959 36.336 1.00 29.94 ATOM 3671 C ALA 3167 −1.496 37.405 34.920 1.00 29.25 ATOM 3672 O ALA 3167 −0.961 36.311 35.105 1.00 30.60 ATOM 3673 N VAL 3168 −2.094 37.722 33.781 1.00 26.81 ATOM 3674 CA VAL 3168 −2.164 36.769 32.684 1.00 24.17 ATOM 3675 CB VAL 3168 −3.602 36.150 32.624 1.00 23.29 ATOM 3676 CG1 VAL 3168 −4.154 36.141 31.198 1.00 22.64 ATOM 3677 CG2 VAL 3168 −3.574 34.757 33.180 1.00 19.45 ATOM 3678 C VAL 3168 −1.796 37.364 31.325 1.00 23.88 ATOM 3679 O VAL 3168 −2.079 38.534 31.028 1.00 23.24 ATOM 3680 N PRO 3169 −1.126 36.574 30.483 1.00 22.93 ATOM 3681 CD PRO 3169 −0.561 35.222 30.633 1.00 21.77 ATOM 3682 CA PRO 3169 −0.796 37.148 29.180 1.00 23.68 ATOM 3683 CB PRO 3169 0.281 36.200 28.651 1.00 22.17 ATOM 3684 CG PRO 3169 −0.140 34.884 29.203 1.00 19.69 ATOM 3685 C PRO 3169 −2.093 37.132 28.344 1.00 23.78 ATOM 3686 O PRO 3169 −2.878 36.172 28.397 1.00 21.15 ATOM 3687 N ALA 3170 −2.326 38.204 27.597 1.00 23.56 ATOM 3688 CA ALA 3170 −3.525 38.315 26.773 1.00 21.30 ATOM 3689 CB ALA 3170 −3.358 39.449 25.776 1.00 18.95 ATOM 3690 C ALA 3170 −3.833 37.022 26.036 1.00 20.56 ATOM 3691 O ALA 3170 −2.917 36.315 25.595 1.00 19.94 ATOM 3692 N ALA 3171 −5.126 36.710 25.932 1.00 19.85 ATOM 3693 CA ALA 3171 −5.601 35.519 25.221 1.00 18.11 ATOM 3694 CB ALA 3171 −4.642 35.165 24.078 1.00 15.17 ATOM 3695 C ALA 3171 −5.834 34.295 26.081 1.00 17.89 ATOM 3696 O ALA 3171 −6.490 33.349 25.655 1.00 21.43 ATOM 3697 N ALA 3172 −5.296 34.290 27.287 1.00 18.71 ATOM 3698 CA ALA 3172 −5.489 33.137 28.140 1.00 18.57 ATOM 3699 CB ALA 3172 −4.399 33.084 29.188 1.00 15.97 ATOM 3700 C ALA 317 −6.867 33.173 28.797 1.00 21.38 ATOM 3701 O ALA 3172 −7.439 34.243 29.019 1.00 22.10 ATOM 3702 N THR 3173 −7.416 31.989 29.065 1.00 24.31 ATOM 3703 CA THR 3173 −8.710 31.876 29.740 1.00 23.82 ATOM 3704 CB THR 3173 −9.343 30.465 29.550 1.00 23.64 ATOM 3705 OG1 THR 3173 −9.900 30.368 28.234 1.00 26.07 ATOM 3706 CG2 THR 3173 −10.449 30.206 30.584 1.00 20.22 ATOM 3707 C THR 3173 −8.402 32.092 31.219 1.00 22.88 ATOM 3708 O THR 3173 −7.450 31.521 31.752 1.00 23.50 ATOM 3709 N VAL 3174 −9.196 32.921 31.877 1.00 19.83 ATOM 3710 CA VAL 3174 −8.976 33.200 33.282 1.00 16.83 ATOM 3711 CB VAL 3174 −8.822 34.708 33.493 1.00 15.67 ATOM 3712 CG1 VAL 3174 −9.055 35.062 34.940 1.00 17.37 ATOM 3713 CG2 VAL 3174 −7.450 35.143 33.052 1.00 12.57 ATOM 3714 C VAL 3174 −10.140 32.711 34.117 1.00 17.52 ATOM 3715 O VAL 3174 −11.284 33.032 33.810 1.00 21.82 ATOM 3716 N ALA 3175 −9.862 31.935 35.161 1.00 16.14 ATOM 3717 CA ALA 3175 −10.931 31.458 36.048 1.00 17.44 ATOM 3718 CB ALA 3175 −10.977 29.935 36.044 1.00 14.62 ATOM 3719 C ALA 3175 −10.715 31.983 37.483 1.00 19.37 ATOM 3720 O ALA 3175 −9.577 32.116 37.936 1.00 21.07 ATOM 3721 N PHE 3176 −11.803 32.316 38.180 1.00 21.52 ATOM 3722 CA PHE 3176 −11.730 32.800 39.572 1.00 22.20 ATOM 3723 CB PHE 3176 −12.181 34.271 39.710 1.00 21.08 ATOM 3724 CG PHE 3176 −11.178 35.263 39.195 1.00 17.44 ATOM 3725 CD1 PHE 3176 −9.820 35.061 39.403 1.00 13.20 ATOM 3726 CD2 PHE 3176 −11.590 36.378 38.471 1.00 19.12 ATOM 3727 CE1 PHE 3176 −8.881 35.945 38.896 1.00 15.24 ATOM 3728 CE2 PHE 3176 −10.652 37.282 37.951 1.00 20.36 ATOM 3729 CZ PHE 3176 −9.292 37.062 38.164 1.00 18.37 ATOM 3730 C PHE 3176 −12.613 31.932 40.453 1.00 23.14 ATOM 3731 O PHE 3176 −13.757 31.657 40.123 1.00 25.48 ATOM 3732 N ALA 3177 −12.092 31.517 41.592 1.00 24.72 ATOM 3733 CA ALA 3177 −12.860 30.652 42.460 1.00 26.07 ATOM 3734 CB ALA 3177 −12.216 29.256 42.483 1.00 25.30 ATOM 3735 C ALA 3177 −13.022 31.175 43.879 1.00 27.27 ATOM 3736 O ALA 3177 −12.136 31.830 44.440 1.00 26.09 ATOM 3737 N CYS 3178 −14.177 30.866 44.447 1.00 26.85 ATOM 3738 CA CYS 3178 −14.508 31.249 45.799 1.00 26.83 ATOM 3739 C CYS 3178 −15.230 30.059 46.399 1.00 26.94 ATOM 3740 O CYS 3178 −16.431 30.116 46.671 1.00 27.90 ATOM 3741 CB CYS 3178 −15.418 32.490 45.811 1.00 27.91 ATOM 3742 SG CYS 3178 −14.573 34.029 45.310 1.00 34.46 ATOM 3743 N PRO 3179 −14.520 28.936 46.563 1.00 26.83 ATOM 3744 CD PRO 3179 −13.163 28.607 46.096 1.00 24.75 ATOM 3745 CA PRO 3179 −15.180 27.763 47.150 1.00 28.17 ATOM 3746 CB PRO 3179 −14.031 26.784 47.344 1.00 26.22 ATOM 3747 CG PRO 3179 −13.171 27.086 46.151 1.00 27.38 ATOM 3748 C PRO 3179 −15.828 28.181 48.473 1.00 29.86 ATOM 3749 O PRO 3179 −15.203 28.851 49.308 1.00 30.65 ATOM 3750 N SER 3180 −17.082 27.802 48.662 1.00 28.44 ATOM 3751 CA SER 3180 −17.771 28.188 49.873 1.00 28.03 ATOM 3752 CB SER 3180 −18.368 29.578 49.710 1.00 30.25 ATOM 3753 OG SER 3180 −17.374 30.494 49.298 1.00 35.90 ATOM 3754 C SER 3180 −18.870 27.233 50.223 1.00 27.25 ATOM 3755 O SER 3180 −19.266 26.391 49.430 1.00 28.30 ATOM 3756 N SER 3181 −19.371 27.378 51.433 1.00 27.12 ATOM 3757 CA SER 3181 −20.441 26.530 51.890 1.00 27.21 ATOM 3758 CB SER 3181 −19.862 25.312 52.612 1.00 29.78 ATOM 3759 OG SER 3181 −20.880 24.385 52.940 1.00 35.40 ATOM 3760 C SER 3181 −21.294 27.366 52.827 1.00 25.72 ATOM 3761 O SER 3181 −20.961 28.518 53.126 1.00 23.32 ATOM 3762 N GLY 3182 −22.392 26.780 53.283 1.00 25.53 ATOM 3763 CA GLY 3182 −23.291 27.475 54.179 1.00 25.82 ATOM 3764 C GLY 3182 −24.686 26.946 53.961 1.00 25.46 ATOM 3765 O GLY 3182 −24.999 26.440 52.885 1.00 25.71 ATOM 3766 N THR 3183 −25.527 27.051 54.980 1.00 25.41 ATOM 3767 CA THR 3183 −26.889 26.569 54.864 1.00 24.64 ATOM 3768 CB THR 3183 −27.064 25.185 55.567 1.00 23.85 ATOM 3769 OG1 THR 3183 −27.889 25.318 56.727 1.00 25.02 ATOM 3770 CG2 THR 3183 −25.720 24.624 55.972 1.00 21.75 ATOM 3771 C THR 3183 −27.889 27.574 55.422 1.00 24.27 ATOM 3772 O THR 3183 −27.669 28.166 56.474 1.00 25.47 ATOM 3773 N PRO 3184 −28.986 27.816 54.686 1.00 25.01 ATOM 3774 CD PRO 3184 −30.069 28.743 55.036 1.00 24.48 ATOM 3775 CA PRO 3184 −29.250 27.171 53.393 1.00 23.19 ATOM 3776 CB PRO 3184 −30.614 27.724 53.004 1.00 21.27 ATOM 3777 CG PRO 3184 −30.648 29.052 53.681 1.00 25.55 ATOM 3778 C PRO 3184 −28.147 27.519 52.401 1.00 23.47 ATOM 3779 O PRO 3184 −27.450 28.519 52.571 1.00 21.98 ATOM 3780 N ASN 3185 −27.983 26.679 51.382 1.00 25.79 ATOM 3781 CA ASN 3185 −26.933 26.867 50.394 1.00 26.96 ATOM 3782 CB ASN 3185 −27.052 25.836 49.279 1.00 31.34 ATOM 3783 CG ASN 3185 −25.694 25.452 48.706 1.00 39.03 ATOM 3784 OD1 ASN 3185 −25.091 26.198 47.924 1.00 41.63 ATOM 3785 ND2 ASN 3185 −25.192 24.292 49.116 1.00 42.36 ATOM 3786 C ASN 3185 −26.929 28.262 49.817 1.00 25.86 ATOM 3787 O ASN 3185 −27.906 28.698 49.225 1.00 27.89 ATOM 3788 N PRO 3186 −25.811 28.981 49.984 1.00 24.67 ATOM 3789 CD PRO 3186 −24.632 28.493 50.723 1.00 24.39 ATOM 3790 CA PRO 3186 −25.596 30.351 49.517 1.00 25.60 ATOM 3791 CB PRO 3186 −24.317 30.761 50.241 1.00 25.99 ATOM 3792 CG PRO 3186 −23.568 29.479 50.326 1.00 24.50 ATOM 3793 C PRO 3186 −25.515 30.608 48.007 1.00 26.93 ATOM 3794 O PRO 3186 −25.245 29.710 47.197 1.00 26.83 ATOM 3795 N THR 3187 −25.738 31.876 47.675 1.00 23.65 ATOM 3796 CA THR 3187 −25.752 32.405 46.327 1.00 19.53 ATOM 3797 CB THR 3187 −26.787 33.531 46.263 1.00 19.53 ATOM 3798 OG1 THR 3187 −28.028 32.977 45.838 1.00 21.66 ATOM 3799 CG2 THR 3187 −26.355 34.664 45.348 1.00 19.57 ATOM 3800 C THR 3187 −24.390 32.921 45.883 1.00 20.94 ATOM 3801 O THR 3187 −23.563 33.303 46.714 1.00 22.44 ATOM 3802 N LEU 3188 −24.168 32.936 44.567 1.00 18.27 ATOM 3803 CA LEU 3188 −22.904 33.402 44.011 1.00 14.85 ATOM 3804 CB LEU 3188 −22.117 32.227 43.412 1.00 9.58 ATOM 3805 CG LEU 3188 −20.579 32.262 43.367 1.00 8.72 ATOM 3806 CD1 LEU 3188 −20.100 31.213 42.370 1.00 6.67 ATOM 3807 CD2 LEU 3188 −20.055 33.648 42.982 1.00 5.30 ATOM 3808 C LEU 3188 −23.130 34.454 42.929 1.00 15.82 ATOM 3809 O LEU 3188 −23.698 34.177 41.878 1.00 16.74 ATOM 3810 N ALA 3189 −22.666 35.662 43.199 1.00 15.51 ATOM 3811 CA ALA 3189 −22.780 36.761 42.262 1.00 14.78 ATOM 3812 CB ALA 3189 −23.719 37.826 42.820 1.00 9.44 ATOM 3813 C ALA 3189 −21.370 37.330 42.055 1.00 17.07 ATOM 3814 O ALA 3189 −20.496 37.188 42.915 1.00 16.25 ATOM 3815 N TRP 3190 −21.149 37.977 40.918 1.00 18.41 ATOM 3816 CA TRP 3190 −19.845 38.539 40.623 1.00 21.12 ATOM 3817 CB TRP 3190 −19.174 37.703 39.548 1.00 21.41 ATOM 3818 CG TRP 3190 −18.589 36.409 40.035 1.00 21.03 ATOM 3819 CD2 TRP 3190 −17.282 36.226 40.581 1.00 18.76 ATOM 3820 CE2 TRP 3190 −17.116 34.840 40.815 1.00 17.01 ATOM 3821 CE3 TRP 3190 −16.227 37.099 40.888 1.00 19.08 ATOM 3822 CD1 TRP 3190 −19.158 35.163 39.972 1.00 18.61 ATOM 3823 NE1 TRP 3190 −18.276 34.217 40.433 1.00 15.64 ATOM 3824 CZ2 TRP 3190 −15.936 34.304 41.343 1.00 15.99 ATOM 3825 CZ3 TRP 3190 −15.046 36.564 41.413 1.00 19.91 ATOM 3826 CH2 TRP 3190 −14.914 35.176 41.634 1.00 17.87 ATOM 3827 C TRP 3190 −19.868 40.005 40.188 1.00 22.99 ATOM 3828 O TRP 3190 −20.731 40.427 39.423 1.00 25.42 ATOM 3829 N LEU 3191 −18.895 40.772 40.668 1.00 24.94 ATOM 3830 CA LEU 3191 −18.794 42.193 40.355 1.00 26.37 ATOM 3831 CB LEU 3191 −18.926 43.023 41.642 1.00 25.49 ATOM 3832 CG LEU 3191 −20.162 42.870 42.541 1.00 28.84 ATOM 3833 CD1 LEU 3191 −20.127 43.967 43.607 1.00 28.14 ATOM 3834 CD2 LEU 3191 −21.447 42.979 41.728 1.00 27.31 ATOM 3835 C LEU 3191 −17.470 42.560 39.670 1.00 29.34 ATOM 3836 O LEU 3191 −16.453 41.874 39.821 1.00 31.79 ATOM 3837 N LYS 3192 −17.489 43.647 38.909 1.00 30.17 ATOM 3838 CA LYS 3192 −16.285 44.120 38.242 1.00 31.89 ATOM 3839 CB LYS 3192 −16.415 43.980 36.718 1.00 31.26 ATOM 3840 CG LYS 3192 −15.190 44.450 35.920 1.00 29.80 ATOM 3841 CD LYS 3192 −15.219 43.874 34.505 1.00 32.69 ATOM 3842 CE LYS 3192 −14.429 44.713 33.485 1.00 34.71 ATOM 3843 NZ LYS 3192 −12.968 44.837 33.773 1.00 34.92 ATOM 3844 C LYS 3192 −16.137 45.582 38.656 1.00 33.72 ATOM 3845 O LYS 3192 −16.972 46.426 38.325 1.00 34.33 ATOM 3846 N ASN 3193 −15.086 45.867 39.413 1.00 34.19 ATOM 3847 CA ASN 3193 −14.837 47.218 39.893 1.00 36.46 ATOM 3848 CB ASN 3193 −14.382 48.111 38.740 1.00 35.57 ATOM 3849 CG ASH 3193 −13.214 47.526 37.978 1.00 37.77 ATOM 3850 OD1 ASH 3193 −12.219 47.108 38.567 1.00 39.10 ATOM 3851 ND2 ASH 3193 −13.326 47.498 36.657 1.00 40.56 ATOM 3852 C ASN 3193 −16.069 47.834 40.575 1.00 37.56 ATOM 3853 O ASN 3193 −16.462 48.962 40.271 1.00 41.08 ATOM 3854 N GLY 3194 −16.685 47.090 41.488 1.00 34.84 ATOM 3855 CA GLY 3194 −17.833 47.615 42.201 1.00 33.97 ATOM 3856 C GLY 3194 −19.197 47.440 41.565 1.00 35.07 ATOM 3857 O GLY 3194 −20.161 47.117 42.258 1.00 34.48 ATOM 3858 N ALA 3195 −19.297 47.657 40.260 1.00 35.47 ATOM 3859 CA ALA 3195 −20.586 47.523 39.585 1.00 36.44 ATOM 3860 CB ALA 3195 −20.598 48.366 38.309 1.00 34.68 ATOM 3861 C ALA 3195 −20.904 46.066 39.255 1.00 36.34 ATOM 3862 O ALA 3195 −20.033 45.194 39.332 1.00 34.71 ATOM 3863 N ALA 3196 −22.161 45.808 38.903 1.00 35.91 ATOM 3864 CA ALA 3196 −22.592 44.465 38.536 1.00 36.77 ATOM 3865 CB ALA 3196 −24.109 44.435 38.340 1.00 35.46 ATOM 3866 C ALA 3196 −21.880 44.093 37.235 1.00 37.93 ATOM 3867 O ALA 3196 −21.557 44.966 36.430 1.00 39.51 ATOM 3868 N PHE 3197 −21.634 42.804 37.026 1.00 38.80 ATOM 3869 CA PHE 3197 −20.939 42.344 35.826 1.00 38.95 ATOM 3870 CB PHE 3197 −19.657 41.607 36.220 1.00 38.39 ATOM 3871 CG PHE 3197 −18.768 41.252 35.059 1.00 40.65 ATOM 3872 CD1 PHE 3197 −18.057 40.049 35.055 1.00 41.69 ATOM 3873 CD2 PHE 3197 −18.597 42.133 33.991 1.00 42.76 ATOM 3874 CE1 PHE 3197 −17.182 39.721 34.004 1.00 41.49 ATOM 3875 CE2 PHE 3197 −17.728 41.822 32.935 1.00 42.78 ATOM 3876 CZ PHE 3197 −17.018 40.610 32.943 1.00 43.47 ATOM 3877 C PHE 3197 −21.817 41.401 35.022 1.00 40.42 ATOM 3878 O PHE 3197 −21.913 40.222 35.347 1.00 40.89 ATOM 3879 N ALA 3198 −22.468 41.910 33.981 1.00 40.45 ATOM 3880 CA ALA 3198 −23.311 41.057 33.149 1.00 40.04 ATOM 3881 CB ALA 3198 −24.511 41.849 32.614 1.00 39.13 ATOM 3882 C ALA 3198 −22.435 40.543 32.002 1.00 39.08 ATOM 3883 O ALA 3198 −21.550 41.254 31.530 1.00 37.45 ATOM 3884 N PRO 3199 −22.662 39.296 31.550 1.00 38.58 ATOM 3885 CD PRO 3199 −23.725 38.385 31.994 1.00 38.44 ATOM 3886 CA PRO 3199 −21.886 38.688 30.462 1.00 39.44 ATOM 3887 CB PRO 3199 −22.601 37.356 30.224 1.00 38.24 ATOM 3888 CG PRO 3199 −23.973 37.596 30.754 1.00 40.50 ATOM 3889 C PRO 3199 −21.737 39.521 29.190 1.00 39.48 ATOM 3890 O PRO 3199 −20.756 39.388 28.458 1.00 39.70 ATOM 3891 N ASP 3200 −22.699 40.396 28.939 1.00 40.10 ATOM 3892 CA ASP 3200 −22.660 41.248 27.757 1.00 39.53 ATOM 3893 CB ASP 3200 −24.061 41.776 27.485 1.00 41.17 ATOM 3894 CG ASP 3200 −25.128 40.902 28.414 1.00 46.36 ATOM 3895 OD1 ASP 3200 −25.218 39.708 27.744 1.00 48.73 ATOM 3896 OD2 ASP 3200 −25.865 41.403 28.995 1.00 47.90 ATOM 3897 C ASP 3200 −21.686 42.402 27.979 1.00 37.25 ATOM 3898 O ASP 3200 −21.412 43.182 27.071 1.00 35.42 ATOM 3899 N HIS 3201 −21.165 42.500 29.198 1.00 36.00 ATOM 3900 CA HIS 3201 −20.219 43.552 29.555 1.00 35.44 ATOM 3901 CB HIS 3201 −19.992 43.579 31.059 1.00 36.77 ATOM 3902 CG HIS 3201 −21.091 44.239 31.825 1.00 37.96 ATOM 3903 CD2 HIS 3201 −21.052 45.092 32.874 1.00 39.27 ATOM 3904 ND1 HIS 3201 −22.423 44.025 31.550 1.00 36.90 ATOM 3905 CE1 HIS 3201 −23.160 44.721 32.397 1.00 39.05 ATOM 3906 NE2 HIS 3201 −22.353 45.376 33.211 1.00 40.51 ATOM 3907 C HIS 3201 −18.878 43.361 28.882 1.00 34.44 ATOM 3908 O HIS 3201 −18.025 44.238 28.941 1.00 33.90 ATOM 3909 N ARG 3202 −18.684 42.208 28.256 1.00 33.68 ATOM 3910 CA ARG 3202 −17.420 41.932 27.592 1.00 32.76 ATOM 3911 CB ARG 3202 −16.428 41.326 28.579 1.00 28.87 ATOM 3912 CG ARG 3202 −16.799 39.929 29.043 1.00 27.45 ATOM 3913 CD ARG 3202 −15.666 39.314 29.833 1.00 24.91 ATOM 3914 NE ARG 3202 −14.431 39.318 29.059 1.00 23.34 ATOM 3915 CZ ARG 3202 −13.899 38.242 28.491 1.00 25.12 ATOM 3916 NH1 ARG 3202 −14.499 37.066 28.618 1.00 26.45 ATOM 3917 NH2 ARG 3202 −12.771 38.337 27.791 1.00 24.21 ATOM 3918 C ARG 3202 −17.594 40.971 26.433 1.00 34.21 ATOM 3919 O ARG 3202 −18.490 40.125 26.442 1.00 37.16 ATOM 3920 N ILE 3203 −16.731 41.095 25.433 1.00 33.29 ATOM 3921 CA ILE 3203 −16.800 40.198 24.295 1.00 32.59 ATOM 3922 CB ILE 3203 −15.846 40.635 23.173 1.00 32.07 ATOM 3923 CG2 ILE 3203 −16.124 39.824 21.909 1.00 28.91 ATOM 3924 CG1 ILE 3203 −16.034 42.129 22.899 1.00 29.28 ATOM 3925 CD1 ILE 3203 −15.099 42.673 21.856 1.00 29.62 ATOM 3926 C ILE 3203 −16.374 38.835 24.821 1.00 32.99 ATOM 3927 O ILE 3203 −15.434 38.729 25.608 1.00 33.73 ATOM 3928 N GLY 3204 −17.072 37.796 24.387 1.00 32.52 ATOM 3929 CA GLY 3204 −16.759 36.460 24.848 1.00 30.79 ATOM 3930 C GLY 3204 −17.756 36.066 25.918 1.00 31.96 ATOM 3931 O GLY 3204 −18.175 34.911 25.991 1.00 30.10 ATOM 3932 N GLY 3205 −18.150 37.039 26.740 1.00 32.74 ATOM 3933 CA GLY 3205 −19.100 36.775 27.808 1.00 32.98 ATOM 3934 C GLY 3205 −18.375 36.147 28.975 1.00 33.96 ATOM 3935 O GLY 3205 −17.243 36.536 29.277 1.00 35.51 ATOM 3936 N TYR 3206 −19.010 35.189 29.643 1.00 33.42 ATOM 3937 CA TYR 3206 −18.360 34.507 30.760 1.00 33.07 ATOM 3938 CB TYR 3206 −17.815 35.531 31.779 1.00 29.93 ATOM 3939 CG TYR 3206 −18.845 36.172 32.686 1.00 30.96 ATOM 3940 CD1 TYR 3206 −19.494 35.426 33.682 1.00 31.46 ATOM 3941 CE1 TYR 3206 −20.397 36.012 34.552 1.00 27.77 ATOM 3942 CD2 TYR 3206 −19.142 37.532 32.585 1.00 31.20 ATOM 3943 CE2 TYR 3206 −20.047 38.129 33.458 1.00 30.81 ATOM 3944 CZ TYR 3206 −20.667 37.356 34.436 1.00 31.02 ATOM 3945 OH TYR 3206 −21.549 37.919 35.317 1.00 35.48 ATOM 3946 C TYR 3206 −19.280 33.509 31.445 1.00 32.14 ATOM 3947 O TYR 3206 −20.448 33.787 31.672 1.00 32.65 ATOM 3948 N ALA 3207 −18.752 32.337 31.770 1.00 33.10 ATOM 3949 CA ALA 3207 −19.554 31.326 32.440 1.00 33.85 ATOM 3950 CB ALA 3207 −19.270 29.947 31.841 1.00 31.32 ATOM 3951 C ALA 3207 −19.266 31.321 33.944 1.00 35.21 ATOM 3952 O ALA 3207 −18.191 31.727 34.396 1.00 38.16 ATOM 3953 N VAL 3208 −20.245 30.871 34.716 1.00 34.20 ATOM 3954 CA VAL 3208 −20.107 30.776 36.160 1.00 32.45 ATOM 3955 CB VAL 3208 −21.056 31.767 36.885 1.00 30.98 ATOM 3956 CG1 VAL 3208 −20.906 31.625 38.392 1.00 33.08 ATOM 3957 CG2 VAL 3208 −20.753 33.183 36.455 1.00 28.98 ATOM 3958 C VAL 3208 −20.487 29.348 36.551 1.00 32.33 ATOM 3959 O VAL 3208 −21.647 28.960 36.446 1.00 34.87 ATOM 3960 N ALA 3209 −19.514 28.552 36.967 1.00 30.63 ATOM 3961 CA ALA 3209 −19.821 27.194 37.383 1.00 31.14 ATOM 3962 CB ALA 3209 −18.619 26.293 37.167 1.00 32.43 ATOM 3963 C ALA 3209 −20.212 27.232 38.864 1.00 31.16 ATOM 3964 O ALA 3209 −19.363 27.196 39.748 1.00 29.00 ATOM 3965 N TYR 3210 −21.509 27.315 39.126 1.00 33.46 ATOM 3966 CA TYR 3210 −21.997 27.371 40.494 1.00 36.52 ATOM 3967 CB TYR 3210 −23.525 27.484 40.498 1.00 36.08 ATOM 3968 CG TYR 3210 −24.012 28.661 39.682 1.00 42.00 ATOM 3969 CD1 TYR 3210 −24.258 28.533 38.312 1.00 43.49 ATOM 3970 CE1 TYR 3210 −24.632 29.639 37.536 1.00 44.89 ATOM 3971 CD2 TYR 3210 −24.155 29.926 40.262 1.00 44.22 ATOM 3972 CE2 TYR 3210 −24.528 31.040 39.496 1.00 45.78 ATOM 3973 CZ TYR 3210 −24.761 30.887 38.136 1.00 46.22 ATOM 3974 OH TYR 3210 −25.109 31.983 37.377 1.00 47.71 ATOM 3975 C TYR 3210 −21.537 26.169 41.320 1.00 36.86 ATOM 3976 O TYR 3210 −21.359 26.259 42.535 1.00 38.85 ATOM 3977 N ALA 3211 −21.319 25.043 40.665 1.00 35.89 ATOM 3978 CA ALA 3211 −20.884 23.873 41.395 1.00 34.71 ATOM 3979 CB ALA 3211 −20.942 22.654 40.489 1.00 36.35 ATOM 3980 C ALA 3211 −19.463 24.079 41.923 1.00 34.75 ATOM 3981 O ALA 3211 −19.112 23.608 43.002 1.00 33.71 ATOM 3982 N THR 3212 −18.656 24.813 41.167 1.00 34.33 ATOM 3983 CA THR 3212 −17.263 25.044 41.532 1.00 32.16 ATOM 3984 CB THR 3212 −16.363 24.782 40.332 1.00 34.28 ATOM 3985 OG1 THR 3212 −16.919 23.714 39.561 1.00 40.52 ATOM 3986 CG2 THR 3212 −14.969 24.386 40.784 1.00 34.26 ATOM 3987 C THR 3212 −16.965 26.449 42.032 1.00 30.76 ATOM 3988 O THR 3212 −15.818 26.881 42.020 1.00 27.65 ATOM 3989 N TRP 3213 −18.001 27.166 42.447 1.00 31.81 ATOM 3990 CA TRP 3213 −17.857 28.525 42.968 1.00 29.81 ATOM 3991 CB TRP 3213 −17.441 28.457 44.447 1.00 28.25 ATOM 3992 CG TRP 3213 −18.421 27.688 45.280 1.00 27.86 ATOM 3993 CD2 TRP 3213 −19.641 28.189 45.843 1.00 28.56 ATOM 3994 CE2 TRP 3213 −20.288 27.104 46.470 1.00 27.84 ATOM 3995 CE3 TRP 3213 −20.248 29.450 45.879 1.00 28.08 ATOM 3996 CD1 TRP 3213 −18.380 26.360 45.580 1.00 27.37 ATOM 3997 NE1 TRP 3213 −19.497 26.001 46.293 1.00 27.93 ATOM 3998 CZ2 TRP 3213 −21.516 27.240 47.123 1.00 29.13 ATOM 3999 CZ3 TRP 3213 −21.468 29.586 46.526 1.00 28.50 ATOM 4000 CH2 TRP 3213 −22.088 28.487 47.141 1.00 29.91 ATOM 4001 C TRP 3213 −16.877 29.390 42.167 1.00 29.53 ATOM 4002 O TRP 3213 −16.084 30.166 42.716 1.00 26.76 ATOM 4003 N SER 3214 −16.949 29.274 40.851 1.00 30.34 ATOM 4004 CA SER 3214 −16.047 30.048 40.018 1.00 31.47 ATOM 4005 CB SER 3214 −14.866 29.167 39.594 1.00 31.73 ATOM 4006 OG SER 3214 −15.322 27.911 39.137 1.00 34.16 ATOM 4007 C SER 3214 −16.691 30.688 38.792 1.00 30.14 ATOM 4008 O SER 3214 −17.837 30.396 38.442 1.00 30.07 ATOM 4009 N ILE 3215 −15.941 31.595 38.173 1.00 28.38 ATOM 4010 CA ILE 3215 −16.368 32.294 36.970 1.00 27.47 ATOM 4011 CB ILE 3215 −16.488 33.817 37.180 1.00 28.53 ATOM 4012 CG2 ILE 3215 −15.297 34.338 37.991 1.00 29.31 ATOM 4013 CG1 ILE 3215 −16.568 34.502 35.809 1.00 27.46 ATOM 4014 CD1 ILE 3215 −16.680 35.996 35.844 1.00 24.34 ATOM 4015 C ILE 3215 −15.279 32.049 35.945 1.00 27.26 ATOM 4016 O ILE 3215 −14.087 32.067 36.264 1.00 28.20 ATOM 4017 N ILE 3216 −15.677 31.832 34.707 1.00 25.77 ATOM 4018 CA ILE 3216 −14.691 31.556 33.690 1.00 26.67 ATOM 4019 CB ILE 3216 −14.832 30.099 33.197 1.00 26.81 ATOM 4020 CG2 ILE 3216 −13.809 29.809 32.118 1.00 28.49 ATOM 4021 CG1 ILE 3216 −14.615 29.144 34.373 1.00 28.35 ATOM 4022 CD1 ILE 3216 −14.607 27.674 34.002 1.00 26.95 ATOM 4023 C ILE 3216 −14.762 32.504 32.511 1.00 26.79 ATOM 4024 O ILE 3216 −15.796 32.579 31.828 1.00 24.85 ATOM 4025 N MET 3217 −13.654 33.214 32.277 1.00 25.00 ATOM 4026 CA MET 3217 −13.559 34.166 31.174 1.00 25.44 ATOM 4027 CE MET 3217 −13.172 35.562 31.672 1.00 25.70 ATOM 4028 CG MET 3217 −14.091 36.180 32.710 1.00 29.30 ATOM 4029 SD MET 3217 −13.594 37.900 33.045 1.00 33.66 ATOM 4030 CE MET 3217 −12.001 37.656 33.913 1.00 30.93 ATOM 4031 C MET 3217 −12.530 33.740 30.137 1.00 24.78 ATOM 4032 O MET 3217 −11.321 33.788 30.391 1.00 27.30 ATOM 4033 N ASP 3218 −13.006 33.336 28.964 1.00 22.50 ATOM 4034 CA ASP 3218 −12.108 32.936 27.892 1.00 20.29 ATOM 4035 CB ASP 3218 −12.861 32.100 26.846 1.00 23.60 ATOM 4036 CG ASP 3218 −12.907 30.607 27.200 1.00 29.86 ATOM 4037 OD1 ASP 3218 −12.875 30.278 28.407 1.00 33.46 ATOM 4038 OD2 ASP 3218 −12.984 29.755 26.276 1.00 32.53 ATOM 4039 C ASP 3218 −11.498 34.175 27.239 1.00 18.77 ATOM 4040 O ASP 3218 −12.027 35.283 27.338 1.00 14.25 ATOM 4041 N SER 3219 −10.353 33.979 26.602 1.00 21.90 ATOM 4042 CA SER 3219 −9.656 35.047 25.905 1.00 22.27 ATOM 4043 CB SER 3219 −10.160 35.142 24.472 1.00 25.60 ATOM 4044 OG SER 3219 −9.655 36.309 23.851 1.00 33.16 ATOM 4045 C SER 3219 −9.782 36.404 26.556 1.00 21.83 ATOM 4046 O SER 3219 −10.606 37.233 26.169 1.00 22.35 ATOM 4047 N VAL 3220 −8.946 36.627 27.553 1.00 23.69 ATOM 4048 CA VAL 3220 −8.931 37.897 28.255 1.00 21.63 ATOM 4049 CB VAL 3220 −8.254 37.761 29.631 1.00 21.56 ATOM 4050 CG1 VAL 3220 −9.053 36.809 30.515 1.00 23.43 ATOM 4051 CG2 VAL 3220 −6.830 37.246 29.449 1.00 19.83 ATOM 4052 C VAL 3220 −8.104 38.860 27.419 1.00 20.60 ATOM 4053 O VAL 3220 −7.209 38.452 26.662 1.00 19.89 ATOM 4054 N VAL 3221 −8.409 40.139 27.561 1.00 19.29 ATOM 4055 CA VAL 3221 −7.684 41.179 26.851 1.00 19.94 ATOM 4056 CE VAL 3221 −8.402 41.569 25.548 1.00 21.60 ATOM 4057 CG1 VAL 3221 −8.003 40.600 24.424 1.00 17.47 ATOM 4058 CG2 VAL 3221 −9.919 41.548 25.778 1.00 18.75 ATOM 4059 C VAL 3221 −7.657 42.359 27.797 1.00 19.84 ATOM 4060 O VAL 3221 −8.501 42.446 28.698 1.00 18.89 ATOM 4061 N PRO 3222 −6.695 43.280 27.613 1.00 19.44 ATOM 4062 CD PRO 3222 −5.765 43.319 26.469 1.00 19.55 ATOM 4063 CA PRO 3222 −6.531 44.477 28.449 1.00 18.50 ATOM 4064 CB PRO 3222 −5.757 45.420 27.542 1.00 17.22 ATOM 4065 CG PRO 3222 −4.842 44.490 26.830 1.00 16.82 ATOM 4066 C PRO 3222 −7.825 45.091 28.980 1.00 19.70 ATOM 4067 O PRO 3222 −7.914 45.418 30.164 1.00 20.49 ATOM 4068 N SER 3223 −8.831 45.231 28.122 1.00 20.64 ATOM 4069 CA SER 3223 −10.106 45.805 28.552 1.00 22.52 ATOM 4070 CB SER 3223 −11.114 45.832 27.390 1.00 21.18 ATOM 4071 OG SER 3223 −11.721 44.565 27.215 1.00 22.75 ATOM 4072 C SER 3223 −10.698 45.001 29.717 1.00 24.89 ATOM 4073 O SER 3223 −11.542 45.502 30.473 1.00 27.76 ATOM 4074 N ASP 3224 −10.262 43.754 29.864 1.00 24.30 ATOM 4075 CA ASP 3224 −10.767 42.923 30.942 1.00 24.39 ATOM 4076 CB ASP 3224 −10.550 41.438 30.629 1.00 24.86 ATOM 4077 CG ASP 3224 −11.488 40.924 29.548 1.00 25.47 ATOM 4078 OD1 ASP 3224 −12.696 41.247 29.630 1.00 20.81 ATOM 4079 OD2 ASP 3224 −11.017 40.194 28.634 1.00 23.43 ATOM 4080 C ASP 3224 −10.139 43.260 32.289 1.00 24.51 ATOM 4081 O ASP 3224 −10.729 42.972 33.335 1.00 24.74 ATOM 4082 N ALA 3225 −8.955 43.873 32.270 1.00 24.04 ATOM 4083 CA ALA 3225 −8.258 44.230 33.509 1.00 23.28 ATOM 4084 CB ALA 3225 −7.059 45.133 33.199 1.00 19.86 ATOM 4085 C ALA 3225 −9.186 44.913 34.517 1.00 23.54 ATOM 4086 O ALA 3225 −9.977 45.792 34.155 1.00 23.35 ATOM 4087 N GLY 3226 −9.095 44.495 35.779 1.00 24.35 ATOM 4088 CA GLY 3226 −9.920 45.087 36.823 1.00 25.68 ATOM 4089 C GLY 3226 −10.098 44.208 38.049 1.00 27.63 ATOM 4090 O GLY 3226 −9.588 43.080 38.114 1.00 28.87 ATOM 4091 N ASN 3227 −10.817 44.728 39.037 1.00 27.73 ATOM 4092 CA ASN 3227 −11.081 43.971 40.258 1.00 28.14 ATOM 4093 CB ASN 3227 −11.330 44.902 41.444 1.00 27.66 ATOM 4094 CG ASN 3227 −10.204 45.866 41.659 1.00 33.30 ATOM 4095 OD1 ASN 3227 −9.038 45.467 41.717 1.00 34.86 ATOM 4096 ND2 ASN 3227 −10.535 47.155 41.777 1.00 35.26 ATOM 4097 C ASN 3227 −12.328 43.132 40.047 1.00 27.43 ATOM 4098 O ASN 3227 −13.320 43.615 39.500 1.00 29.97 ATOM 4099 N TYR 3228 −12.279 41.877 40.475 1.00 23.65 ATOM 4100 CA TYR 3228 −13.427 41.005 40.354 1.00 19.54 ATOM 4101 CB TYR 3228 −13.120 39.857 39.420 1.00 16.85 ATOM 4102 CG TYR 3228 −13.022 40.318 38.000 1.00 17.95 ATOM 4103 CD1 TYR 3228 −11.925 41.064 37.563 1.00 16.43 ATOM 4104 CE1 TYR 3228 −11.832 41.510 36.248 1.00 17.97 ATOM 4105 CD2 TYR 3228 −14.035 40.032 37.089 1.00 18.73 ATOM 4106 CE2 TYR 3228 −13.961 40.477 35.770 1.00 20.90 ATOM 4107 CZ TYR 3228 −12.855 41.214 35.350 1.00 20.24 ATOM 4108 OH TYR 3228 −12.764 41.617 34.030 1.00 18.53 ATOM 4109 C TYR 3228 −13.787 40.503 41.730 1.00 20.76 ATOM 4110 O TYR 3228 −12.956 39.934 42.440 1.00 20.32 ATOM 4111 N THR 3229 −15.039 40.723 42.107 1.00 19.38 ATOM 4112 CA THR 3229 −15.481 40.331 43.421 1.00 19.14 ATOM 4113 CB THR 3229 −15.972 41.555 44.229 1.00 19.74 ATOM 4114 OG1 THR 3229 −14.893 42.487 44.387 1.00 15.99 ATOM 4115 CG2 THR 3229 −16.465 41.122 45.611 1.00 18.22 ATOM 4116 C THR 3229 −16.581 39.314 43.413 1.00 20.02 ATOM 4117 O THR 3229 −17.611 39.495 42.764 1.00 21.54 ATOM 4118 N CYS 3230 −16.360 38.227 44.135 1.00 18.45 ATOM 4119 CA CYS 3230 −17.393 37.234 44.226 1.00 18.73 ATOM 4120 C CYS 3230 −18.151 37.601 45.487 1.00 16.50 ATOM 4121 O CYS 3230 −17.580 38.147 46.423 1.00 15.77 ATOM 4122 CB CYS 3230 −16.805 35.832 44.344 1.00 20.59 ATOM 4123 SG CYS 3230 −15.821 35.551 45.839 1.00 28.94 ATOM 4124 N ILE 3231 −19.447 37.339 45.497 1.00 15.83 ATOM 4125 CA ILE 3231 −20.240 37.632 46.663 1.00 16.36 ATOM 4126 CB ILE 3231 −21.087 38.880 46.449 1.00 17.80 ATOM 4127 CG2 ILE 3231 −22.099 39.031 47.572 1.00 17.03 ATOM 4128 CG1 ILE 3231 −20.155 40.096 46.402 1.00 17.70 ATOM 4129 CD1 ILE 3231 −20.854 41.396 46.183 1.00 17.16 ATOM 4130 C ILE 3231 −21.117 36.449 46.978 1.00 17.26 ATOM 4131 O ILE 3231 −22.016 36.111 46.209 1.00 21.97 ATOM 4132 N VAL 3232 −20.827 35.815 48.112 1.00 16.47 ATOM 4133 CA VAL 3232 −21.559 34.651 48.589 1.00 16.73 ATOM 4134 CB VAL 3232 −20.592 33.560 49.054 1.00 16.46 ATOM 4135 CG1 VAL 3232 −21.368 32.336 49.523 1.00 15.36 ATOM 4136 CG2 VAL 3232 −19.640 33.204 47.919 1.00 15.79 ATOM 4137 C VAL 3232 −22.446 35.062 49.752 1.00 19.52 ATOM 4138 O VAL 3232 −21.998 35.738 50.679 1.00 19.11 ATOM 4139 N GLU 3233 −23.710 34.660 49.703 1.00 23.22 ATOM 4140 CA GLU 3233 −24.640 35.027 50.761 1.00 28.85 ATOM 4141 CB GLU 3233 −25.045 36.495 50.607 1.00 35.57 ATOM 4142 CG GLU 3233 −25.465 36.859 49.189 1.00 45.86 ATOM 4143 CD GLU 3233 −25.881 38.318 49.041 1.00 52.61 ATOM 4144 OE1 GLU 3233 −25.205 39.196 49.625 1.00 56.75 ATOM 4145 OE2 GLU 3233 −26.876 38.591 48.328 1.00 57.00 ATOM 4146 C GLU 3233 −25.906 34.192 50.799 1.00 28.73 ATOM 4147 O GLU 3233 −26.337 33.642 49.779 1.00 27.70 ATOM 4148 N ASN 3234 −26.486 34.103 51.996 1.00 26.80 ATOM 4149 CA ASN 3234 −27.738 33.394 52.223 1.00 25.14 ATOM 4150 CB ASN 3234 −27.515 31.945 52.709 1.00 24.39 ATOM 4151 CG ASN 3234 −26.752 31.856 54.025 1.00 26.09 ATOM 4152 OD1 ASN 3234 −26.658 32.824 54.781 1.00 25.60 ATOM 4153 ND2 ASN 3234 −26.217 30.668 54.313 1.00 27.06 ATOM 4154 C ASN 3234 −28.500 34.206 53.260 1.00 25.03 ATOM 4155 O ASN 3234 −28.059 35.292 53.649 1.00 21.71 ATOM 4156 N ALA 3235 −29.639 33.688 53.710 1.00 25.62 ATOM 4157 CA ALA 3235 −30.454 34.396 54.692 1.00 23.50 ATOM 4158 CB ALA 3235 −31.732 33.593 54.997 1.00 22.56 ATOM 4159 C ALA 3235 −29.701 34.677 55.987 1.00 22.86 ATOM 4160 O ALA 3235 −30.190 35.405 56.846 1.00 25.91 ATOM 4161 N TYR 3236 −28.503 34.134 56.134 1.00 20.91 ATOM 4162 CA TYR 3236 −27.782 34.342 57.380 1.00 21.67 ATOM 4163 CB TYR 3236 −27.652 33.010 58.105 1.00 24.91 ATOM 4164 CG TYR 3236 −28.992 32.447 58.456 1.00 26.84 ATOM 4165 CD1 TYR 3236 −29.739 31.731 57.519 1.00 30.31 ATOM 4166 CE1 TYR 3236 −31.017 31.280 57.820 1.00 32.58 ATOM 4167 CD2 TYR 3236 −29.552 32.692 59.700 1.00 27.82 ATOM 4168 CE2 TYR 3236 −30.824 32.248 60.016 1.00 32.47 ATOM 4169 CZ TYR 3236 −31.554 31.545 59.075 1.00 34.13 ATOM 4170 OH TYR 3236 −32.822 31.132 59.398 1.00 34.11 ATOM 4171 C TYR 3236 −26.426 35.013 57.330 1.00 20.53 ATOM 4172 O TYR 3236 −25.739 35.076 58.345 1.00 17.76 ATOM 4173 N GLY 3237 −26.039 35.511 56.163 1.00 20.51 ATOM 4174 CA GLY 3237 −24.756 36.169 56.060 1.00 20.51 ATOM 4175 C GLY 3237 −24.249 36.284 54.644 1.00 22.21 ATOM 4176 O GLY 3237 −24.719 35.593 53.740 1.00 24.70 ATOM 4177 N SER 3238 −23.278 37.167 54.459 1.00 22.08 ATOM 4178 CA SER 3238 −22.687 37.385 53.159 1.00 23.41 ATOM 4179 CB SER 3238 −23.323 38.592 52.480 1.00 24.80 ATOM 4180 OG SER 3238 −22.605 38.916 51.301 1.00 29.81 ATOM 4181 C SER 3238 −21.206 37.637 53.312 1.00 23.57 ATOM 4182 O SER 3238 −20.793 38.467 54.109 1.00 25.04 ATOM 4183 N ILE 3239 −20.403 36.918 52.549 1.00 24.19 ATOM 4184 CA ILE 3239 −18.964 37.111 52.602 1.00 25.62 ATOM 4185 CB ILE 3239 −18.230 35.806 53.039 1.00 24.95 ATOM 4186 CG2 ILE 3239 −18.633 35.441 54.456 1.00 22.17 ATOM 4187 CG1 ILE 3239 −18.587 34.641 52.107 1.00 25.70 ATOM 4188 CD1 ILE 3239 −17.955 33.301 52.512 1.00 20.71 ATOM 4189 C ILE 3239 −18.542 37.528 51.207 1.00 26.33 ATOM 4190 O ILE 3239 −19.295 37.345 50.260 1.00 28.84 ATOM 4191 N ASN 3240 −17.360 38.112 51.073 1.00 27.41 ATOM 4192 CA ASN 3240 −16.892 38.537 49.759 1.00 28.02 ATOM 4193 CB ASN 3240 −17.263 39.990 49.501 1.00 31.85 ATOM 4194 CG ASN 3240 −16.718 40.912 50.555 1.00 34.70 ATOM 4195 OD1 ASN 3240 −15.580 40.756 51.006 1.00 38.73 ATOM 4196 ND2 ASN 3240 −17.522 41.890 50.956 1.00 38.85 ATOM 4197 C ASN 3240 −15.392 38.397 49.629 1.00 26.81 ATOM 4198 O ASN 3240 −14.688 38.163 50.610 1.00 27.58 ATOM 4199 N HIS 3241 −14.904 38.555 48.409 1.00 24.50 ATOM 4200 CA HIS 3241 −13.481 38.452 48.159 1.00 24.61 ATOM 4201 CB HIS 3241 −13.059 36.985 48.084 1.00 27.80 ATOM 4202 CG HIS 3241 −11.579 36.796 47.994 1.00 30.76 ATOM 4203 CD2 HIS 3241 −10.801 36.293 47.006 1.00 32.96 ATOM 4204 ND1 HIS 3241 −10.719 37.187 48.998 1.00 31.80 ATOM 4205 CE1 HIS 3241 −9.475 36.935 48.633 1.00 32.92 ATOM 4206 NE2 HIS 3241 −9.497 36.394 47.426 1.00 34.12 ATOM 4207 C HIS 3241 −13.234 39.125 46.837 1.00 22.95 ATOM 4208 O HIS 3241 −14.061 39.022 45.939 1.00 26.24 ATOM 4209 N THR 3242 −12.112 39.820 46.706 1.00 20.64 ATOM 4210 CA THR 3242 −11.828 40.499 45.453 1.00 21.13 ATOM 4211 CB THR 3242 −11.786 42.047 45.618 1.00 20.79 ATOM 4212 OG1 THR 3242 −13.034 42.514 46.145 1.00 20.51 ATOM 4213 CG2 THR 3242 −11.545 42.723 44.260 1.00 19.11 ATOM 4214 C THR 3242 −10.507 40.055 44.865 1.00 20.94 ATOM 4215 O THR 3242 −9.541 39.852 45.590 1.00 20.69 ATOM 4216 N TYR 3243 −10.482 39.909 43.542 1.00 20.75 ATOM 4217 CA TYR 3243 −9.283 39.510 42.821 1.00 20.72 ATOM 4218 CB TYR 3243 −9.511 38.227 42.024 1.00 19.39 ATOM 4219 CG TYR 3243 −9.685 36.958 42.823 1.00 23.05 ATOM 4220 CD1 TYR 3243 −10.953 36.433 43.067 1.00 24.01 ATOM 4221 CE1 TYR 3243 −11.113 35.229 43.758 1.00 25.82 ATOM 4222 CD2 TYR 3243 −8.572 36.249 43.296 1.00 22.82 ATOM 4223 CE2 TYR 3243 −8.719 35.047 43.987 1.00 21.94 ATOM 4224 CZ TYR 3243 −9.992 34.542 44.216 1.00 23.52 ATOM 4225 OH TYR 3243 −10.156 33.357 44.902 1.00 22.85 ATOM 4226 C TYR 3243 −8.899 40.593 41.828 1.00 21.98 ATOM 4227 O TYR 3243 −9.756 41.162 41.150 1.00 23.12 ATOM 4228 N ALA 3244 −7.609 40.882 41.731 1.00 24.08 ATOM 4229 CA ALA 3244 −7.152 41.874 40.766 1.00 23.35 ATOM 4230 CB ALA 3244 −5.918 42.613 41.300 1.00 20.36 ATOM 4231 C ALA 3244 −6.800 41.067 39.517 1.00 22.90 ATOM 4232 O ALA 3244 −6.313 39.942 39.621 1.00 21.75 ATOM 4233 N LEU 3245 −7.087 41.601 38.337 1.00 23.40 ATOM 4234 CA LEU 3245 −6.722 40.877 37.129 1.00 23.04 ATOM 4235 CB LEU 3245 −7.949 40.348 36.383 1.00 20.49 ATOM 4236 CG LEU 3245 −7.587 39.202 35.416 1.00 18.53 ATOM 4237 CD1 LEU 3245 −8.834 38.515 34.932 1.00 24.70 ATOM 4238 CD2 LEU 3245 −6.804 39.717 34.248 1.00 15.82 ATOM 4239 C LEU 3245 −5.906 41.759 36.202 1.00 22.88 ATOM 4240 O LEU 3245 −6.354 42.818 35.770 1.00 23.46 ATOM 4241 N ASP 3246 −4.693 41.327 35.910 1.00 22.07 ATOM 4242 CA ASP 3246 −3.872 42.098 35.014 1.00 26.75 ATOM 4243 CB ASP 3246 −2.591 42.552 35.706 1.00 32.91 ATOM 4244 CG ASP 3246 −1.813 43.540 34.871 1.00 38.77 ATOM 4245 OD1 ASP 3246 −2.431 44.502 34.348 1.00 42.43 ATOM 4246 OD2 ASP 3246 −0.586 43.353 34.738 1.00 43.87 ATOM 4247 C ASP 3246 −3.572 41.224 33.808 1.00 26.40 ATOM 4248 O ASP 3246 −3.356 40.017 33.942 1.00 24.28 ATOM 4249 N VAL 3247 −3.582 41.845 32.632 1.00 26.01 ATOM 4250 CA VAL 3247 −3.351 41.160 31.365 1.00 24.26 ATOM 4251 CB VAL 3247 −4.631 41.197 30.500 1.00 25.02 ATOM 4252 CG1 VAL 3247 −4.390 40.513 29.147 1.00 24.28 ATOM 4253 CG2 VAL 3247 −5.775 40.534 31.254 1.00 24.22 ATOM 4254 C VAL 3247 −2.228 41.828 30.592 1.00 23.02 ATOM 4255 O VAL 3247 −2.191 43.048 30.493 1.00 26.47 ATOM 4256 N VAL 3248 −1.317 41.037 30.041 1.00 21.59 ATOM 4257 CA VAL 3248 −0.208 41.596 29.274 1.00 21.39 ATOM 4258 CB VAL 3248 1.146 41.351 29.974 1.00 22.58 ATOM 4259 CG1 VAL 3248 2.256 42.033 29.211 1.00 24.91 ATOM 4260 CG2 VAL 3248 1.101 41.872 31.376 1.00 25.63 ATOM 4261 C VAL 3248 −0.131 40.978 27.881 1.00 21.94 ATOM 4262 O VAL 3248 −0.018 39.749 27.728 1.00 22.78 ATOM 4263 N GLU 3249 −0.191 41.831 26.868 1.00 18.89 ATOM 4264 CA GLU 3249 0.106 41.373 25.498 1.00 20.08 ATOM 4265 CB GLU 3249 −0.585 42.473 24.547 1.00 23.18 ATOM 4266 CG GLU 3249 −2.023 42.896 24.804 1.00 31.25 ATOM 4267 CD GLU 3249 −2.467 44.090 23.971 1.00 34.98 ATOM 4268 OE1 GLU 3249 −1.752 45.120 23.967 1.00 36.08 ATOM 4269 OE2 GLU 3249 −3.545 44.002 23.335 1.00 39.35 ATOM 4270 C GLU 3249 1.355 41.047 25.230 1.00 20.01 ATOM 4271 O GLU 3249 2.214 41.920 25.359 1.00 18.96 ATOM 4272 N ARG 3250 1.637 39.790 24.874 1.00 19.49 ATOM 4273 CA ARG 3250 3.010 39.363 24.589 1.00 17.58 ATOM 4274 CB ARG 3250 3.246 37.913 25.063 1.00 15.61 ATOM 4275 CG ARG 3250 3.047 37.673 26.568 1.00 15.26 ATOM 4276 CD ARG 3250 3.778 38.702 27.435 1.00 13.10 ATOM 4277 NE ARG 3250 5.231 38.616 27.308 1.00 15.86 ATOM 4278 CZ ARG 3250 5.984 37.658 27.849 1.00 16.04 ATOM 4279 NH1 ARG 3250 5.436 36.682 28.573 1.00 10.22 ATOM 4280 NH2 ARG 3250 7.294 37.679 27.655 1.00 12.79 ATOM 4281 C ARG 3250 3.303 39.487 23.096 1.00 15.82 ATOM 4282 O ARG 3250 2.445 39.189 22.273 1.00 17.84 ATOM 4283 N ALA 3251 4.513 39.930 22.753 1.00 15.48 ATOM 4284 CA ALA 3251 4.898 40.119 21.354 1.00 14.42 ATOM 4285 CB ALA 3251 5.215 41.580 21.090 1.00 13.95 ATOM 4286 C ALA 3251 6.076 39.269 20.952 1.00 15.60 ATOM 4287 O ALA 3251 7.224 39.691 21.019 1.00 17.78 ATOM 4288 N PRO 3252 5.802 38.051 20.517 1.00 16.45 ATOM 4289 CD PRO 3252 4.527 37.344 20.712 1.00 14.69 ATOM 4290 CA PRO 3252 6.853 37.129 20.098 1.00 15.71 ATOM 4291 CB PRO 3252 6.210 35.778 20.345 1.00 11.93 ATOM 4292 CG PRO 3252 4.781 36.053 20.008 1.00 11.24 ATOM 4293 C PRO 3252 7.317 37.305 18.656 1.00 16.31 ATOM 4294 O PRO 3252 7.055 36.464 17.812 1.00 19.07 ATOM 4295 N HIS 3253 8.005 38.406 18.380 1.00 18.22 ATOM 4296 CA HIS 3253 8.536 38.693 17.048 1.00 18.62 ATOM 4297 CB HIS 3253 7.727 39.798 16.362 1.00 20.70 ATOM 4298 CG HIS 3253 6.250 39.679 16.556 1.00 25.37 ATOM 4299 CD2 HIS 3253 5.376 40.459 17.236 1.00 26.10 ATOM 4300 ND1 HIS 3253 5.519 30.617 16.066 1.00 27.46 ATOM 4301 CE1 HIS 3253 4.256 38.744 16.441 1.00 28.08 ATOM 4302 NE2 HIS 3253 4.143 39.852 17.152 1.00 29.83 ATOM 4303 C HIS 3253 9.956 39.198 17.291 1.00 18.94 ATOM 4304 O HIS 3253 10.344 39.428 18.438 1.00 15.09 ATOM 4305 N ARG 3254 10.744 39.357 16.232 1.00 20.26 ATOM 4306 CA ARG 3254 12.089 39.872 16.425 1.00 21.29 ATOM 4307 CB ARG 3254 12.957 39.675 15.168 1.00 23.70 ATOM 4308 CG ARG 3254 12.702 40.615 13.987 1.00 24.93 ATOM 4309 CD ARG 3254 11.433 40.262 13.215 1.00 31.22 ATOM 4310 NE ARG 3254 11.665 40.088 11.774 1.00 34.34 ATOM 4311 CZ ARG 3254 12.155 41.024 10.961 1.00 34.35 ATOM 4312 NH1 ARG 3254 12.483 42.222 11.425 1.00 37.58 ATOM 4313 NH2 ARG 3254 12.304 40.771 9.674 1.00 30.94 ATOM 4314 C ARG 3254 11.906 41.357 16.738 1.00 20.88 ATOM 4315 O ARG 3254 10.789 41.878 16.686 1.00 18.88 ATOM 4316 N PRO 3255 12.987 42.054 17.095 1.00 19.70 ATOM 4317 CD PRO 3255 14.381 41.624 17.300 1.00 18.17 ATOM 4318 CA PRO 3255 12.821 43.480 17.396 1.00 19.74 ATOM 4319 CB PRO 3255 14.238 43.912 17.802 1.00 20.14 ATOM 4320 CG PRO 3255 14.863 42.624 18.296 1.00 18.36 ATOM 4321 C PRO 3255 12.299 44.281 16.188 1.00 16.87 ATOM 4322 O PRO 3255 12.444 43.851 15.046 1.00 11.59 ATOM 4323 N ILE 3256 11.703 45.441 16.460 1.00 16.70 ATOM 4324 CA ILE 3256 11.184 46.338 15.423 1.00 18.17 ATOM 4325 CB ILE 3256 9.686 46.638 15.607 1.00 20.28 ATOM 4326 CG2 ILE 3256 9.261 47.740 14.640 1.00 19.60 ATOM 4327 CG1 ILE 3256 8.842 45.380 15.397 1.00 22.58 ATOM 4328 CD1 ILE 3256 7.345 45.596 15.681 1.00 17.47 ATOM 4329 C ILE 3256 11.887 47.688 15.543 1.00 19.66 ATOM 4330 O ILE 3256 11.850 48.311 16.603 1.00 22.49 ATOM 4331 N LEU 3257 12.520 48.151 14.474 1.00 19.13 ATOM 4332 CA LEU 3257 13.193 49.447 14.522 1.00 20.83 ATOM 4333 CB LEU 3257 14.501 49.420 13.727 1.00 17.27 ATOM 4334 CG LEU 3257 15.576 48.370 14.019 1.00 17.87 ATOM 4335 CD1 LEU 3257 16.917 48.850 13.467 1.00 14.59 ATOM 4336 CD2 LEU 3257 15.692 48.142 15.504 1.00 19.59 ATOM 4337 C LEU 3257 12.275 50.510 13.924 1.00 25.22 ATOM 4338 O LEU 3257 11.457 50.206 13.048 1.00 30.51 ATOM 4339 N GLN 3258 12.401 51.753 14.382 1.00 26.92 ATOM 4340 CA GLN 3258 11.567 52.825 13.848 1.00 23.92 ATOM 4341 CB GLN 3258 11.650 54.072 14.719 1.00 24.97 ATOM 4342 CG GLN 3258 10.876 55.240 14.161 1.00 30.42 ATOM 4343 CD GLN 3258 9.412 54.897 13.910 1.00 35.39 ATOM 4344 OE1 GLN 3258 8.653 54.619 14.845 1.00 36.83 ATOM 4345 NE2 GLN 3258 9.011 54.910 12.641 1.00 35.58 ATOM 4346 C GLN 3258 12.052 53.151 12.455 1.00 22.49 ATOM 4347 O GLN 3258 13.225 53.444 12.260 1.00 23.57 ATOM 4348 N ALA 3259 11.145 53.086 11.486 1.00 23.47 ATOM 4349 CA ALA 3259 11.475 53.373 10.094 1.00 23.33 ATOM 4350 CB ALA 3259 10.231 53.236 9.234 1.00 22.24 ATOM 4351 C ALA 3259 12.063 54.782 9.962 1.00 23.53 ATOM 4352 O ALA 3259 11.590 55.728 10.604 1.00 25.64 ATOM 4353 N GLY 3260 13.098 54.923 9.140 1.00 21.38 ATOM 4354 CA GLY 3260 13.718 56.224 8.973 1.00 19.46 ATOM 4355 C GLY 3260 14.940 56.397 9.859 1.00 19.56 ATOM 4356 O GLY 3260 15.831 57.190 9.548 1.00 18.36 ATOM 4357 N LEU 3261 14.991 55.655 10.961 1.00 17.37 ATOM 4358 CA LEU 3261 16.118 55.743 11.873 1.00 18.85 ATOM 4359 CB LEU 3261 15.607 55.920 13.303 1.00 20.55 ATOM 4360 CG LEU 3261 14.753 57.166 13.510 1.00 21.64 ATOM 4361 CD1 LEU 3261 14.286 57.268 14.959 1.00 20.59 ATOM 4362 CD2 LEU 3261 15.584 58.385 13.125 1.00 21.95 ATOM 4363 C LEU 3261 17.046 54.516 11.795 1.00 19.51 ATOM 4364 O LEU 3261 16.584 53.370 11.773 1.00 19.28 ATOM 4365 N PRO 3262 18.369 54.747 11.731 1.00 17.57 ATOM 4366 CD PRO 3262 19.394 53.687 11.659 1.00 15.35 ATOM 4367 CA PRO 3262 18.988 56.077 11.731 1.00 16.54 ATOM 4368 CB PRO 3262 20.450 55.773 12.020 1.00 16.77 ATOM 4369 CG PRO 3262 20.647 54.460 11.303 1.00 18.22 ATOM 4370 C PRO 3262 18.791 56.732 10.365 1.00 16.01 ATOM 4371 O PRO 3262 18.456 56.061 9.397 1.00 20.63 ATOM 4372 N ALA 3263 18.995 58.035 10.285 1.00 14.64 ATOM 4373 CA ALA 3263 18.824 58.752 9.028 1.00 10.82 ATOM 4374 CB ALA 3263 17.789 59.866 9.207 1.00 2.08 ATOM 4375 C ALA 3263 20.150 59.328 8.529 1.00 10.32 ATOM 4376 O ALA 3263 21.013 59.716 9.321 1.00 9.06 ATOM 4377 N ASN 3264 20.317 59.369 7.213 1.00 10.19 ATOM 4378 CA ASN 3264 21.532 59.919 6.636 1.00 12.92 ATOM 4379 CB ASN 3264 21.402 60.084 5.137 1.00 10.62 ATOM 4380 CG ASN 3264 21.014 58.831 4.472 1.00 12.92 ATOM 4381 OD1 ASN 3264 21.294 57.745 4.983 1.00 18.04 ATOM 4382 ND2 ASN 3264 20.375 58.946 3.313 1.00 10.07 ATOM 4383 C ASN 3264 21.831 61.285 7.208 1.00 16.47 ATOM 4384 O ASN 3264 20.950 61.990 7.685 1.00 18.20 ATOM 4385 N LYS 3265 23.091 61.664 7.127 1.00 21.11 ATOM 4386 CA LYS 3265 23.513 62.947 7.615 1.00 23.74 ATOM 4387 CB LYS 3265 23.887 62.853 9.082 1.00 26.87 ATOM 4388 CG LYS 3265 22.704 62.759 10.018 1.00 34.24 ATOM 4389 CD LYS 3265 22.894 63.716 11.179 1.00 36.62 ATOM 4390 CE LYS 3265 23.130 65.140 10.667 1.00 38.76 ATOM 4391 HZ LYS 3265 23.421 66.112 11.766 1.00 45.11 ATOM 4392 C LYS 3265 24.712 63.383 6.827 1.00 26.80 ATOM 4393 O LYS 3265 25.515 62.554 6.386 1.00 26.18 ATOM 4394 N THR 3266 24.805 64.691 6.628 1.00 29.75 ATOM 4395 CA THR 3266 25.926 65.300 5.931 1.00 31.69 ATOM 4396 CB THR 3266 25.485 66.033 4.646 1.00 34.37 ATOM 4397 OG1 THR 3266 24.834 65.111 3.755 1.00 36.34 ATOM 4398 CG2 THR 3266 26.694 66.636 3.947 1.00 35.21 ATOM 4399 C THR 3266 26.423 66.313 6.950 1.00 31.31 ATOM 4400 O THR 3266 25.628 67.032 7.548 1.00 28.58 ATOM 4401 N VAL 3267 27.731 66.342 7.178 1.00 33.41 ATOM 4402 CA VAL 3267 28.315 67.264 8.146 1.00 31.55 ATOM 4403 CB VAL 3267 28.479 66.602 9.544 1.00 32.83 ATOM 4404 CG1 VAL 3267 27.126 66.138 10.058 1.00 31.71 ATOM 4405 CG2 VAL 3267 29.454 65.425 9.463 1.00 32.77 ATOM 4406 C VAL 3267 29.676 67.735 7.674 1.00 30.75 ATOM 4407 O VAL 3267 30.250 67.180 6.731 1.00 30.39 ATOM 4408 N ALA 3268 30.190 68.761 8.346 1.00 30.65 ATOM 4409 CA ALA 3268 31.480 69.334 8.004 1.00 26.28 ATOM 4410 CB ALA 3268 31.474 70.814 8.300 1.00 24.19 ATOM 4411 C ALA 3268 32.562 68.651 8.801 1.00 26.26 ATOM 4412 O ALA 3268 32.304 68.141 9.896 1.00 24.95 ATOM 4413 N LEU 3269 33.769 68.630 8.242 1.00 26.36 ATOM 4414 CA LEU 3269 34.910 68.039 8.917 1.00 27.81 ATOM 4415 CB LEU 3269 36.190 68.351 8.146 1.00 28.05 ATOM 4416 CG LEU 3269 36.472 67.600 6.845 1.00 32.65 ATOM 4417 CD1 LEU 3269 37.560 68.322 6.079 1.00 31.75 ATOM 4418 CD2 LEU 3269 36.885 66.145 7.146 1.00 32.96 ATOM 4419 C LEU 3269 34.988 68.653 10.313 1.00 29.41 ATOM 4420 O LEU 3269 34.945 69.875 10.454 1.00 30.14 ATOM 4421 N GLY 3270 35.073 67.811 11.338 1.00 29.51 ATOM 4422 CA GLY 3270 35.168 68.314 12.694 1.00 33.16 ATOM 4423 C GLY 3270 33.867 68.301 13.465 1.00 36.49 ATOM 4424 O GLY 3270 33.864 68.345 14.695 1.00 38.70 ATOM 4425 N SER 3271 32.757 68.237 12.744 1.00 38.64 ATOM 4426 CA SER 3271 31.439 68.211 13.368 1.00 38.36 ATOM 4427 CB SER 3271 30.339 68.295 12.298 1.00 41.39 ATOM 4428 OG SER 3271 30.542 69.365 11.392 1.00 46.90 ATOM 4429 C SER 3271 31.238 66.915 14.141 1.00 36.54 ATOM 4430 O SER 3271 31.698 65.847 13.714 1.00 35.98 ATOM 4431 N ASH 3272 30.554 67.005 15.276 1.00 34.22 ATOM 4432 CA ASH 3272 30.248 65.810 16.046 1.00 32.39 ATOM 4433 CB ASH 3272 30.088 66.137 17.521 1.00 33.02 ATOM 4434 CG ASN 3272 31.275 66.891 18.065 1.00 39.47 ATOM 4435 OD1 ASN 3272 32.424 66.609 17.711 1.00 42.72 ATOM 4436 ND2 ASN 3272 31.011 67.861 18.934 1.00 44.46 ATOM 4437 C ASH 3272 28.931 65.325 15.453 1.00 30.76 ATOM 4438 O ASH 3272 28.197 66.104 14.839 1.00 29.02 ATOM 4439 N VAL 3273 28.628 64.044 15.607 1.00 27.27 ATOM 4440 CA VAL 3273 27.408 63.530 15.027 1.00 21.00 ATOM 4441 CB VAL 3273 27.663 62.986 13.604 1.00 18.45 ATOM 4442 CG1 VAL 3273 29.088 62.570 13.473 1.00 17.09 ATOM 4443 CG2 VAL 3273 26.745 61.818 13.303 1.00 16.60 ATOM 4444 C VAL 3273 26.784 62.471 15.876 1.00 20.13 ATOM 4445 O VAL 3273 27.464 61.776 16.617 1.00 17.90 ATOM 4446 N GLU 3274 25.465 62.375 15.764 1.00 22.07 ATOM 4447 CA GLU 3274 24.688 61.401 16.509 1.00 23.18 ATOM 4448 CB GLU 3274 23.979 62.074 17.690 1.00 23.38 ATOM 4449 CG GLU 3274 24.913 62.655 18.749 1.00 27.48 ATOM 4450 CD GLU 3274 24.164 63.399 19.858 1.00 31.71 ATOM 4451 OE1 GLU 3274 23.681 64.538 19.628 1.00 32.69 ATOM 4452 OE2 GLU 3274 24.048 62.833 20.965 1.00 31.25 ATOM 4453 C GLU 3274 23.649 60.737 15.610 1.00 21.95 ATOM 4454 O GLU 3274 22.935 61.400 14.861 1.00 21.49 ATOM 4455 N PHE 3275 23.597 59.418 15.672 1.00 19.24 ATOM 4456 CA PHE 3275 22.626 58.674 14.916 1.00 19.23 ATOM 4457 CB PHE 3275 23.287 57.514 14.191 1.00 19.10 ATOM 4458 CG PHE 3275 24.127 57.924 13.024 1.00 19.09 ATOM 4459 CD1 PHE 3275 23.549 58.509 11.903 1.00 16.19 ATOM 4460 CD2 PHE 3275 25.502 57.691 13.032 1.00 18.92 ATOM 4461 CE1 PHE 3275 24.327 58.856 10.798 1.00 19.77 ATOM 4462 CE2 PHE 3275 26.296 58.033 11.930 1.00 19.55 ATOM 4463 CZ PHE 3275 25.709 58.617 10.809 1.00 19.45 ATOM 4464 C PHE 3275 21.674 58.146 15.976 1.00 21.86 ATOM 4465 O PHE 3275 22.112 57.809 17.079 1.00 21.13 ATOM 4466 N MET 3276 20.381 58.089 15.651 1.00 22.58 ATOM 4467 CA MET 3276 19.374 57.594 16.581 1.00 20.39 ATOM 4468 CB MET 3276 18.189 58.559 16.669 1.00 24.62 ATOM 4469 CG MET 3276 18.569 60.006 16.901 1.00 28.34 ATOM 4470 SD MET 3276 17.107 61.034 17.050 1.00 35.45 ATOM 4471 CE MET 3276 16.966 61.152 18.854 1.00 30.79 ATOM 4472 C MET 3276 18.875 56.255 16.096 1.00 17.79 ATOM 4473 O MET 3276 19.039 55.897 14.940 1.00 18.35 ATOM 4474 N CYS 3277 18.248 55.520 16.992 1.00 17.70 ATOM 4475 CA CYS 3277 17.710 54.222 16.662 1.00 20.83 ATOM 4476 C CYS 3277 16.625 53.942 17.694 1.00 20.81 ATOM 4477 O CYS 3277 16.870 54.046 18.888 1.00 21.06 ATOM 4478 CB CYS 3277 18.814 53.177 16.750 1.00 22.91 ATOM 4479 SG CYS 3277 18.391 51.532 16.092 1.00 30.91 ATOM 4480 N LYS 3278 15.424 53.617 17.232 1.00 21.63 ATOM 4481 CA LYS 3278 14.317 53.330 18.133 1.00 22.79 ATOM 4482 CB LYS 3278 13.116 54.204 17.774 1.00 22.66 ATOM 4483 CG LYS 3278 12.549 55.036 18.920 1.00 25.77 ATOM 4484 CD LYS 3278 11.525 54.270 19.754 1.00 27.26 ATOM 4485 CE LYS 3278 10.787 55.171 20.761 1.00 32.36 ATOM 4486 NZ LYS 3278 9.998 56.303 20.152 1.00 36.39 ATOM 4487 C LYS 3278 13.964 51.854 17.991 1.00 22.92 ATOM 4488 O LYS 3278 13.645 51.388 16.903 1.00 26.50 ATOM 4489 N VAL 3279 14.010 51.128 19.101 1.00 19.71 ATOM 4490 CA VAL 3279 13.740 49.699 19.101 1.00 17.12 ATOM 4491 CB VAL 3279 15.001 48.917 19.619 1.00 17.18 ATOM 4492 CG1 VAL 3279 14.748 47.431 19.611 1.00 16.48 ATOM 4493 CG2 VAL 3279 16.218 49.251 18.782 1.00 14.76 ATOM 4494 C VAL 3279 12.563 49.360 20.009 1.00 18.51 ATOM 4495 O VAL 3279 12.359 50.014 21.036 1.00 17.83 ATOM 4496 N TYR 3280 11.772 48.365 19.611 1.00 18.37 ATOM 4497 CA TYR 3280 10.663 47.877 20.434 1.00 19.65 ATOM 4498 CB TYR 3280 9.283 48.153 19.848 1.00 21.02 ATOM 4499 CG TYR 3280 8.217 47.325 20.584 1.00 26.66 ATOM 4500 CD1 TYR 3280 7.618 47.794 21.765 1.00 26.80 ATOM 4501 CE1 TYR 3280 6.736 46.989 22.504 1.00 24.94 ATOM 4502 CD2 TYR 3280 7.890 46.025 20.160 1.00 24.05 ATOM 4503 CE2 TYR 3280 7.012 45.219 20.896 1.00 24.17 ATOM 4504 CZ TYR 3280 6.442 45.706 22.064 1.00 25.11 ATOM 4505 OH TYR 3280 5.602 44.905 22.807 1.00 26.64 ATOM 4506 C TYR 3280 10.859 46.370 20.461 1.00 20.50 ATOM 4507 O TYR 3280 11.101 45.749 19.423 1.00 20.46 ATOM 4508 N SER 3281 10.724 45.771 21.632 1.00 18.62 ATOM 4509 CA SER 3281 10.951 44.352 21.722 1.00 18.26 ATOM 4510 CB SER 3281 12.446 44.103 21.521 1.00 13.72 ATOM 4511 OG SER 3281 12.762 42.733 21.584 1.00 23.33 ATOM 4512 C SER 3281 10.489 43.821 23.067 1.00 20.13 ATOM 4513 O SER 3281 11.004 44.249 24.092 1.00 23.43 ATOM 4514 N ASP 3282 9.506 42.915 23.071 1.00 21.92 ATOM 4515 CA ASP 3282 9.023 42.327 24.319 1.00 18.13 ATOM 4516 CB ASP 3282 7.911 41.313 24.046 1.00 17.35 ATOM 4517 CG ASP 3282 7.463 40.592 25.297 1.00 23.20 ATOM 4518 OD1 ASP 3282 6.423 39.898 25.266 1.00 21.51 ATOM 4519 OD2 ASP 3282 8.160 40.709 26.324 1.00 29.34 ATOM 4520 C ASP 3282 10.238 41.675 24.993 1.00 17.69 ATOM 4521 O ASP 3282 10.647 42.102 26.072 1.00 18.82 ATOM 4522 N PRO 3283 10.837 40.640 24.379 1.00 16.79 ATOM 4523 CD PRO 3283 10.440 39.777 23.257 1.00 16.75 ATOM 4524 CA PRO 3283 12.003 40.079 25.072 1.00 18.89 ATOM 4525 CB PRO 3283 12.267 38.779 24.315 1.00 19.64 ATOM 4526 CG PRO 3283 11.723 39.043 22.959 1.00 17.42 ATOM 4527 C PRO 3283 13.165 41.070 24.982 1.00 18.93 ATOM 4528 O PRO 3283 13.200 41.882 24.064 1.00 19.18 ATOM 4529 N GLN 3284 14.100 41.017 25.927 1.00 20.79 ATOM 4530 CA GLN 3284 15.228 41.954 25.923 1.00 23.12 ATOM 4531 CB GLN 3284 16.190 41.670 27.079 1.00 26.64 ATOM 4532 CG GLN 3284 15.686 42.185 28.403 1.00 31.18 ATOM 4533 CD GLN 3284 15.444 43.677 28.369 1.00 33.51 ATOM 4534 OE1 GLN 3284 14.530 44.187 29.025 1.00 37.06 ATOM 4535 NE2 GLN 3284 16.270 44.392 27.611 1.00 30.56 ATOM 4536 C GLN 3284 16.024 41.991 24.632 1.00 22.12 ATOM 4537 O GLN 3284 16.584 40.984 24.198 1.00 22.15 ATOM 4538 N PRO 3285 16.088 43.170 24.000 1.00 21.03 ATOM 4539 CD PRO 3285 15.338 44.399 24.314 1.00 18.24 ATOM 4540 CA PRO 3285 16.831 43.327 22.748 1.00 20.96 ATOM 4541 CB PRO 3285 16.141 44.520 22.100 1.00 16.42 ATOM 4542 CG PRO 3285 15.890 45.387 23.289 1.00 17.30 ATOM 4543 C PRO 3285 18.308 43.614 23.016 1.00 19.61 ATOM 4544 O PRO 3285 18.652 44.229 24.019 1.00 17.18 ATOM 4545 N HIS 3286 19.172 43.159 22.122 1.00 18.93 ATOM 4546 CA HIS 3286 20.590 43.421 22.256 1.00 21.50 ATOM 4547 CB HIS 3286 21.386 42.122 22.155 1.00 24.23 ATOM 4548 CG HIS 3286 22.858 42.309 22.322 1.00 31.35 ATOM 4549 CD2 HIS 3286 23.614 42.468 23.436 1.00 35.30 ATOM 4550 ND1 HIS 3286 23.725 42.413 21.255 1.00 33.71 ATOM 4551 CE1 HIS 3286 24.949 42.629 21.702 1.00 35.42 ATOM 4552 NE2 HIS 3286 24.909 42.667 23.023 1.00 36.55 ATOM 4553 C HIS 3286 20.909 44.351 21.094 1.00 20.80 ATOM 4554 O HIS 3286 20.759 43.969 19.941 1.00 23.48 ATOM 4555 N ILE 3287 21.334 45.573 21.391 1.00 20.39 ATOM 4556 CA ILE 3287 21.621 46.542 20.339 1.00 20.95 ATOM 4557 CB ILE 3287 20.963 47.928 20.640 1.00 20.11 ATOM 4558 CG2 ILE 3287 21.540 48.991 19.725 1.00 18.21 ATOM 4559 CG1 ILE 3287 19.453 47.874 20.409 1.00 17.87 ATOM 4560 CD1 ILE 3287 18.684 47.133 21.453 1.00 19.51 ATOM 4561 G ILE 3287 23.098 46.781 20.079 1.00 22.79 ATOM 4562 O ILE 3287 23.882 46.958 21.004 1.00 26.54 ATOM 4563 N GLN 3288 23.465 46.802 18.803 1.00 24.49 ATOM 4564 CA GLN 3288 24.847 47.044 18.394 1.00 26.54 ATOM 4565 CB GLN 3288 25.519 45.772 17.891 1.00 27.11 ATOM 4566 CG GLN 3288 25.897 44.755 18.923 1.00 29.11 ATOM 4567 CD GLN 3288 26.700 43.633 18.300 1.00 32.97 ATOM 4568 OE1 GLN 3288 26.985 42.623 18.942 1.00 36.15 ATOM 4569 NE2 GLN 3288 27.077 43.809 17.035 1.00 34.32 ATOM 4570 C GLN 3288 24.871 48.020 17.240 1.00 27.48 ATOM 4571 O GLN 3288 23.938 48.058 16.432 1.00 28.66 ATOM 4572 N TRP 3289 25.933 48.811 17.157 1.00 26.47 ATOM 4573 CA TRP 3289 26.067 49.736 16.045 1.00 26.74 ATOM 4574 CB TRP 3289 26.374 51.152 16.533 1.00 23.41 ATOM 4575 CG TRP 3289 25.166 51.857 17.065 1.00 23.14 ATOM 4576 CD2 TRP 3289 24.250 52.667 16.319 1.00 24.29 ATOM 4577 CE2 TRP 3289 23.249 53.110 17.221 1.00 24.25 ATOM 4578 CE3 TRP 3289 24.176 53.068 14.977 1.00 21.24 ATOM 4579 CD1 TRP 3289 24.696 51.836 18.350 1.00 23.53 ATOM 4580 NE1 TRP 3289 23.546 52.587 18.453 1.00 21.95 ATOM 4581 CZ2 TRP 3289 22.191 53.930 16.821 1.00 21.61 ATOM 4582 CZ3 TRP 3289 23.128 53.882 14.585 1.00 20.89 ATOM 4583 CH2 TRP 3289 22.148 54.303 15.505 1.00 21.46 ATOM 4584 C TRP 3289 27.209 49.187 15.212 1.00 27.47 ATOM 4585 O TRP 3289 28.209 48.729 15.770 1.00 26.21 ATOM 4586 N LEU 3290 27.062 49.206 13.890 1.00 27.19 ATOM 4587 CA LEU 3290 28.112 48.670 13.030 1.00 30.23 ATOM 4588 CB LEU 3290 27.654 47.363 12.364 1.00 30.65 ATOM 4589 CG LEU 3290 26.744 46.363 13.088 1.00 32.74 ATOM 4590 CD1 LEU 3290 26.405 45.229 12.126 1.00 32.45 ATOM 4591 CD2 LEU 3290 27.415 45.814 14.331 1.00 31.09 ATOM 4592 C LEU 3290 28.540 49.627 11.925 1.00 31.63 ATOM 4593 O LEU 3290 27.706 50.259 11.281 1.00 32.46 ATOM 4594 N LYS 3291 29.847 49.725 11.706 1.00 31.42 ATOM 4595 CA LYS 3291 30.367 50.556 10.636 1.00 30.67 ATOM 4596 CB LYS 3291 31.649 51.270 11.086 1.00 32.02 ATOM 4597 CG LYS 3291 32.367 52.067 9.979 1.00 34.48 ATOM 4598 CD LYS 3291 31.482 53.169 9.410 1.00 36.64 ATOM 4599 CE LYS 3291 32.240 54.108 8.483 1.00 37.18 ATOM 4600 NZ LYS 3291 32.575 53.496 7.171 1.00 40.53 ATOM 4601 C LYS 3291 30.677 49.592 9.483 1.00 31.41 ATOM 4602 O LYS 3291 31.101 48.457 9.703 1.00 32.63 ATOM 4603 N HIS 3292 30.450 50.025 8.257 1.00 29.58 ATOM 4604 CA HIS 3292 30.744 49.181 7.123 1.00 30.27 ATOM 4605 CB HIS 3292 29.750 49.477 6.012 1.00 32.12 ATOM 4606 CG HIS 3292 28.356 49.047 6.340 1.00 35.10 ATOM 4607 CD2 HIS 3292 27.449 49.557 7.208 1.00 37.52 ATOM 4608 ND1 HIS 3292 27.782 47.917 5.807 1.00 36.31 ATOM 4609 CE1 HIS 3292 26.580 47.746 6.332 1.00 37.82 ATOM 4610 NE2 HIS 3292 26.356 48.728 7.185 1.00 36.14 ATOM 4611 C HIS 3292 32.167 49.447 6.674 1.00 33.55 ATOM 4612 O HIS 3292 32.593 50.595 6.598 1.00 37.07 ATOM 4613 N ILE 3293 32.923 48.393 6.403 1.00 36.32 ATOM 4614 CA ILE 3293 34.305 48.570 5.961 1.00 38.28 ATOM 4615 CB ILE 3293 35.306 47.935 6.941 1.00 38.79 ATOM 4616 CG2 ILE 3293 36.727 48.397 6.594 1.00 39.12 ATOM 4617 CG1 ILE 3293 34.959 48.331 8.374 1.00 40.05 ATOM 4618 CD1 ILE 3293 35.815 47.629 9.413 1.00 42.09 ATOM 4619 C ILE 3293 34.524 47.942 4.592 1.00 36.87 ATOM 4620 O ILE 3293 34.286 46.754 4.413 1.00 35.64 ATOM 4621 N PRO 3306 28.867 41.727 3.498 1.00 50.53 ATOM 4622 CD PRO 3306 27.398 41.849 3.543 1.00 49.75 ATOM 4623 CA PRO 3306 29.512 43.010 3.811 1.00 49.98 ATOM 4624 CB PRO 3306 28.333 43.986 3.832 1.00 48.87 ATOM 4625 CG PRO 3306 27.204 43.134 4.329 1.00 48.75 ATOM 4626 C PRO 3306 30.270 42.985 5.142 1.00 49.99 ATOM 4627 O PRO 3306 29.706 42.596 6.172 1.00 50.18 ATOM 4628 N TYR 3307 31.541 43.393 5.126 1.00 49.25 ATOM 4629 CA TYR 3307 32.328 43.399 6.363 1.00 49.05 ATOM 4630 CB TYR 3307 33.815 43.615 6.087 1.00 53.62 ATOM 4631 CG TYR 3307 34.323 42.890 4.877 1.00 58.69 ATOM 4632 CD1 TYR 3307 34.194 43.454 3.605 1.00 61.80 ATOM 4633 CE1 TYR 3307 34.648 42.790 2.470 1.00 63.44 ATOM 4634 CD2 TYR 3307 34.919 41.633 4.991 1.00 60.87 ATOM 4635 CE2 TYR 3307 35.376 40.952 3.861 1.00 63.67 ATOM 4636 CZ TYR 3307 35.236 41.539 2.604 1.00 64.69 ATOM 4637 OH TYR 3307 35.680 40.877 1.482 1.00 65.93 ATOM 4638 C TYR 3307 31.841 44.510 7.274 1.00 46.00 ATOM 4639 O TYR 3307 31.348 45.536 6.810 1.00 45.20 ATOM 4640 N VAL 3308 31.977 44.305 8.574 1.00 42.35 ATOM 4641 CA VAL 3308 31.540 45.311 9.514 1.00 42.49 ATOM 4642 CB VAL 3308 30.100 45.020 10.042 1.00 41.34 ATOM 4643 CG1 VAL 3308 29.126 44.929 8.875 1.00 38.13 ATOM 4644 CG2 VAL 3308 30.076 43.740 10.854 1.00 39.99 ATOM 4645 C VAL 3308 32.504 45.398 10.679 1.00 42.70 ATOM 4646 O VAL 3308 33.301 44.492 10.919 1.00 41.81 ATOM 4647 N GLN 3309 32.427 46.512 11.394 1.00 44.15 ATOM 4648 CA GLN 3309 33.273 46.765 12.549 1.00 45.11 ATOM 4649 CB GLN 3309 34.236 47.914 12.245 1.00 47.30 ATOM 4650 CG GLN 3309 35.242 48.211 13.350 1.00 53.22 ATOM 4651 CD GLN 3309 35.912 49.576 13.194 1.00 54.67 ATOM 4652 OE1 GLN 3309 36.545 49.870 12.171 1.00 53.51 ATOM 4653 NE2 GLN 3309 35.777 50.414 14.219 1.00 56.15 ATOM 4654 C GLN 3309 32.346 47.156 13.691 1.00 45.06 ATOM 4655 O GLN 3309 31.785 48.252 13.703 1.00 44.56 ATOM 4656 N ILE 3310 32.157 46.242 14.637 1.00 44.25 ATOM 4657 CA ILE 3310 31.300 46.520 15.779 1.00 43.66 ATOM 4658 CB ILE 3310 31.339 45.393 16.829 1.00 43.39 ATOM 4659 CG2 ILE 3310 30.367 45.716 17.973 1.00 42.44 ATOM 4660 CG1 ILE 3310 31.027 44.054 16.167 1.00 44.49 ATOM 4661 CD1 ILE 3310 29.676 43.946 15.554 1.00 45.12 ATOM 4662 C ILE 3310 31.856 47.788 16.426 1.00 44.91 ATOM 4663 O ILE 3310 33.062 47.895 16.668 1.00 47.75 ATOM 4664 N LEU 3311 30.983 48.745 16.700 1.00 44.00 ATOM 4665 CA LEU 3311 31.416 49.981 17.314 1.00 44.24 ATOM 4666 CB LEU 3311 30.826 51.171 16.568 1.00 41.92 ATOM 4667 CG LEU 3311 31.261 51.359 15.118 1.00 39.13 ATOM 4668 CD1 LEU 3311 30.663 52.645 14.587 1.00 37.21 ATOM 4669 CD2 LEU 3311 32.783 51.415 15.040 1.00 39.70 ATOM 4670 C LEU 3311 30.994 50.028 18.777 1.00 47.49 ATOM 4671 O LEU 3311 31.833 50.177 19.670 1.00 48.37 ATOM 4672 N LYS 3312 29.692 49.894 19.011 1.00 50.65 ATOM 4673 CA LYS 3312 29.133 49.913 20.362 1.00 54.46 ATOM 4674 CB LYS 3312 28.221 51.136 20.515 1.00 53.77 ATOM 4675 CG LYS 3312 28.241 51.855 21.869 1.00 52.70 ATOM 4676 CD LYS 3312 27.424 53.137 21.769 1.00 51.76 ATOM 4677 CE LYS 3312 27.481 53.952 23.049 1.00 52.83 ATOM 4678 NZ LYS 3312 26.811 55.293 22.886 1.00 53.72 ATOM 4679 C LYS 3312 28.343 48.607 20.616 1.00 57.49 ATOM 4680 O LYS 3312 27.749 48.046 19.687 1.00 59.53 ATOM 4681 N THR 3313 28.359 48.115 21.860 1.00 59.16 ATOM 4682 CA THR 3313 27.664 46.873 22.244 1.00 60.02 ATOM 4683 CB THR 3313 28.689 45.666 22.326 1.00 59.43 ATOM 4684 OG1 THR 3313 29.391 45.525 21.079 1.00 56.36 ATOM 4685 CG2 THR 3313 27.970 44.349 22.630 1.00 59.12 ATOM 4686 C THR 3313 26.983 47.091 23.615 1.00 61.92 ATOM 4687 O THR 3313 27.650 47.438 24.597 1.00 62.79 ATOM 4688 N ALA 3314 25.661 46.915 23.686 1.00 63.68 ATOM 4689 CA ALA 3314 24.932 47.099 24.951 1.00 64.89 ATOM 4690 CB ALA 3314 23.410 47.023 24.709 1.00 63.92 ATOM 4691 C ALA 3314 25.347 46.050 25.991 1.00 66.12 ATOM 4692 O ALA 3314 25.748 44.927 25.650 1.00 67.50 ATOM 4693 N GLU 3324 20.459 54.050 22.281 1.00 34.45 ATOM 4694 CA GLU 3324 19.646 54.513 21.164 1.00 33.67 ATOM 4695 CB GLU 3324 18.445 55.300 21.667 1.00 34.05 ATOM 4696 CG GLU 3324 17.497 54.551 22.561 1.00 41.24 ATOM 4697 CD GLU 3324 16.378 55.455 23.059 1.00 47.04 ATOM 4698 OE1 GLU 3324 16.315 56.614 22.587 1.00 50.25 ATOM 4699 OE2 GLU 3324 15.562 55.020 23.908 1.00 49.44 ATOM 4700 C GLU 3324 20.436 55.413 20.221 1.00 32.17 ATOM 4701 O GLU 3324 20.021 55.642 19.087 1.00 34.70 ATOM 4702 N VAL 3325 21.566 55.939 20.675 1.00 28.22 ATOM 4703 CA VAL 3325 22.332 56.815 19.808 1.00 26.02 ATOM 4704 CB VAL 3325 22.258 56.306 20.284 1.00 25.39 ATOM 4705 CG1 VAL 3325 21.084 58.494 21.229 1.00 19.03 ATOM 4706 CG2 VAL 3325 23.565 58.739 20.923 1.00 22.06 ATOM 4707 C VAL 3325 23.787 56.413 19.655 1.00 25.59 ATOM 4708 O VAL 3325 24.409 55.904 20.582 1.00 22.40 ATOM 4709 N LEU 3326 24.308 56.631 18.454 1.00 26.42 ATOM 4710 CA LEU 3326 25.696 56.339 18.140 1.00 26.12 ATOM 4711 CB LEU 3326 25.821 55.622 16.786 1.00 21.59 ATOM 4712 CG LEU 3326 27.247 55.571 16.215 1.00 22.26 ATOM 4713 CD1 LEU 3326 28.197 55.075 17.290 1.00 20.08 ATOM 4714 CD2 LEU 3326 27.315 54.682 14.976 1.00 17.56 ATOM 4715 C LEU 3326 26.333 57.708 18.075 1.00 27.14 ATOM 4716 O LEU 3326 25.902 58.557 17.300 1.00 28.80 ATOM 4717 N HIS 3327 27.350 57.940 18.892 1.00 30.53 ATOM 4718 CA HIS 3327 27.980 59.253 18.896 1.00 32.36 ATOM 4719 CB HIS 3327 27.952 59.818 20.318 1.00 34.97 ATOM 4720 CG HIS 3327 28.135 61.304 20.380 1.00 42.68 ATOM 4721 CD2 HIS 3327 28.575 62.189 19.457 1.00 45.04 ATOM 4722 ND1 HIS 3327 27.860 62.038 21.515 1.00 45.87 ATOM 4723 CE1 HIS 3327 28.124 63.313 21.284 1.00 45.71 ATOM 4724 NE2 HIS 3327 28.560 63.433 20.045 1.00 44.63 ATOM 4725 C HIS 3327 29.400 59.293 18.317 1.00 30.23 ATOM 4726 O HIS 3327 30.319 58.662 18.826 1.00 29.19 ATOM 4727 N LEU 3328 29.561 60.040 17.234 1.00 28.95 ATOM 4728 CA LEU 3328 30.857 60.180 16.595 1.00 30.99 ATOM 4729 CB LEU 3328 30.703 60.100 15.074 1.00 29.16 ATOM 4730 CG LEU 3328 29.951 58.865 14.555 1.00 29.23 ATOM 4731 CD1 LEU 3328 29.728 58.998 13.062 1.00 29.68 ATOM 4732 CD2 LEU 3328 30.732 57.594 14.869 1.00 26.10 ATOM 4733 C LEU 3328 31.422 61.534 17.007 1.00 33.81 ATOM 4734 O LEU 3328 30.798 62.573 16.784 1.00 32.11 ATOM 4735 N ARG 3329 32.600 61.518 17.623 1.00 37.31 ATOM 4736 CA ARG 3329 33.235 62.750 18.077 1.00 39.81 ATOM 4737 CB ARG 3329 34.451 62.424 18.939 1.00 40.20 ATOM 4738 C ARG 3329 33.643 63.685 16.936 1.00 41.53 ATOM 4739 O ARG 3329 32.839 63.984 16.052 1.00 43.65 ATOM 4740 N ASN 3330 34.890 64.146 16.957 1.00 42.05 ATOM 4741 CA ASN 3330 35.387 65.074 15.946 1.00 42.40 ATOM 4742 CB ASN 3330 36.678 65.732 16.431 1.00 45.71 ATOM 4743 CG ASN 3330 37.104 66.884 15.547 1.00 50.73 ATOM 4744 OD1 ASN 3330 37.765 66.693 14.521 1.00 51.29 ATOM 4745 ND2 ASN 3330 36.711 68.098 15.933 1.00 53.42 ATOM 4746 C ASN 3330 35.612 64.418 14.595 1.00 40.92 ATOM 4747 O ASN 3330 36.744 64.184 14.175 1.00 41.46 ATOM 4748 N VAL 3331 34.506 64.154 13.916 1.00 39.86 ATOM 4749 CA VAL 3331 34.482 63.510 12.612 1.00 38.36 ATOM 4750 CB VAL 3331 33.044 63.514 12.083 1.00 36.46 ATOM 4751 CG1 VAL 3331 33.009 63.151 10.607 1.00 35.11 ATOM 4752 CG2 VAL 3331 32.221 62.536 12.897 1.00 35.94 ATOM 4753 C VAL 3331 35.413 64.059 11.533 1.00 38.81 ATOM 4754 O VAL 3331 35.677 65.254 11.476 1.00 39.52 ATOM 4755 N SER 3332 35.900 63.155 10.684 1.00 39.14 ATOM 4756 CA SER 3332 36.782 63.476 9.561 1.00 41.46 ATOM 4757 CB SER 3332 38.215 63.009 9.842 1.00 42.72 ATOM 4758 OG SER 3332 38.306 61.593 9.834 1.00 45.96 ATOM 4759 C SER 3332 36.257 62.760 8.303 1.00 41.31 ATOM 4760 O SER 3332 35.185 62.150 8.326 1.00 40.97 ATOM 4761 N PHE 3333 37.006 62.832 7.208 1.00 39.77 ATOM 4762 CA PHE 3333 36.580 62.170 5.984 1.00 40.03 ATOM 4763 CB PHE 3333 37.557 62.455 4.838 1.00 40.48 ATOM 4764 CG PHE 3333 37.425 63.836 4.262 1.00 42.80 ATOM 4765 CD1 PHE 3333 38.497 64.724 4.291 1.00 44.08 ATOM 4766 CD2 PHE 3333 36.218 64.261 3.710 1.00 41.76 ATOM 4767 CE1 PHE 3333 38.366 66.017 3.783 1.00 43.95 ATOM 4768 CE2 PHE 3333 36.080 65.549 3.201 1.00 40.09 ATOM 4769 CZ PHE 3333 37.153 66.427 3.237 1.00 42.04 ATOM 4770 C PHE 3333 36.470 60.668 6.192 1.00 40.10 ATOM 4771 O PHE 3333 35.508 60.042 5.756 1.00 37.43 ATOM 4772 N GLU 3334 37.459 60.093 6.869 1.00 41.76 ATOM 4773 CA GLU 3334 37.462 58.660 7.115 1.00 41.91 ATOM 4774 CB GLU 3334 38.665 58.259 7.963 1.00 44.33 ATOM 4775 CG GLU 3334 38.832 56.755 8.062 1.00 51.69 ATOM 4776 CD GLU 3334 39.519 56.324 9.340 1.00 56.76 ATOM 4777 OE1 GLU 3334 40.658 56.776 9.582 1.00 59.33 ATOM 4778 OE2 GLU 3334 38.919 55.531 10.104 1.00 59.43 ATOM 4779 CG GLU 3334 36.179 58.214 7.810 1.00 39.11 ATOM 4780 O GLU 3334 35.738 57.074 7.654 1.00 39.71 ATOM 4781 N ASP 3335 35.582 59.111 8.579 1.00 35.54 ATOM 4782 CA ASP 3335 34.349 58.788 9.280 1.00 33.54 ATOM 4783 CB ASP 3335 34.019 59.886 10.300 1.00 36.08 ATOM 4784 CG ASP 3335 35.021 59.951 11.438 1.00 37.24 ATOM 4785 OD1 ASP 3335 35.176 58.940 12.148 1.00 38.81 ATOM 4786 OD2 ASP 3335 35.651 61.012 11.628 1.00 36.88 ATOM 4787 C ASP 3335 33.185 58.631 8.298 1.00 30.04 ATOM 4788 O ASP 3335 32.156 58.029 8.616 1.00 27.28 ATOM 4789 N ALA 3336 33.344 59.177 7.102 1.00 28.20 ATOM 4790 CA ALA 3336 32.280 59.082 6.116 1.00 28.61 ATOM 4791 CB ALA 3336 32.669 59.814 4.835 1.00 27.15 ATOM 4792 C ALA 3336 32.003 57.614 5.827 1.00 27.66 ATOM 4793 O ALA 3336 32.885 56.770 5.972 1.00 25.77 ATOM 4794 N GLY 3337 30.767 57.311 5.440 1.00 26.67 ATOM 4795 CA GLY 3337 30.417 55.942 5.130 1.00 25.15 ATOM 4796 C GLY 3337 29.093 55.504 5.701 1.00 25.47 ATOM 4797 O GLY 3337 28.368 56.292 6.303 1.00 26.07 ATOM 4798 N GLU 3338 28.790 54.222 5.530 1.00 26.41 ATOM 4799 CA GLU 3338 27.536 53.653 6.000 1.00 24.31 ATOM 4800 CB GLU 3338 27.053 52.616 4.989 1.00 25.61 ATOM 4801 CG GLU 3338 25.817 51.840 5.414 1.00 32.75 ATOM 4802 CD GLU 3338 25.319 50.907 4.320 1.00 35.06 ATOM 4803 OE1 GLU 3338 26.163 50.234 3.679 1.00 36.67 ATOM 4804 OE2 GLU 3338 24.087 50.844 4.109 1.00 34.11 ATOM 4805 C GLU 3338 27.583 53.034 7.398 1.00 23.74 ATOM 4806 O LEU 3338 28.500 52.294 7.737 1.00 19.53 ATOM 4807 N TYR 3339 26.574 53.351 8.204 1.00 24.95 ATOM 4808 CA TYR 3339 26.474 52.825 9.554 1.00 23.86 ATOM 4809 CB TYR 3339 26.518 53.952 10.585 1.00 24.35 ATOM 4810 CG TYR 3339 27.847 54.638 10.645 1.00 26.70 ATOM 4811 CD1 TYR 3339 28.227 55.545 9.659 1.00 27.89 ATOM 4812 CE1 TYR 3339 29.474 56.161 9.692 1.00 32.57 ATOM 4813 CD2 TYR 3339 28.747 54.359 11.674 1.00 28.26 ATOM 4814 CE2 TYR 3339 30.002 54.965 11.721 1.00 30.08 ATOM 4815 CZ TYR 3339 30.359 55.868 10.728 1.00 32.77 ATOM 4816 OH TYR 3339 31.592 56.482 10.771 1.00 34.79 ATOM 4817 C TYR 3339 25.181 52.059 9.715 1.00 23.89 ATOM 4818 O TYR 3339 24.203 52.340 9.028 1.00 25.21 ATOM 4819 N THR 3340 25.186 51.103 10.643 1.00 23.89 ATOM 4820 CA THR 3340 24.028 50.265 10.916 1.00 22.98 ATOM 4821 CB THR 3340 24.203 48.853 10.293 1.00 21.86 ATOM 4822 OG1 THR 3340 24.075 48.934 8.874 1.00 18.87 ATOM 4823 CG2 THR 3340 23.158 47.889 10.839 1.00 22.00 ATOM 4824 C THR 3340 23.735 50.074 12.402 1.00 23.05 ATOM 4825 O THR 3340 24.635 49.893 13.225 1.00 19.63 ATOM 4826 N CYS 3341 22.452 50.114 12.722 1.00 25.37 ATOM 4827 CA CYS 3341 21.991 49.893 14.076 1.00 27.60 ATOM 4828 C CYS 3341 21.339 48.514 14.013 1.00 27.96 ATOM 4829 O CYS 3341 20.367 48.316 13.290 1.00 28.46 ATOM 4830 CB CYS 3341 20.951 50.938 14.484 1.00 28.73 ATOM 4831 SG CYS 3341 20.192 50.580 16.106 1.00 35.79 ATOM 4832 N LEU 3342 21.890 47.560 14.757 1.00 27.49 ATOM 4833 CA LEU 3342 21.363 46.206 14.778 1.00 24.07 ATOM 4834 CB LEU 3342 22.454 45.207 14.376 1.00 23.74 ATOM 4835 CG LEU 3342 22.026 43.755 14.114 1.00 27.37 ATOM 4836 CD1 LEU 3342 23.123 43.028 13.334 1.00 25.92 ATOM 4837 CD2 LEU 3342 21.723 43.042 15.425 1.00 24.75 ATOM 4838 C LEU 3342 20.827 45.860 16.159 1.00 22.92 ATOM 4839 O LEU 3342 21.451 46.152 17.182 1.00 21.73 ATOM 4840 N ALA 3343 19.650 45.249 16.169 1.00 21.21 ATOM 4841 CA ALA 3343 18.997 44.826 17.393 1.00 20.79 ATOM 4842 CB ALA 3343 17.799 45.726 17.692 1.00 21.86 ATOM 4843 C ALA 3343 18.534 43.390 17.178 1.00 20.82 ATOM 4844 O ALA 3343 18.058 43.039 16.088 1.00 21.13 ATOM 4845 N GLY 3344 18.666 42.563 18.209 1.00 17.15 ATOM 4846 CA GLY 3344 18.244 41.188 18.073 1.00 17.04 ATOM 4847 C GLY 3344 17.772 40.569 19.365 1.00 18.04 ATOM 4848 O GLY 3344 18.237 40.938 20.448 1.00 19.90 ATOM 4849 N ASN 3345 16.824 39.644 19.257 1.00 16.54 ATOM 4850 CA ASN 3345 16.337 38.950 20.429 1.00 20.08 ATOM 4851 CB ASN 3345 14.943 39.451 20.852 1.00 23.76 ATOM 4852 CG ASN 3345 13.883 39.209 19.807 1.00 25.69 ATOM 4853 OD1 ASN 3345 13.806 38.125 19.226 1.00 27.26 ATOM 4854 ND2 ASN 3345 13.039 40.214 19.572 1.00 24.39 ATOM 4855 C ASN 3345 16.320 37.465 20.117 1.00 20.29 ATOM 4856 O ASN 3345 16.736 37.047 19.039 1.00 19.27 ATOM 4857 N SER 3346 15.838 36.666 21.060 1.00 20.72 ATOM 4858 CA SER 3346 15.808 35.231 20.868 1.00 19.34 ATOM 4859 CB SER 3346 15.228 34.551 22.095 1.00 20.12 ATOM 4860 OG SER 3346 13.819 34.647 22.082 1.00 26.95 ATOM 4861 C SER 3346 15.040 34.775 19.638 1.00 19.31 ATOM 4862 O SER 3346 15.288 33.678 19.147 1.00 22.73 ATOM 4863 N ILE 3347 14.109 35.585 19.141 1.00 17.32 ATOM 4864 CA ILE 3347 13.347 35.189 17.954 1.00 17.57 ATOM 4865 CB ILE 3347 11.964 35.906 17.878 1.00 17.04 ATOM 4866 CG2 ILE 3347 11.324 35.644 16.520 1.00 14.02 ATOM 4867 CG1 ILE 3347 11.008 35.366 18.946 1.00 15.83 ATOM 4868 CD1 ILE 3347 11.542 35.388 20.341 1.00 16.40 ATOM 4869 C ILE 3347 14.115 35.447 16.643 1.00 17.76 ATOM 4870 O ILE 3347 14.223 34.569 15.787 1.00 18.04 ATOM 4871 N GLY 3348 14.645 36.650 16.493 1.00 15.82 ATOM 4872 CA GLY 3348 15.389 36.981 15.300 1.00 17.40 ATOM 4873 C GLY 3348 16.071 38.324 15.475 1.00 19.13 ATOM 4874 O GLY 3348 16.068 38.890 16.561 1.00 18.77 ATOM 4875 N LEU 3349 16.658 38.853 14.415 1.00 20.47 ATOM 4876 CA LEU 3349 17.314 40.130 14.552 1.00 21.34 ATOM 4877 CB LEU 3349 18.831 39.928 14.590 1.00 22.11 ATOM 4878 CG LEU 3349 19.598 39.437 13.373 1.00 20.52 ATOM 4879 CD1 LEU 3349 19.815 40.602 12.421 1.00 23.69 ATOM 4880 CD2 LEU 3349 20.940 38.868 13.815 1.00 19.06 ATOM 4881 C LEU 3349 16.894 41.072 13.437 1.00 23.13 ATOM 4882 O LEU 3349 16.408 40.628 12.406 1.00 23.32 ATOM 4883 N SER 3350 17.061 42.376 13.657 1.00 25.95 ATOM 4884 CA SER 3350 16.677 43.380 12.660 1.00 23.88 ATOM 4885 CB SER 3350 15.323 43.989 13.024 1.00 22.02 ATOM 4886 OG SER 3350 14.564 43.127 13.856 1.00 20.06 ATOM 4887 C SER 3350 17.702 44.503 12.618 1.00 23.27 ATOM 4888 O SER 3350 18.470 44.670 13.552 1.00 24.39 ATOM 4889 N HIS 3351 17.708 45.273 11.538 1.00 23.70 ATOM 4890 CA HIS 3351 18.622 46.403 11.439 1.00 25.12 ATOM 4891 CB HIS 3351 20.066 45.935 11.248 1.00 26.03 ATOM 4892 CG HIS 3351 20.311 45.254 9.942 1.00 28.05 ATOM 4893 CD2 HIS 3351 20.947 45.670 8.821 1.00 28.57 ATOM 4894 ND1 HIS 3351 19.876 43.973 9.683 1.00 28.17 ATOM 4895 CE1 HIS 3351 20.236 43.626 8.461 1.00 25.88 ATOM 4896 NE2 HIS 3351 20.888 44.636 7.916 1.00 27.45 ATOM 4897 C HIS 3351 18.268 47.385 10.335 1.00 25.20 ATOM 4898 O HIS 3351 17.614 47.038 9.355 1.00 27.97 ATOM 4899 N HIS 3352 18.707 48.622 10.527 1.00 25.02 ATOM 4900 CA HIS 3352 18.498 49.708 9.581 1.00 22.68 ATOM 4901 CB HIS 3352 17.509 50.733 10.124 1.00 22.61 ATOM 4902 CG HIS 3352 16.093 50.258 10.172 1.00 24.89 ATOM 4903 CD2 HIS 3352 15.552 49.031 9.994 1.00 25.59 ATOM 4904 ND1 HIS 3352 15.043 51.100 10.472 1.00 27.28 ATOM 4905 CE1 HIS 3352 13.916 50.411 10.481 1.00 27.37 ATOM 4906 NE2 HIS 3352 14.197 49.152 10.194 1.00 29.53 ATOM 4907 C HIS 3352 19.856 50.369 9.435 1.00 22.26 ATOM 4908 O HIS 3352 20.671 50.347 10.363 1.00 20.06 ATOM 4909 N SER 3353 20.109 50.950 8.273 1.00 21.46 ATOM 4910 CA SER 3353 21.382 51.606 8.047 1.00 22.89 ATOM 4911 CB SER 3353 22.185 50.828 7.013 1.00 24.69 ATOM 4912 OG SER 3353 22.276 49.466 7.388 1.00 27.42 ATOM 4913 C SER 3353 21.180 53.035 7.580 1.00 23.21 ATOM 4914 O SER 3353 20.061 53.441 7.281 1.00 24.15 ATOM 4915 N ALA 3354 22.267 53.797 7.537 1.00 23.66 ATOM 4916 CA ALA 3354 22.226 55.191 7.104 1.00 24.08 ATOM 4917 CB ALA 3354 21.800 56.094 8.250 1.00 21.96 ATOM 4918 C ALA 3354 23.610 55.569 6.613 1.00 23.61 ATOM 4919 O ALA 3354 24.589 54.890 6.929 1.00 23.28 ATOM 4920 N TRP 3355 23.688 56.634 5.816 1.00 25.31 ATOM 4921 CA TRP 3355 24.971 57.084 5.265 1.00 28.33 ATOM 4922 CB TRP 3355 24.919 57.091 3.733 1.00 34.37 ATOM 4923 CG TRP 3355 26.122 56.457 3.088 1.00 41.09 ATOM 4924 CD2 TRP 3355 27.356 57.106 2.749 1.00 43.54 ATOM 4925 CE2 TRP 3355 28.230 56.113 2.244 1.00 44.52 ATOM 4926 CE3 TRP 3355 27.814 58.433 2.824 1.00 46.23 ATOM 4927 CD1 TRP 3355 26.289 55.130 2.778 1.00 42.95 ATOM 4928 NE1 TRP 3355 27.552 54.918 2.271 1.00 44.11 ATOM 4929 CZ2 TRP 3355 29.538 56.403 1.819 1.00 46.99 ATOM 4930 CZ3 TRP 3355 29.125 58.725 2.395 1.00 46.82 ATOM 4931 CH2 TRP 3355 29.966 57.710 1.903 1.00 47.21 ATOM 4932 C TRP 3355 25.369 58.464 5.784 1.00 27.48 ATOM 4933 O TRP 3355 24.548 59.400 5.818 1.00 24.86 ATOM 4934 N LEU 3356 26.618 58.581 6.210 1.00 26.25 ATOM 4935 CA LEU 3356 27.137 59.820 6.743 1.00 24.44 ATOM 4936 CB LEU 3356 27.968 59.567 7.987 1.00 26.37 ATOM 4937 CG LEU 3356 28.642 60.839 8.517 1.00 26.66 ATOM 4938 CD1 LEU 3356 27.578 61.699 9.187 1.00 25.57 ATOM 4939 CD2 LEU 3356 29.746 60.490 9.505 1.00 25.10 ATOM 4940 C LEU 3356 28.003 60.498 5.710 1.00 23.94 ATOM 4941 O LEU 3356 29.026 59.954 5.285 1.00 20.62 ATOM 4942 N THR 3357 27.598 61.683 5.307 1.00 26.42 ATOM 4943 CA THR 3357 28.376 62.416 4.323 1.00 26.09 ATOM 4944 CB THR 3357 27.459 63.010 3.267 1.00 25.60 ATOM 4945 OG1 THR 3357 26.573 61.984 2.793 1.00 30.06 ATOM 4946 CG2 THR 3357 28.265 63.514 2.110 1.00 26.38 ATOM 4947 C THR 3357 29.198 63.499 4.993 1.00 23.29 ATOM 4948 O THR 3357 28.696 64.243 5.836 1.00 21.43 ATOM 4949 N VAL 3358 30.465 63.579 4.618 1.00 20.55 ATOM 4950 CA VAL 3358 31.325 64.568 5.231 1.00 22.35 ATOM 4951 CB VAL 3358 32.469 63.889 5.973 1.00 23.52 ATOM 4952 CG1 VAL 3358 33.132 64.901 6.887 1.00 24.27 ATOM 4953 CG2 VAL 3358 31.934 62.693 6.755 1.00 20.28 ATOM 4954 C VAL 3358 31.880 65.595 4.248 1.00 22.21 ATOM 4955 O VAL 3358 32.343 65.253 3.155 1.00 16.76 ATOM 4956 N LEU 3359 31.834 66.863 4.661 1.00 24.15 ATOM 4957 CA LEU 3359 32.276 67.973 3.822 1.00 25.25 ATOM 4958 CB LEU 3359 31.050 68.821 3.465 1.00 21.53 ATOM 4959 CG LEU 3359 29.968 68.004 2.752 1.00 20.11 ATOM 4960 CD1 LEU 3359 28.734 68.857 2.488 1.00 18.40 ATOM 4961 CD2 LEU 3359 30.553 67.447 1.448 1.00 16.31 ATOM 4962 C LEU 3359 33.383 68.851 4.404 1.00 26.37 ATOM 4963 O LEU 3359 33.406 69.014 5.644 1.00 31.30 ATOM 4964 S SO4 4000 5.633 24.099 44.777 1.00 72.77 ATOM 4965 O1 SO4 4000 4.278 23.915 44.236 1.00 73.25 ATOM 4966 O2 SO4 4000 6.603 23.359 43.945 1.00 72.28 ATOM 4967 O3 SO4 4000 5.958 25.529 44.784 1.00 72.55 ATOM 4968 O4 SO4 4000 5.678 23.586 46.157 1.00 75.61 ATOM 4969 S SO4 4001 10.965 21.084 46.120 1.00 83.74 ATOM 4970 O1 SO4 4001 12.014 21.413 47.103 1.00 84.81 ATOM 4971 O2 SO4 4001 11.205 19.741 45.559 1.00 83.81 ATOM 4972 O3 SO4 4001 9.641 21.112 46.776 1.00 83.46 ATOM 4973 O4 SO4 4001 11.008 22.071 45.032 1.00 84.31 ATOM 4974 S SO4 4002 −2.986 74.153 −11.455 1.00 58.62 ATOM 4975 O1 SO4 4002 −1.886 73.544 −12.230 1.00 56.25 ATOM 4976 O2 SO4 4002 −3.387 73.255 −10.356 1.00 57.05 ATOM 4977 O3 SO4 4002 −2.542 75.460 −10.941 1.00 59.05 ATOM 4978 O4 SO4 4002 −4.157 74.370 −12.323 1.00 63.86 ATOM 4979 S SO4 4003 0.500 75.090 −5.675 1.00 41.03 ATOM 4980 O1 SO4 4003 0.983 74.248 −6.786 1.00 39.49 ATOM 4981 O2 SO4 4003 0.212 74.253 −4.505 1.00 44.82 ATOM 4982 O3 SO4 4003 1.532 76.084 −5.344 1.00 46.05 ATOM 4983 O4 SO4 4003 −0.732 75.799 −6.055 1.00 44.94

TABLE 3 FGFR2(D2–D3) Complexed with FGF2 HEADER GROWTH FACTOR/GROWTH FACTOR RECEPTOR 19-APR-00 1EV2 TITLE CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR TITLE 2 LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR 2; COMPND 3 CHAIN: A, B, C, D; COMPND 4 FRAGMENT: THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2; COMPND 5 SYNONYM: FGF2; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: FIBROBLAST GROWTH FACTOR RECEPTOR 2; COMPND 10 CHAIN: E, F, G, H; COMPND 11 FRAGMENT: EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF COMPND 12 RECEPTOR 2 CONSISTING OF IMMUNOGLOBULIN LIKE DOMAINS II COMPND 13 (D2) AND III (D3); COMPND 14 SYNONYM: FGFR2; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 5 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 6 EXPRESSION_SYSTEM_PLASMID: PET15B; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET28A KEYWDS IMMUNOGLOBULIN (IG)LIKE DOMAINS BELONGING TO THE I-SET KEYWDS 2 SUBGROUP WITHIN IG-LIKE DOMAINS, B-TREFOIL FOLD EXPDTA X-RAY DIFFRACTION AUTHOR A. N. PLOTNIKOV, S. R. HUBBARD, J. SCHLESSINGER, M. MOHAMMADI REVDAT 1 31-MAY-00 1EV2 0 JRNL AUTH A. N. PLOTNIKOV, S. R. HUBBARD, J. SCHLESSINGER, JRNL AUTH 2 M. MOHAMMADI JRNL TITL CRYSTAL STRUCTURES OF TWO FGF-FGFR COMPLEXES JRNL TITL 2 REVEAL THE DETERMINANTS OF LIGAND-RECEPTOR JRNL TITL 3 SPECIFICITY JRNL REF CELL (CAMBRIDGE,MASS.) V. 101 413 2000 JRNL REFN ASTM CELLB5 US ISSN 0092-8674 REMARK  1 REMARK  2 REMARK  2 RESOLUTION. 2.2 ANGSTROMS. REMARK  3 REMARK  3 REFINEMENT. REMARK  3 PROGRAM : CNS REMARK  3 AUTHORS : BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE- REMARK  3    : KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU, REMARK  3    : READ, RICE, SIMONSON, WARREN REMARK  3 REMARK  3 REFINEMENT TARGET: ENGH & HUBER REMARK  3 REMARK  3 DATA USED IN REFINEMENT. REMARK  3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20 REMARK  3 RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00 REMARK  3 DATA CUTOFF   (SIGMA(F)) : 0.000 REMARK  3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL REMARK  3 COMPLETENESS (WORKING+TEST) (%) : 91.7 REMARK  3 NUMBER OF REFLECTIONS   : 84816 REMARK  3 REMARK  3 REMARK  3 FIT TO DATA USED IN REFINEMENT. REMARK  3 CROSS-VALIDATION METHOD   : NULL REMARK  3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK  3 R VALUE   (WORKING SET) : 0.248 REMARK  3 FREE R VALUE     : 0.273 REMARK  3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK  3 FREE R VALUE TEST SET COUNT  : 4291 REMARK  3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK  3 REMARK  3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK  3 TOTAL NUMBER OF BINS USED   : NULL REMARK  3 BIN RESOLUTION RANGE HIGH  (A) : NULL REMARK  3 BIN RESOLUTION RANGE LOW   (A) : NULL REMARK  3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK  3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK  3 BIN R VALUE   (WORKING SET) : NULL REMARK  3 BIN FREE R VALUE     : NULL REMARK  3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK  3 BIN FREE R VALUE TEST SET COUNT  : NULL REMARK  3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK  3 REMARK  3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK  3 PROTEIN ATOMS   : 9818 REMARK  3 NUCLEIC ACID ATOMS  : 0 REMARK  3 HETEROGEN ATOMS   : 20 REMARK  3 SOLVENT ATOMS   : 263 REMARK  3 REMARK  3 B VALUES. REMARK  3 FROM WILSON PLOT   (A**2) : NULL REMARK  3 MEAN B VALUE  (OVERALL, A**2) : NULL REMARK  3 OVERALL ANISOTROPIC B VALUE. REMARK  3 B11 (A**2) : −14.90300 REMARK  3 B22 (A**2) : −0.98800 REMARK  3 B33 (A**2) : 15.89200 REMARK  3 B12 (A**2) : 0.00000 REMARK  3 B13 (A**2) : 0.00000 REMARK  3 B23 (A**2) : −0.65800 REMARK  3 REMARK  3 ESTIMATED COORDINATE ERROR. REMARK  3 ESD FROM LUZZATI PLOT  (A) : NULL REMARK  3 ESD FROM SIGMAA    (A) : NULL REMARK  3 LOW RESOLUTION CUTOFF  (A) : NULL REMARK  3 REMARK  3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK  3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK  3 ESD FROM C-V SIGMAA   (A) : NULL REMARK  3 REMARK  3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK  3 BOND LENGTHS     (A) : 0.007 REMARK  3 BOND ANGLES   (DEGREES) : 1.33 REMARK  3 DIHEDRAL ANGLES  (DEGREES) : NULL REMARK  3 IMPROPER ANGLES  (DEGREES) : 0.78 REMARK  3 REMARK  3 ISOTROPIC THERMAL MODEL : NULL REMARK  3 REMARK  3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA REMARK  3 MAIN-CHAIN BOND    (A**2) : 0.87 ; 1.500 REMARK  3 MAIN-CHAIN ANGLE   (A**2) : 1.53 ; 2.000 REMARK  3 SIDE-CHAIN BOND    (A**2) : 1.16 ; 2.000 REMARK  3 SIDE-CHAIN ANGLE   (A**2) : 1.79 ; 2.500 REMARK  3 REMARK  3 REMARK  3 BULK SOLVENT MODELING. REMARK  3 METHOD USED : CNS REMARK  3 KSOL  : 0.38 REMARK  3 BSOL  : 47.84 REMARK  3 REMARK  3 NCS MODEL : NULL REMARK  3 REMARK  3 NCS RESTRAINTS.      RMS SIGMA/WEIGHT REMARK  3 GROUP 1 POSITIONAL   (A) : NULL ; NULL REMARK  3 GROUP 1 B-FACTOR   (A**2) : NULL ; NULL REMARK  3 REMARK  3 PARAMETER FILE 1 : NULL REMARK  3 TOPOLOGY FILE 1 : NULL REMARK  3 REMARK  3 OTHER REFINEMENT REMARKS: NULL REMARK  4 REMARK  4 1EV2 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-APR-2000. REMARK 100 THE RCSB ID CODE IS RCSB010917. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE    : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION  : 22-SEP-1999 REMARK 200 TEMPERATURE   (KELVIN) : 110.0 REMARK 200 PH       : 7.50 REMARK 200 NUMBER OF CRYSTALS USED  : 1 REMARK 200 REMARK 200 SYNCHROTRON    (Y/N) : Y REMARK 200 RADIATION SOURCE    : NSLS REMARK 200 BEAMLINE      : X4A REMARK 200 X-RAY GENERATOR MODEL   : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE  (A) : 0.9789 REMARK 200 MONOCHROMATOR     : NULL REMARK 200 OPTICS       : NULL REMARK 200 REMARK 200 DETECTOR TYPE     : CCD REMARK 200 DETECTOR MANUFACTURER   : SDMS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : SDMS REMARK 200 DATA SCALING SOFTWARE   : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 206913 REMARK 200 RESOLUTION RANGE HIGH  (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW    (A) : 25.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3 REMARK 200 DATA REDUNDANCY    : 2.200 REMARK 200 R MERGE     (I) : 0.04200 REMARK 200 R SYM     (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8 REMARK 200 DATA REDUNDANCY IN SHELL  : NULL REMARK 200 R MERGE FOR SHELL   (I) : 0.24100 REMARK 200 R SYM FOR SHELL   (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL   : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: AMORE REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, ISOPROPANOL, HEPES- REMARK 280 NAOH REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 REMARK 290 REMARK 290  SYMOP SYMMETRY REMARK 290  NNNMMM OPERATOR REMARK 290  1555 X,Y,Z REMARK 290 REMARK 290  WHERE NNN −> OPERATOR NUMBER REMARK 290   MMM −> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000  0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000  0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000  0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 8 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLY A 15 REMARK 465 SER A 146 REMARK 465 GLY B 15 REMARK 465 SER B 146 REMARK 465 GLY C 15 REMARK 465 SER C 146 REMARK 465 GLY D 15 REMARK 465 SER D 146 REMARK 465 ASN E 147 REMARK 465 SER E 148 REMARK 465 ASN E 149 REMARK 465 THR E 268 REMARK 465 VAL E 269 REMARK 465 VAL E 270 REMARK 465 GLY E 271 REMARK 465 GLY E 272 REMARK 465 GLU E 295 REMARK 465 LYS E 296 REMARK 465 ASN E 297 REMARK 465 GLY E 298 REMARK 465 SER E 299 REMARK 465 LYS E 300 REMARK 465 TYR E 301 REMARK 465 GLY E 302 REMARK 465 PRO E 303 REMARK 465 ASP E 304 REMARK 465 GLY E 305 REMARK 465 LEU E 306 REMARK 465 PRO E 361 REMARK 465 ALA E 362 REMARK 465 PRO E 363 REMARK 465 GLY E 364 REMARK 465 ARG E 365 REMARK 465 GLU E 366 REMARK 465 ASN F 147 REMARK 465 SER F 148 REMARK 465 ASN F 149 REMARK 465 GLY F 272 REMARK 465 VAL F 294 REMARK 465 GLU F 295 REMARK 465 LYS F 296 REMARK 465 ASN F 297 REMARK 465 GLY F 298 REMARK 465 SER F 299 REMARK 465 LYS F 300 REMARK 465 TYR F 301 REMARK 465 GLY F 302 REMARK 465 PRO F 303 REMARK 465 ASP F 304 REMARK 465 GLY F 305 REMARK 465 LEU F 306 REMARK 465 PRO F 307 REMARK 465 LEU F 360 REMARK 465 PRO F 361 REMARK 465 ALA F 362 REMARK 465 PRO F 363 REMARK 465 GLY F 364 REMARK 465 ARG F 365 REMARK 465 GLU F 366 REMARK 465 ASN G 147 REMARK 465 SER G 148 REMARK 465 ASN G 149 REMARK 465 ASN G 150 REMARK 465 GLU G 295 REMARK 465 LYS G 296 REMARK 465 ASN G 297 REMARK 465 GLY G 298 REMARK 465 SER G 299 REMARK 465 LYS G 300 REMARK 465 TYR G 301 REMARK 465 GLY G 302 REMARK 465 PRO G 303 REMARK 465 ASP G 304 REMARK 465 GLY G 305 REMARK 465 LEU G 306 REMARK 465 PRO G 307 REMARK 465 GLY G 364 REMARK 465 ARG G 365 REMARK 465 GLU G 366 REMARK 465 ASN H 147 REMARK 465 SER H 148 REMARK 465 ASN H 149 REMARK 465 ASN H 150 REMARK 465 GLU H 295 REMARK 465 LYS H 296 REMARK 465 ASN H 297 REMARK 465 GLY H 298 REMARK 465 SER H 299 REMARK 465 LYS H 300 REMARK 465 TYR H 301 REMARK 465 GLY H 302 REMARK 465 PRO H 303 REMARK 465 ASP H 304 REMARK 465 GLY H 305 REMARK 465 LEU H 306 REMARK 465 GLY H 364 REMARK 465 ARG H 365 REMARK 465 GLU H 366 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 HIS A 16 CG ND1 CD2 CE1 NE2 REMARK 470 ARG A 39 CG CD NE CZ NH1 NH2 REMARK 470 GLU A 45 CG CD OE1 OE2 REMARK 470 LYS A 46 CG CD CE NZ REMARK 470 SER A 47 OG REMARK 470 ARG A 72 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 77 CG CD CE NZ REMARK 470 GLU A 78 CG CD OE1 OE2 REMARK 470 ARG A 81 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 86 CG CD CE NZ REMARK 470 GLU A 91 CG CD OE1 OE2 REMARK 470 LYS A 110 CG CD CE NZ REMARK 470 TRP A 114 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP A 114 CZ3 CH2 REMARK 470 LYS A 119 CG CD CE NZ REMARK 470 ARG A 120 CG CD NE CZ NH1 NH2 REMARK 470 LEU A 126 CG CD1 CD2 REMARK 470 LYS A 129 CG CD CE NZ REMARK 470 LYS A 145 CG CD CE NZ REMARK 470 HIS B 16 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 46 CG CD CE NZ REMARK 470 HIS B 50 CG ND1 CD2 CE1 NE2 REMARK 470 LYS B 52 CG CD CE NZ REMARK 470 LYS B 77 CG CD CE NZ REMARK 470 GLU B 78 CG CD OE1 OE2 REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2 REMARK 470 LYS B 86 CG CD CE NZ REMARK 470 GLU B 91 CG CD OE1 OE2 REMARK 470 LYS B 110 CG CD CE NZ REMARK 470 TYR B 111 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TRP B 114 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP B 114 CZ3 CH2 REMARK 470 LYS B 119 CG CD CE NZ REMARK 470 ARG B 120 CG CD NE CZ NH1 NH2 REMARK 470 GLN B 123 CG CD OE1 NE2 REMARK 470 LEU B 126 CG CD1 CD2 REMARK 470 LYS B 145 CG CD CE NZ REMARK 470 HIS C 16 CG ND1 CD2 CE1 NE2 REMARK 470 HIS C 35 CG ND1 CD2 CE1 NE2 REMARK 470 ARG C 39 CG CD NE CZ NH1 NH2 REMARK 470 GLU C 45 CG CD OE1 OE2 REMARK 470 LYS C 46 CG CD CE NZ REMARK 470 SER C 69 OG REMARK 470 GLU C 78 CG CD OE1 OE2 REMARK 470 ARG C 81 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 86 CG CD CE NZ REMARK 470 ASN C 101 CG OD1 ND2 REMARK 470 ARG C 120 CG CD NE CZ NH1 NH2 REMARK 470 LYS C 129 CG CD CE NZ REMARK 470 LYS C 145 CG CD CE NZ REMARK 470 HIS D 16 CG ND1 CD2 CE1 NE2 REMARK 470 HIS D 35 CG ND1 CD2 CE1 NE2 REMARK 470 GLU D 45 CG CD OE1 OE2 REMARK 470 LYS D 46 CG CD CE NZ REMARK 470 ASP D 48 CG OD1 OD2 REMARK 470 SER D 69 OG REMARK 470 GLU D 78 CG CD OE1 OE2 REMARK 470 ARG D 81 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 86 CG CD CE NZ REMARK 470 SER D 87 OG REMARK 470 LYS D 119 CG CD CE NZ REMARK 470 ARG D 120 CG CD NE CZ NH1 NH2 REMARK 470 LYS D 129 CG CD CE NZ REMARK 470 LYS D 145 CG CD CE NZ REMARK 470 ASN E 150 CG OD1 ND2 REMARK 470 LYS E 151 CG CD CE NZ REMARK 470 GLU E 160 CG CD OE1 OE2 REMARK 470 LYS E 161 CG CD CE NZ REMARK 470 GLU E 163 CG CD OE1 OE2 REMARK 470 ASN E 184 CG OD1 ND2 REMARK 470 ARG E 210 CG CD NE CZ NH1 NH2 REMARK 470 ASN E 211 CG OD1 ND2 REMARK 470 GLN E 212 CG CD OE1 NE2 REMARK 470 HIS E 213 CG ND1 CD2 CE1 NE2 REMARK 470 GLU E 234 CG CD OE1 OE2 REMARK 470 SER E 267 OG REMARK 470 TYR E 281 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS E 292 CG CD CE NZ REMARK 470 HIS E 293 CG ND1 CD2 CE1 NE2 REMARK 470 VAL E 294 CG1 CG2 REMARK 470 TYR E 308 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS E 310 CG CD CE NZ REMARK 470 LYS E 322 CG CD CE NZ REMARK 470 GLU E 323 CG CD OE1 OE2 REMARK 470 ARG E 330 CG CD NE CZ NH1 NH2 REMARK 470 ASN E 331 CG OD1 ND2 REMARK 470 VAL E 332 CG1 CG2 REMARK 470 THR E 333 OG1 CG2 REMARK 470 PHE E 334 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU E 335 CG CD OE1 OE2 REMARK 470 VAL E 359 CG1 CG2 REMARK 470 LEU E 360 CG CD1 CD2 REMARK 470 ASN F 150 CG OD1 ND2 REMARK 470 LYS F 151 CG CD CE NZ REMARK 470 GLU F 160 CG CD OE1 OE2 REMARK 470 LYS F 161 CG CD CE NZ REMARK 470 GLU F 163 CG CD OE1 OE2 REMARK 470 ASN F 184 CG OD1 ND2 REMARK 470 ARG F 210 CG CD NE CZ NH1 NH2 REMARK 470 GLN F 212 CG CD OE1 NE2 REMARK 470 HIS F 213 CG ND1 CD2 CE1 NE2 REMARK 470 GLU F 234 CG CD OE1 OE2 REMARK 470 GLU F 236 CG CD OE1 OE2 REMARK 470 SER F 267 OG REMARK 470 VAL F 269 CG1 CG2 REMARK 470 VAL F 270 CG1 CG2 REMARK 470 HIS F 293 CG ND1 CD2 CE1 NE2 REMARK 470 TYR F 308 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS F 310 CG CD CE NZ REMARK 470 LYS F 322 CG CD CE NZ REMARK 470 GLU F 323 CG CD OE1 OE2 REMARK 470 TYR F 328 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ILE F 329 CG1 CG2 CD1 REMARK 470 ARG F 330 CG CD NE CZ NH1 NH2 REMARK 470 ASN F 331 CG OD1 ND2 REMARK 470 VAL F 332 CG1 CG2 REMARK 470 THR F 333 OG1 CG2 REMARK 470 PHE F 334 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU F 335 CG CD OE1 OE2 REMARK 470 TRP F 356 CG CD1 CD2 NE1 CE2 CE3 CZ2 REMARK 470 TRP F 356 CZ3 CH2 REMARK 470 THR F 358 OG1 CG2 REMARK 470 VAL F 359 CG1 CG2 REMARK 470 LYS G 151 CG CD CE NZ REMARK 470 GLU G 160 CG CD OE1 OE2 REMARK 470 ARG G 165 CG CD NE CZ NH1 NH2 REMARK 470 LYS G 176 CG CD CE NZ REMARK 470 LYS G 196 CG CD CE NZ REMARK 470 ARG G 203 CG CD NE CZ NH1 NH2 REMARK 470 ARG G 210 CG CD NE CZ NH1 NH2 REMARK 470 GLN G 212 CG CD OE1 NE2 REMARK 470 HIS G 213 CG ND1 CD2 CE1 NE2 REMARK 470 LYS G 226 CG CD CE NZ REMARK 470 GLU G 236 CG CD OE1 OE2 REMARK 470 ASP G 273 CG OD1 OD2 REMARK 470 TYR G 308 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS G 310 CG CD CE NZ REMARK 470 LYS G 322 CG CD CE NZ REMARK 470 GLU G 323 CG CD OE1 OE2 REMARK 470 GLU G 335 CG CD OE1 OE2 REMARK 470 LYS H 151 CG CD CE NZ REMARK 470 GLU H 160 CG CD OE1 OE2 REMARK 470 LYS H 161 CG CD CE NZ REMARK 470 ARG H 165 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 176 CG CD CE NZ REMARK 470 LYS H 196 CG CD CE NZ REMARK 470 GLU H 197 CG CD OE1 OE2 REMARK 470 LYS H 199 CG CD CE NZ REMARK 470 ARG H 210 CG CD NE CZ NH1 NH2 REMARK 470 ASN H 211 CG OD1 ND2 REMARK 470 GLN H 212 CG CD OE1 NE2 REMARK 470 GLU H 236 CG CD OE1 OE2 REMARK 470 HIS H 245 CG ND1 CD2 CE1 NE2 REMARK 470 VAL H 269 CG1 CG2 REMARK 470 HIS H 293 CG ND1 CD2 CE1 NE2 REMARK 470 TYR H 308 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS H 310 CG CD CE NZ REMARK 470 ASN H 318 CG OD1 ND2 REMARK 470 LYS H 322 CG CD CE NZ REMARK 470 GLU H 323 CG CD OE1 OE2 REMARK 470 PHE H 334 CG CD1 CD2 CE1 CE2 CZ REMARK 470 GLU H 335 CG CD OE1 OE2 REMARK 470 VAL H 359 CG1 CG2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 MET A 76 CE MET A 76 SD 0.046 REMARK 500 MET E 162 SD MET E 162 CG 0.047 REMARK 500 MET E 189 CE MET E 189 SD 0.050 REMARK 500 MET F 218 CE MET F 218 SD −0.073 REMARK 500 PRO F 286 CD PRO F 286 CG 0.048 REMARK 500 PRO G 361 CG PRO G 361 CB 0.061 REMARK 500 PRO G 363 CG PRO G 363 CB 0.051 REMARK 500 PRO H 363 CG PRO H 363 CB 0.048 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 ARG A  22 N - CA - C ANGL. DEV. = −10.0 DEGREES REMARK 500 SER A  64 N - CA - C ANGL. DEV. = −9.7 DEGREES REMARK 500 THR A 112 N - CA - C ANGL. DEV. = 10.5 DEGREES REMARK 500 VAL A 116 N - CA - C ANGL. DEV. = −10.5 DEGREES REMARK 500 ARG B  22 N - CA - C ANGL. DEV. = = 10.2 DEGREES REMARK 500 SER B  64 N - CA - C ANGL. DEV. = −9.9 DEGREES REMARK 500 THR B 112 N - CA - C ANGL. DEV. = 10.8 DEGREES REMARK 500 VAL B 116 N - CA - C ANGL. DEV. = −10.1 DEGREES REMARK 500 ARG C  22 N - CA - C ANGL. DEV. = −9.5 DEGREES REMARK 500 SER C  64 N - CA - C ANGL. DEV. = −9.0 DEGREES REMARK 500 THR C 112 N - CA - C ANGL. DEV. = 10.7 DEGREES REMARK 500 VAL C 116 N - CA - C ANGL. DEV. = −9.8 DEGREES REMARK 500 ARG D  22 N - CA - C ANGL. DEV. = −9.6 DEGREES REMARK 500 SER D  64 N - CA - C ANGL. DEV. = −9.2 DEGREES REMARK 500 THR D 112 N - CA - C ANGL. DEV. = 10.6 DEGREES REMARK 500 VAL D 116 N - CA - C ANGL. DEV. = −10.1 DEGREES REMARK 500 GLU E 234 N - CA - C ANGL. DEV. = 8.0 DEGREES REMARK 500 CYS E 342 N - CA - C ANGL. DEV. = −8.2 DEGREES REMARK 500 GLU F 234 N - CA - C ANGL. DEV. = 8.2 DEGREES REMARK 500 LEU F 258 CA - CB - CG ANGL. DEV. = 8.1 DEGREES REMARK 500 CYS F 342 N - CA - C ANGL. DEV. = −8.5 DEGREES REMARK 500 GLU G 234 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 500 ALA G 362 N - CA - C ANGL. DEV. = 13.7 DEGREES REMARK 500 PRO G 363 C - N - CA ANGL. DEV. = −10.5 DEGREES REMARK 500 GLU H 234 N - CA - C ANGL. DEV. = 8.6 DEGREES REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1CVS RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR REMARK 900 LIGAND BINDING DOMAIN OF FGF RECEPTOR 1 (FGFR1) REMARK 900 RELATED ID: 1EVT RELATED DB: PDB REMARK 900 FGF1-FGFR1 COMPLEX DBREF 1EV2 A  15 146 SWS P09038 FGF2_HUMAN  24 155 DBREF 1EV2 B  15 146 SWS P09038 FGF2_HUMAN  24 155 DBREF 1EV2 C  15 146 SWS P09038 FGF2_HUMAN  24 155 DBREF 1EV2 D  15 146 SWS P09038 FGF2_HUMAN  24 155 DBREF 1EV2 E 147 366 SWS P21802 FGR2_HUMAN 147 366 DBREF 1EV2 F 147 366 SWS P21802 FGR2_HUMAN 147 366 DEREF 1EV2 G 147 366 SWS P21802 FGR2_HUMAN 147 366 DBREF IEV2 H 147 366 SWS P21802 FGR2_HUMAN 147 366 SEQADV 1EV2 SER A 69 SWS P09038 CYS 78 ENGINEERED SEQADV 1EV2 SER A 87 SWS P09038 CYS 96 ENGINEERED SEQADV 1EV2 SER B 69 SWS P09038 CYS 78 ENGINEERED SEQADV 1EV2 SER B 87 SWS P09038 CYS 96 ENGINEERED SEQADV 1EV2 SER C 69 SWS P09038 CYS 78 ENGINEERED SEQADV 1EV2 SER C 87 SWS P09038 CYS 96 ENGINEERED SEQADV 1EV2 SER D 69 SWS P09038 CYS 78 ENGINEERED SEQADV 1EV2 SER D 87 SWS P09038 CYS 96 ENGINEERED SEQRES  1 A 132 GLY HIS PHE LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN SEQRES  2 A 132 GLY GLY PHE PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL SEQRES  3 A 132 ASP GLY VAL ARG GLU LYS SER ASP PRO HIS ILE LYS LEU SEQRES  4 A 132 GLN LEU GLN ALA GLU GLU ARG GLY VAL VAL SER ILE LYS SEQRES  5 A 132 GLY VAL SER ALA ASN ARG TYR LEU ALA MET LYS GLU ASP SEQRES  6 A 132 GLY ARG LEU LEU ALA SER LYS SER VAL THR ASP GLU CYS SEQRES  7 A 132 PHE PHE PHE GLU ARG LEU GLU SER ASN ASN TYR ASN THR SEQRES  8 A 132 TYR ARG SER ARG LYS TYR THR SER TRP TYR VAL ALA LEU SEQRES  9 A 132 LYS ARG THR GLY GLN TYR LYS LEU GLY SER LYS THR GLY SEQRES 10 A 132 PRO GLY GLN LYS ALA ILE LEU PHE LEU PRO MET SER ALA SEQRES 11 A 132 LYS SER SEQRES  1 B 132 GLY HIS PHE LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN SEQRES  2 B 132 GLY GLY PHE PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL SEQRES  3 B 132 ASP GLY VAL ARG GLU LYS SER ASP PRO HIS ILE LYS LEU SEQRES  4 B 132 GLN LEU GLN ALA GLU GLU ARG GLY VAL VAL SER ILE LYS SEQRES  5 B 132 GLY VAL SER ALA ASN ARG TYR LEU ALA MET LYS GLU ASP SEQRES  6 B 132 GLY ARG LEU LEU ALA SER LYS SER VAL THR ASP GLU CYS SEQRES  7 B 132 PHE PHE PHE GLU ARG LEU GLU SER ASN ASN TYR ASN THR SEQRES  8 B 132 TYR ARG SER ARG LYS TYR THR SER TRP TYR VAL ALA LEU SEQRES  9 B 132 LYS ARG THR GLY GLN TYR LYS LEU GLY SER LYS THR GLY SEQRES 10 B 132 PRO GLY GLN LYS ALA ILE LEU PHE LEU PRO MET SER ALA SEQRES 11 B 132 LYS SER SEQRES  1 C 132 GLY HIS PHE LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN SEQRES  2 C 132 GLY GLY PHE PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL SEQRES  3 C 132 ASP GLY VAL ARG GLU LYS SER ASP PRO HIS ILE LYS LEU SEQRES  4 C 132 GLN LEU GLN ALA GLU GLU ARG GLY VAL VAL SER ILE LYS SEQRES  5 C 132 GLY VAL SER ALA ASN ARG TYR LEU ALA MET LYS GLU ASP SEQRES  6 C 132 GLY ARG LEU LEU ALA SER LYS SER VAL THR ASP GLU CYS SEQRES  7 C 132 PHE PHE PHE GLU ARG LEU GLU SER ASN ASN TYR ASN THR SEQRES  8 C 132 TYR ARG SER ARG LYS TYR THR SER TRP TYR VAL ALA LEU SEQRES  9 C 132 LYS ARG THR GLY GLN TYR LYS LEU GLY SER LYS THR GLY SEQRES 10 C 132 PRO GLY GLN LYS ALA ILE LEU PHE LEU PRO MET SER ALA SEQRES 11 C 132 LYS SER SEQRES  1 D 132 GLY HIS PHE LYS ASP PRO LYS ARG LEU TYR CYS LYS ASN SEQRES  2 D 132 GLY GLY PHE PHE LEU ARG ILE HIS PRO ASP GLY ARG VAL SEQRES  3 D 132 ASP GLY VAL ARG GLU LYS SER ASP PRO HIS ILE LYS LEU SEQRES  4 D 132 GLN LEU GLN ALA GLU GLU ARG GLY VAL VAL SER ILE LYS SEQRES  5 D 132 GLY VAL SER ALA ASN ARG TYR LEU ALA MET LYS GLU ASP SEQRES  6 D 132 GLY ARG LEU LEU ALA SER LYS SER VAL THR ASP GLU CYS SEQRES  7 D 132 PHE PHE PHE GLU ARG LEU GLU SER ASN ASN TYR ASN THR SEQRES  8 D 132 TYR ARG SER ARG LYS TYR THR SER TRP TYR VAL ALA LEU SEQRES  9 D 132 LYS ARG THR GLY GLN TYR LYS LEU GLY SER LYS THR GLY SEQRES 10 D 132 PRO GLY GLN LYS ALA ILE LEU PHE LEU PRO MET SER ALA SEQRES 11 D 132 LYS SER SEQRES  1 E 220 ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR SEQRES  2 E 220 GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA SEQRES  3 E 220 ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO SEQRES  4 E 220 MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE SEQRES  5 E 220 LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN SEQRES  6 E 220 GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER SEQRES  7 E 220 ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR SEQRES  8 E 220 GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU SEQRES  9 E 220 ARG SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO SEQRES 10 E 220 ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE SEQRES 11 E 220 VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN SEQRES 12 E 220 TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY SEQRES 13 E 220 PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA SEQRES 14 E 220 GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR SEQRES 15 E 220 ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR SEQRES 16 E 220 CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER SEQRES 17 E 220 ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU SEQRES  1 F 220 ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR SEQRES  2 F 220 GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA SEQRES  3 F 220 ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO SEQRES  4 F 220 MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE SEQRES  5 F 220 LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN SEQRES  6 F 220 GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER SEQRES  7 F 220 ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR SEQRES  8 F 220 GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU SEQRES  9 F 220 ARG SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO SEQRES 10 F 220 ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE SEORES 11 F 220 VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN SEQRES 12 F 220 TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY SEQRES 13 F 220 PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA SEQRES 14 F 220 GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR SEQRES 15 F 220 ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR SEQRES 16 F 220 CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER SEQRES 17 F 220 ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU SEQRES  1 G 220 ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR SEQRES  2 G 220 GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA SEQRES  3 G 220 ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO SEQRES  4 G 220 MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE SEQRES  5 G 220 LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN SEQRES  6 G 220 GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER SEQRES  7 G 220 ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR SEQRES  8 G 220 GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU SEQRES  9 G 220 ARG SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO SEQRES 10 G 220 ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE SEQRES 11 G 220 VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN SEQRES 12 G 220 TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY SEQRES 13 G 220 PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA SEQRES 14 G 220 GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR SEQRES 15 G 220 ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR SEQRES 16 G 220 CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER SEQRES 17 G 220 ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU SEQRES  1 H 220 ASN SER ASN ASN LYS ARG ALA PRO TYR TRP THR ASN THR SEQRES  2 H 220 GLU LYS MET GLU LYS ARG LEU HIS ALA VAL PRO ALA ALA SEQRES  3 H 220 ASN THR VAL LYS PHE ARG CYS PRO ALA GLY GLY ASN PRO SEQRES  4 H 220 MET PRO THR MET ARG TRP LEU LYS ASN GLY LYS GLU PHE SEQRES  5 H 220 LYS GLN GLU HIS ARG ILE GLY GLY TYR LYS VAL ARG ASN SEQRES  6 H 220 GLN HIS TRP SER LEU ILE MET GLU SER VAL VAL PRO SER SEQRES  7 H 220 ASP LYS GLY ASN TYR THR CYS VAL VAL GLU ASN GLU TYR SEQRES  8 H 220 GLY SER ILE ASN HIS THR TYR HIS LEU ASP VAL VAL GLU SEQRES  9 H 220 ARG SER PRO HIS ARG PRO ILE LEU GLN ALA GLY LEU PRO SEQRES 10 H 220 ALA ASN ALA SER THR VAL VAL GLY GLY ASP VAL GLU PHE SEQRES 11 H 220 VAL CYS LYS VAL TYR SER ASP ALA GLN PRO HIS ILE GLN SEQRES 12 H 220 TRP ILE LYS HIS VAL GLU LYS ASN GLY SER LYS TYR GLY SEQRES 13 H 220 PRO ASP GLY LEU PRO TYR LEU LYS VAL LEU LYS ALA ALA SEQRES 14 H 220 GLY VAL ASN THR THR ASP LYS GLU ILE GLU VAL LEU TYR SEQRES 15 H 220 ILE ARG ASN VAL THR PHE GLU ASP ALA GLY GLU TYR THR SEQRES 16 H 220 CYS LEU ALA GLY ASN SER ILE GLY ILE SER PHE HIS SER SEQRES 17 H 220 ALA TRP LEU THR VAL LEU PRO ALA PRO GLY ARG GLU HET SO4 9001 5 HET SO4 9002 5 HET SO4 9003 5 HET SO4 9004 5 HETNAM  SO4 SULFATE ION FORMUL 9 SO4 4(O4 S1 2−) FORMUL 13 HOH *263(H2 O1) HELIX 1 1 LEU A 126 THR A 130 5 5 HELIX 2 2 LEU B 126 THR B 130 5 5 HELIX 3 3 LEU C 126 THR C 130 5 5 HELIX 4 4 LEU D 126 THR D 130 5 5 HELIX 5 5 ASN E 158 GLU E 163 5 6 HELIX 6 6 LYS E 199 ARG E 203 5 5 HELIX 7 7 ASN E 211 HIS E 213 5 3 HELIX 8 8 VAL E 222 LYS E 226 5 5 HELIX 9 9 THR E 333 ALA E 337 5 5 HELIX 10 10 ASN F 158 GLU F 163 5 6 HELIX 11 11 LYS F 199 ARG F 203 5 5 HELIX 12 12 ASN F 211 HIS F 213 5 3 HELIX 13 13 VAL F 222 LYS F 226 5 5 HELIX 14 14 THR F 333 ALA F 337 5 5 HELIX 15 15 ASN G 158 GLU G 163 5 6 HELIX 16 16 LYS G 199 ARG G 203 5 5 HELIX 17 17 ASN G 211 HIS G 213 5 3 HELIX 18 18 VAL G 222 LYS G 226 5 5 HELIX 19 19 THR G 333 ALA G 337 5 5 HELIX 20 20 ASN H 158 GLU H 163 5 6 HELIX 21 21 LYS H 199 ARG H 203 5 5 HELIX 22 22 ASN H 211 HIS H 213 5 3 HELIX 23 23 VAL H 222 LYS H 226 5 5 HELIX 24 24 THR H 333 ALA H 337 5 5 SHEET 1 A 4 VAL A 40 VAL A 43 0 SHEET 2 A 4 PHE A 30 ILE A 34 −1 N PHE A 31 O VAL A 43 SHEET 3 A 4 LYS A 21 CYS A 25 −1 O LEU A 23 N LEU A 32 SHEET 4 A 4 PHE A 139 SER A 143 −1 N LEU A 140 O TYR A 24 SHEET 1 B 4 LEU A 53 GLU A 59 0 SHEET 2 B 4 VAL A 62 GLY A 67 −1 N VAL A 62 O GLU A 59 SHEET 3 B 4 ARG A 72 MET A 76 −1 O ARG A 72 N GLY A 67 SHEET 4 B 4 LEU A 82 SER A 85 −1 O LEU A 83 N ALA A 75 SHEET 1 C 4 LEU A 53 GLU A 59 0 SHEET 2 C 4 VAL A 62 GLY A 67 −1 N VAL A 62 O GLU A 59 SHEET 3 C 4 PHE A 94 LEU A 98 −1 N PHE A 94 O VAL A 63 SHEET 4 C 4 ASN A 104 SER A 108 −1 O THR A 105 N ARG A 97 SHEET 1 D 4 VAL B 40 VAL B 43 0 SHEET 2 D 4 PHE B 30 ILE B 34 −1 N PHE B 31 O VAL B 43 SHEET 3 D 4 LYS B 21 CYS B 25 −1 O LEU B 23 N LEU B 32 SHEET 4 D 4 PHE B 139 SER B 143 −1 N LEU B 140 O TYR B 24 SHEET 1 E 4 LEU B 53 GLU B 59 0 SHEET 2 E 4 VAL B 62 GLY B 67 −1 N VAL B 62 O GLU B 59 SHEET 3 E 4 ARG B 72 MET B 76 −1 O ARG B 72 N GLY B 67 SHEET 4 E 4 LEU B 82 SER B 85 −1 O LEU B 83 N ALA B 75 SHEET 1 F 4 LEU B 53 GLU B 59 0 SHEET 2 F 4 VAL B 62 GLY B 67 −1 N VAL B 62 O GLU B 59 SHEET 3 F 4 PHE B 94 LEU B 98 −1 N PHE B 94 O VAL B 63 SHEET 4 F 4 ASN B 104 SER B 108 −1 O THR B 105 N ARG B 97 SHEET 1 G 4 VAL C 40 VAL C 43 0 SHEET 2 G 4 PHE C 30 ILE C 34 −1 N PHE C 31 O VAL C 43 SHEET 3 G 4 LYS C 21 CYS C 25 −1 O LEU C 23 N LEU C 32 SHEET 4 G 4 PHE C 139 SER C 143 −1 N LEU C 140 O TYR C 24 SHEET 1 H 4 LEU C 53 GLU C 59 0 SHEET 2 H 4 VAL C 62 GLY C 67 −1 N VAL C 62 O GLU C 59 SHEET 3 H 4 ARG C 72 MET C 76 −1 O ARG C 72 N GLY C 67 SHEET 4 H 4 LEU C 82 SER C 85 −1 O LEU C 83 N ALA C 75 SHEET 1 I 4 LEU C 53 GLU C 59 0 SHEET 2 I 4 VAL C 62 GLY C 67 −1 N VAL C 62 O GLU C 59 SHEET 3 I 4 PHE C 94 LEU C 98 −1 O PHE C 94 N VAL C 63 SHEET 4 I 4 ASN C 104 SER C 108 −1 O THR C 105 N ARG C 97 SHEET 1 J 4 VAL D 40 VAL D 43 0 SHEET 2 J 4 PHE D 30 ILE D 34 −1 N PHE D 31 O VAL D 43 SHEET 3 J 4 LYS D 21 CYS D 25 −1 O LEU D 23 N LEU D 32 SHEET 4 J 4 PHE D 139 SER D 143 −1 N LEU D 140 O TYR D 24 SHEET 1 K 4 LEU D 53 GLU D 59 0 SHEET 2 K 4 VAL D 62 GLY D 67 −1 N VAL D 62 O GLU D 59 SHEET 3 K 4 ARG D 72 MET D 76 −1 O ARG D 72 N GLY D 67 SHEET 4 K 4 LEU D 82 SER D 85 −1 O LEU D 83 N ALA D 75 SHEET 1 L 4 LEU D 53 GLU D 59 0 SHEET 2 L 4 VAL D 62 GLY D 67 −1 N VAL D 62 O GLU D 59 SHEET 3 L 4 PHE D 94 LEU D 98 −1 O PHE D 94 N VAL D 63 SHEET 4 L 4 ASN D 104 SER D 108 −1 O THR D 105 N ARG D 97 SHEET 1 M 2 ARG E 152 TRP E 156 0 SHEET 2 M 2 ALA E 181 ASN E 184 −1 N GLY E 182 O TYR E 155 SHEET 1 N 5 LEU E 166 PRO E 170 0 SHEET 2 N 5 GLY E 238 VAL E 249 1 O HIS E 245 N HIS E 167 SHEET 3 N 5 GLY E 227 ASN E 235 −1 O GLY E 227 N LEU E 246 SHEET 4 N 5 THR E 188 LYS E 193 −1 N THR E 188 O GLU E 234 SHEET 5 N 5 LYS E 196 GLU E 197 −1 O LYS E 196 N LYS E 193 SHEET 1 O 3 VAL E 175 ARG E 178 0 SHEET 2 O 3 SER E 215 MET E 218 −1 O LEU E 216 N PHE E 177 SHEET 3 O 3 LYS E 208 ARG E 210 −1 O LYS E 208 N ILE E 217 SHEET 1 P 2 ILE E 257 LEU E 258 0 SHEET 2 P 2 VAL E 280 TYR E 281 −1 O TYR E 281 N ILE E 257 SHEET 1 Q 2 VAL E 274 VAL E 277 0 SHEET 2 Q 2 VAL E 326 ILE E 329 −1 N LEU E 327 O PHE E 276 SHEET 1 R 4 LEU E 309 ALA E 314 0 SHEET 2 R 4 HIS E 287 HIS E 293 −1 N TRP E 290 O LYS E 313 SHEET 3 R 4 GLY E 338 GLY E 345 −1 O GLU E 339 N HIS E 293 SHEET 4 R 4 ILE E 350 LEU E 357 −1 O SER E 351 N ALA E 344 SHEET 1 S 2 ARG F 152 TRP F 156 0 SHEET 2 S 2 ALA F 181 ASN F 184 −1 N GLY F 182 O TYR F 155 SHEET 1 T 5 LEU F 166 PRO F 170 0 SHEET 2 T 5 GLY F 238 VAL F 249 1 O HIS F 245 N HIS F 167 SHEET 3 T 5 GLY F 227 ASN F 235 −1 O GLY F 227 N LEU F 246 SHEET 4 T 5 THR F 188 LYS F 193 −1 N THR F 188 O GLU F 234 SHEET 5 T 5 LYS F 196 GLU F 197 −1 O LYS F 196 N LYS F 193 SHEET 1 U 3 VAL F 175 ARG F 178 0 SHEET 2 U 3 SER F 215 MET F 218 −1 O LEU F 216 N PHE F 177 SHEET 3 U 3 LYS F 208 ARG F 210 −1 O LYS F 208 N ILE F 217 SHEET 1 V 2 ILE F 257 LEU F 258 0 SHEET 2 V 2 VAL F 280 TYR F 281 −1 O TYR F 281 N ILE F 257 SHEET 1 W 5 ALA F 266 SER F 267 0 SHEET 2 W 5 ILE F 350 THR F 358 1 O TRP F 356 N ALA F 266 SHEET 3 W 5 GLY F 338 GLY F 345 −1 O GLY F 338 N LEU F 357 SHEET 4 W 5 HIS F 287 LYS F 292 −1 N HIS F 287 O GLY F 345 SHEET 5 W 5 LYS F 310 ALA F 314 −1 O LYS F 310 N LYS F 292 SHEET 1 X 2 VAL F 274 VAL F 277 0 SHEET 2 X 2 VAL F 326 ILE F 329 −1 N LEU F 327 O PHE F 276 SHEET 1 Y 2 ARG G 152 TRP G 156 0 SHEET 2 Y 2 ALA G 181 ASN G 184 −1 N GLY G 182 O TYR G 155 SHEET 1 Z 5 LEU G 166 PRO G 170 0 SHEET 2 Z 5 GLY G 238 VAL G 249 1 O HIS G 245 N HIS G 167 SHEET 3 Z 5 GLY G 227 ASN G 235 −1 O GLY G 227 N LEU G 246 SHEET 4 Z 5 THR G 188 LYS G 193 −1 N THR G 188 O LEU G 234 SHEET 5 Z 5 LYS G 196 GLU G 197 −1 O LYS G 196 N LYS G 193 SHEET 1 AA 3 VAL G 175 ARG G 178 0 SHEET 2 AA 3 SER G 215 MET G 218 −1 O LEU G 216 N PHE G 177 SHEET 3 AA 3 LYS G 208 ARG G 210 −1 O LYS G 208 N ILE G 217 SHEET 1 AB 2 ILE G 257 LEU G 258 0 SHEET 2 AB 2 VAL G 280 TYR G 281 −1 O TYR G 281 N ILE G 257 SHEET 1 AC 5 ALA G 266 VAL G 269 0 SHEET 2 AC 5 ILE G 350 LEU G 360 1 O TRP G 356 N ALA G 266 SHEET 3 AC 5 GLY G 338 GLY G 345 −1 O GLY G 338 N LEU G 357 SHEET 4 AC 5 HIS G 287 HIS G 293 −1 N HIS G 287 O GLY G 345 SHEET 5 AC 5 LEU G 309 ALA G 314 −1 O LYS G 310 N LYS G 292 SHEET 1 AD 2 VAL G 274 VAL G 277 0 SHEET 2 AD 2 VAL G 326 ILE G 329 −1 N LEU G 327 O PHE G 276 SHEET 1 AE 2 ARG H 152 TRP H 156 0 SHEET 2 AE 2 ALA H 181 ASN H 184 −1 N GLY H 182 O TYR H 155 SHEET 1 AF 5 LEU H 166 PRO H 170 0 SHEET 2 AF 5 GLY H 238 VAL H 249 1 O HIS H 245 N HIS H 167 SHEET 3 AF 5 GLY H 227 ASN H 235 −1 O GLY H 227 N LEU H 246 SHEET 4 AF 5 THR H 188 LYS H 193 −1 N THR H 188 O GLU H 234 SHEET 5 AF 5 LYS H 196 GLU H 197 −1 O LYS H 196 N LYS H 193 SHEET 1 AG 3 VAL H 175 ARG H 178 0 SHEET 2 AG 3 SER H 215 MET H 218 −1 O LEU H 216 N PHE H 177 SHEET 3 AG 3 LYS H 208 ARG H 210 −1 O LYS H 208 N ILE H 217 SHEET 1 AH 2 ILE H 257 LEU H 258 0 SHEET 2 AH 2 VAL H 280 TYR H 281 −1 O TYR H 281 N ILE H 257 SHEET 1 AI 5 ALA H 266 VAL H 269 0 SHEET 2 AI 5 ILE H 350 LEU H 360 1 O TRP H 356 N ALA H 266 SHEET 3 AI 5 GLY H 338 GLY H 345 −1 O GLY H 338 N LEU H 357 SHEET 4 AI 5 HIS H 287 HIS H 293 −1 N HIS H 287 O GLY H 345 SHEET 5 AI 5 LEU H 309 ALA H 314 −1 O LYS H 310 N LYS H 292 SHEET 1 AJ 2 VAL H 274 VAL H 277 0 SHEET 2 AJ 2 VAL H 326 ILE H 329 −1 N LEU H 327 O PHE H 276 SSBOND 1 CYS E 179 CYS E 231 SSBOND 2 CYS E 278 CYS E 342 SSBOND 3 CYS F 179 CYS F 231 SSBOND 4 CYS F 278 CYS F 342 SSBOND 5 CYS G 179 CYS G 231 SSBOND 6 CYS G 278 CYS G 342 SSBOND 7 CYS H 179 CYS H 231 SSBOND 8 CYS H 278 CYS H 342 CISPEP 1 ASN E 184 PRO E 185 0 0.40 CISPEP 2 LEU E 262 PRO E 263 0 −0.38 CISPEP 3 ASN F 184 PRO F 185 0 0.15 CISPEP 4 LEU F 262 PRO F 263 0 −0.12 CISPEP 5 ASN G 184 PRO G 185 0 0.49 CISPEP 6 LEU G 262 PRO G 263 0 −0.21 CISPEP 7 ASN H 184 PRO H 185 0 0.32 CISPEP 8 LEU H 262 PRO H 263 0 0.10 CRYST1 72.198 71.677 90.920 90.53 89.98 89.99 P 1   4 ORIGX1  1.000000   0.000000   0.000000  0.00000 ORIGX2  0.000000   1.000000   0.000000  0.00000 ORIGX3  0.000000   0.000000   1.000000  0.00000 SCALE1  0.013851 −0.000002 −0.000005  0.00000 SCALE2  0.000000   0.013951   0.000129  0.00000 SCALE3  0.000000   0.000000   0.010999  0.00000 ATOM 1 N HIS A 16 65.781 −6.823 6.422 1.00 40.96 N ATOM 2 CA HIS A 16 66.617 −7.615 7.378 1.00 40.54 C ATOM 3 C HIS A 16 68.092 −7.469 7.011 1.00 39.31 C ATOM 4 O HIS A 16 68.508 −7.845 5.917 1.00 39.03 O ATOM 5 CB HIS A 16 66.208 −9.095 7.337 1.00 41.05 C ATOM 6 N PHE A 17 68.872 −6.932 7.942 1.00 38.01 N ATOM 7 CA PHE A 17 70.295 −6.694 7.734 1.00 37.01 C ATOM 8 C PHE A 17 71.138 −7.925 7.375 1.00 36.59 C ATOM 9 O PHE A 17 72.148 −7.797 6.674 1.00 35.98 O ATOM 10 CB PHE A 17 70.876 −6.008 8.975 1.00 35.65 C ATOM 11 CG PHE A 17 70.934 −6.887 10.184 1.00 35.24 C ATOM 12 CD1 PHE A 17 72.061 −7.659 10.442 1.00 35.09 C ATOM 13 CD2 PHE A 17 69.877 −6.928 11.084 1.00 35.37 C ATOM 14 CE1 PHE A 17 72.139 −8.452 11.578 1.00 35.43 C ATOM 15 CE2 PHE A 17 69.942 −7.724 12.231 1.00 35.92 C ATOM 16 CZ PHE A 17 71.075 −8.487 12.479 1.00 35.61 C ATOM 17 N LYS A 18 70.743 −9.106 7.844 1.00 36.25 N ATOM 18 CA LYS A 18 71.527 −10.296 7.529 1.00 37.09 C ATOM 19 C LYS A 18 71.279 −10.894 6.143 1.00 37.63 C ATOM 20 O LYS A 18 72.035 −11.753 5.690 1.00 38.05 O ATOM 21 CB LYS A 18 71.410 −11.364 8.626 1.00 37.68 C ATOM 22 CG LYS A 18 70.092 −11.449 9.358 1.00 40.55 C ATOM 23 CD LYS A 18 70.220 −12.396 10.551 1.00 41.58 C ATOM 24 CE LYS A 18 68.877 −12.603 11.238 1.00 42.51 C ATOM 25 NZ LYS A 18 68.252 −11.308 11.616 1.00 43.74 N ATOM 26 N ASP A 19 70.251 −10.412 5.453 1.00 37.64 N ATOM 27 CA ASP A 19 69.948 −10.882 4.106 1.00 37.79 C ATOM 28 C ASP A 19 70.899 −10.289 3.067 1.00 37.96 C ATOM 29 O ASP A 19 71.364 −9.150 3.206 1.00 37.12 O ATOM 30 CB ASP A 19 68.532 −10.476 3.701 1.00 39.51 C ATOM 31 CG ASP A 19 67.454 −11.162 4.521 1.00 40.50 C ATOM 32 OD1 ASP A 19 66.291 −10.708 4.445 1.00 40.65 O ATOM 33 OD2 ASP A 19 67.760 −12.152 5.220 1.00 41.75 O ATOM 34 N PRO A 20 71.209 −11.066 2.011 1.00 38.07 N ATOM 35 CA PRO A 20 72.092 −10.620 0.929 1.00 37.64 C ATOM 36 C PRO A 20 71.431 −9.441 0.211 1.00 37.31 C ATOM 37 O PRO A 20 70.217 −9.264 0.300 1.00 36.68 O ATOM 38 CB PRO A 20 72.208 −11.860 0.033 1.00 38.78 C ATOM 39 CG PRO A 20 70.966 −12.663 0.352 1.00 39.38 C ATOM 40 CD PRO A 20 70.850 −12.489 1.845 1.00 38.63 C ATOM 41 N LYS A 21 72.218 −8.648 −0.508 1.00 36.88 N ATOM 42 CA LYS A 21 71.676 −7.467 −1.180 1.00 37.48 C ATOM 43 C LYS A 21 72.379 −7.166 −2.476 1.00 37.29 C ATOM 44 O LYS A 21 73.460 −7.684 −2.752 1.00 37.08 O ATOM 45 CB LYS A 21 71.872 −6.198 −0.336 1.00 37.95 C ATOM 46 CG LYS A 21 71.512 −6.244 1.129 1.00 38.66 C ATOM 47 CD LYS A 21 71.931 −4.921 1.755 1.00 40.44 C ATOM 48 CE LYS A 21 71.606 −4.821 3.239 1.00 42.18 C ATOM 49 NZ LYS A 21 71.769 −3.412 3.691 1.00 42.97 N ATOM 50 N ARG A 22 71.761 −6.288 −3.254 1.00 36.67 N ATOM 51 CA ARG A 22 72.355 −5.825 −4.492 1.00 36.55 C ATOM 52 C ARG A 22 72.707 −4.390 −4.132 1.00 35.63 C ATOM 53 O ARG A 22 71.986 −3.755 −3.360 1.00 36.38 O ATOM 54 CB ARG A 22 71.340 −5.813 −5.633 1.00 38.00 C ATOM 55 CG ARG A 22 70.630 −7.118 −5.891 1.00 40.54 C ATOM 56 CD ARG A 22 69.712 −6.938 −7.092 1.00 43.45 C ATOM 57 NE ARG A 22 68.439 −7.649 −6.962 1.00 47.18 N ATOM 58 CZ ARG A 22 68.163 −8.822 −7.524 1.00 48.01 C ATOM 59 NH1 ARG A 22 69.072 −9.436 −8.267 1.00 50.26 N ATOM 60 NH2 ARG A 22 66.971 −9.381 −7.348 1.00 48.58 N ATOM 61 N LEU A 23 73.818 −3.881 −4.647 1.00 34.34 N ATOM 62 CA LEU A 23 74.201 −2.502 −4.380 1.00 32.35 C ATOM 63 C LEU A 23 74.093 −1.739 −5.696 1.00 32.62 C ATOM 64 O LEU A 23 74.914 −1.906 −6.603 1.00 32.26 O ATOM 65 CB LEU A 23 75.617 −2.419 −3.811 1.00 30.80 C ATOM 66 CG LEU A 23 75.763 −2.709 −2.306 1.00 30.93 C ATOM 67 CD1 LEU A 23 77.234 −2.691 −1.923 1.00 30.37 C ATOM 68 CD2 LEU A 23 75.009 −1.662 −1.491 1.00 29.15 C ATOM 69 N TYR A 24 73.051 −0.910 −5.783 1.00 31.86 N ATOM 70 CA TYR A 24 72.740 −0.103 −6.965 1.00 31.06 C ATOM 71 C TYR A 24 73.479 1.236 −6.959 1.00 31.28 C ATOM 72 O TYR A 24 73.373 2.008 −6.011 1.00 31.13 O ATOM 73 CB TYR A 24 71.207 0.107 −7.032 1.00 30.62 C ATOM 74 CG TYR A 24 70.689 1.069 −8.092 1.00 29.13 C ATOM 75 CD1 TYR A 24 70.769 2.450 −7.906 1.00 29.62 C ATOM 76 CD2 TYR A 24 70.099 0.599 −9.268 1.00 29.08 C ATOM 77 CE1 TYR A 24 70.271 3.346 −8.864 1.00 29.47 C ATOM 78 CE2 TYR A 24 69.598 1.484 −10.236 1.00 29.62 C ATOM 79 CZ TYR A 24 69.686 2.859 −10.024 1.00 30.70 C ATOM 80 OH TYR A 24 69.181 3.748 −10.957 1.00 31.61 O ATOM 81 N CYS A 25 74.236 1.510 −8.020 1.00 31.62 N ATOM 82 CA CYS A 25 74.975 2.767 −8.097 1.00 32.94 C ATOM 83 C CYS A 25 74.147 3.842 −8.798 1.00 33.32 C ATOM 84 O CYS A 25 73.684 3.650 −9.921 1.00 33.93 O ATOM 85 CB CYS A 25 76.311 2.581 −8.836 1.00 32.09 C ATOM 86 SG CYS A 25 77.380 4.066 −8.811 1.00 34.82 S ATOM 87 N LYS A 26 73.963 4.970 −8.122 1.00 34.61 N ATOM 88 CA LYS A 26 73.189 6.072 −8.676 1.00 36.27 C ATOM 89 C LYS A 26 73.786 6.512 −10.018 1.00 37.44 C ATOM 90 O LYS A 26 73.061 6.928 −10.923 1.00 37.35 O ATOM 91 CB LYS A 26 73.171 7.248 −7.697 1.00 36.24 C ATOM 92 CG LYS A 26 72.293 8.403 −8.145 1.00 38.36 C ATOM 93 CD LYS A 26 72.480 9.630 −7.270 1.00 39.80 C ATOM 94 CE LYS A 26 71.585 10.769 −7.747 1.00 41.47 C ATOM 95 NZ LYS A 26 71.853 12.023 −6.987 1.00 42.04 N ATOM 96 N ASN A 27 75.107 6.406 −10.148 1.00 37.91 N ATOM 97 CA ASN A 27 75.782 6.790 −11.386 1.00 38.44 C ATOM 98 C ASN A 27 75.509 5.753 −12.479 1.00 38.53 C ATOM 99 O ASN A 27 76.092 4.663 −12.479 1.00 38.51 O ATOM 100 CB ASN A 27 77.287 6.904 −11.152 1.00 40.85 C ATOM 101 CG ASN A 27 78.001 7.640 −12.276 1.00 44.71 C ATOM 102 OD1 ASN A 27 79.237 7.582 −12.395 1.00 44.59 O ATOM 103 ND2 ASN A 27 77.230 8.350 −13.101 1.00 44.65 N ATOM 104 N GLY A 28 74.606 6.081 −13.397 1.00 37.85 N ATOM 105 CA GLY A 28 74.285 5.170 −14.481 1.00 37.25 C ATOM 106 C GLY A 28 73.303 4.054 −14.159 1.00 37.29 C ATOM 107 O GLY A 28 72.750 3.427 −15.065 1.00 37.26 O ATOM 108 N GLY A 29 73.089 3.779 −12.878 1.00 37.91 N ATOM 109 CA GLY A 29 72.153 2.730 −12.512 1.00 38.15 C ATOM 110 C GLY A 29 72.674 1.313 −12.685 1.00 38.39 C ATOM 111 O GLY A 29 71.937 0.423 −13.114 1.00 37.89 O ATOM 112 N PHE A 30 73.946 1.100 −12.353 1.00 39.32 N ATOM 113 CA PHE A 30 74.562 −0.225 −12.458 1.00 39.93 C ATOM 114 C PHE A 30 74.609 −0.919 −11.102 1.00 39.45 C ATOM 115 O PHE A 30 74.773 −0.275 −10.070 1.00 40.04 O ATOM 116 CB PHE A 30 76.002 −0.123 −12.971 1.00 40.37 C ATOM 117 CG PHE A 30 76.124 0.432 −14.354 1.00 41.36 C ATOM 118 CD1 PHE A 30 76.436 1.774 −14.554 1.00 40.94 C ATOM 119 CD2 PHE A 30 75.941 −0.393 −15.465 1.00 41.73 C ATOM 120 CE1 PHE A 30 76.568 2.291 −15.841 1.00 41.63 C ATOM 121 CE2 PHE A 30 76.070 0.111 −16.760 1.00 41.47 C ATOM 122 CZ PHE A 30 76.384 1.457 −16.950 1.00 41.25 C ATOM 123 N PHE A 31 74.473 −2.236 −11.113 1.00 39.36 N ATOM 124 CA PHE A 31 74.540 −3.020 −9.893 1.00 38.71 C ATOM 125 C PHE A 31 75.980 −3.498 −9.744 1.00 39.23 C ATOM 126 O PHE A 31 76.546 −4.047 −10.688 1.00 39.27 O ATOM 127 CB PHE A 31 73.599 −4.204 −10.006 1.00 38.16 C ATOM 128 CG PHE A 31 72.164 −3.837 −9.855 1.00 37.93 C ATOM 129 CD1 PHE A 31 71.654 −3.494 −8.605 1.00 36.22 C ATOM 130 CD2 PHE A 31 71.315 −3.821 −10.958 1.00 38.03 C ATOM 131 CE1 PHE A 31 70.317 −3.143 −8.454 1.00 36.77 C ATOM 132 CE2 PHE A 31 69.965 −3.467 −10.815 1.00 38.19 C ATOM 133 CZ PHE A 31 69.469 −3.128 −9.557 1.00 36.80 C ATOM 134 N LEU A 32 76.580 −3.279 −8.575 1.00 39.11 N ATOM 135 CA LEU A 32 77.959 −3.707 −8.352 1.00 39.72 C ATOM 136 C LEU A 32 78.047 −5.205 −8.596 1.00 40.18 C ATOM 137 O LEU A 32 77.254 −5.972 −8.048 1.00 40.08 O ATOM 138 CB LEU A 32 78.403 −3.395 −6.922 1.00 40.02 C ATOM 139 CG LEU A 32 79.896 −3.576 −6.645 1.00 39.28 C ATOM 140 CD1 LEU A 32 80.700 −2.659 −7.556 1.00 39.53 C ATOM 141 CD2 LEU A 32 80.194 −3.263 −5.187 1.00 39.11 C ATOM 142 N ARG A 33 79.006 −5.621 −9.420 1.00 41.12 N ATOM 143 CA ARG A 33 79.162 −7.038 −9.751 1.00 41.65 C ATOM 144 C ARG A 33 80.543 −7.605 −9.427 1.00 41.77 C ATOM 145 O ARG A 33 81.568 −6.987 −9.720 1.00 41.35 O ATOM 146 CB ARG A 33 78.851 −7.253 −11.236 1.00 41.70 C ATOM 147 CG ARG A 33 79.046 −8.686 −11.700 1.00 42.74 C ATOM 148 CD ARG A 33 78.491 −8.922 −13.089 1.00 41.98 C ATOM 149 NE ARG A 33 79.193 −8.155 −14.113 1.00 43.07 N ATOM 150 CZ ARG A 33 78.905 −8.208 −15.413 1.00 43.19 C ATOM 151 NH1 ARG A 33 77.927 −8.996 −15.848 1.00 42.00 N ATOM 152 NH2 ARG A 33 79.590 −7.469 −16.279 1.00 42.32 N ATOM 153 N ILE A 34 80.561 −8.785 −8.813 1.00 42.97 N ATOM 154 CA ILE A 34 81.820 −9.442 −8.465 1.00 44.25 C ATOM 155 C ILE A 34 81.917 −10.784 −9.186 1.00 45.31 C ATOM 156 O ILE A 34 81.232 −11.743 −8.837 1.00 45.06 O ATOM 157 CB ILE A 34 81.957 −9.626 −6.933 1.00 44.16 C ATOM 158 CG1 ILE A 34 82.190 −8.253 −6.285 1.00 43.89 C ATOM 159 CG2 ILE A 34 83.115 −10.575 −6.604 1.00 43.90 C ATOM 160 CD1 ILE A 34 82.527 −8.297 −4.818 1.00 43.24 C ATOM 161 N HIS A 35 82.766 −10.819 −10.213 1.00 47.73 N ATOM 162 CA HIS A 35 82.984 −12.008 −11.044 1.00 49.67 C ATOM 163 C HIS A 35 83.746 −13.118 −10.335 1.00 50.49 C ATOM 164 O HIS A 35 84.558 −12.859 −9.442 1.00 50.08 O ATOM 165 CB HIS A 35 83.761 −11.638 −12.307 1.00 50.99 C ATOM 166 CG HIS A 35 83.016 −10.736 −13.239 1.00 52.80 C ATOM 167 ND1 HIS A 35 81.950 −11.167 −13.998 1.00 53.66 N ATOM 168 CD2 HIS A 35 83.200 −9.432 −13.551 1.00 53.29 C ATOM 169 CE1 HIS A 35 81.511 −10.167 −14.741 1.00 54.14 C ATOM 170 NE2 HIS A 35 82.252 −9.102 −14.488 1.00 54.32 N ATOM 171 N PRO A 36 83.510 −14.376 −10.748 1.00 51.42 N ATOM 172 CA PRO A 36 84.171 −15.543 −10.158 1.00 51.76 C ATOM 173 C PRO A 36 85.698 −15.454 −10.187 1.00 52.11 C ATOM 174 O PRO A 36 86.365 −15.951 −9.281 1.00 52.27 O ATOM 175 CB PRO A 36 83.632 −16.700 −10.998 1.00 52.08 C ATOM 176 CG PRO A 36 82.239 −16.235 −11.327 1.00 52.48 C ATOM 177 CD PRO A 36 82.487 −14.795 −11.725 1.00 51.66 C ATOM 178 N ASP A 37 86.246 −14.813 −11.217 1.00 52.61 N ATOM 179 CA ASP A 37 87.696 −14.685 −11.328 1.00 52.96 C ATOM 180 C ASP A 37 88.259 −13.462 −10.616 1.00 52.62 C ATOM 181 O ASP A 37 89.444 −13.154 −10.746 1.00 53.00 O ATOM 182 CB ASP A 37 88.141 −14.688 −12.803 1.00 54.40 C ATOM 183 CG ASP A 37 87.511 −13.570 −13.620 1.00 55.76 C ATOM 184 OD1 ASP A 37 86.310 −13.676 −13.962 1.00 55.75 O ATOM 185 OD2 ASP A 37 88.226 −12.584 −13.917 1.00 56.34 O ATOM 186 N GLY A 38 87.410 −12.761 −9.868 1.00 52.10 N ATOM 187 CA GLY A 38 87.874 −11.601 −9.126 1.00 50.89 C ATOM 188 C GLY A 38 87.793 −10.223 −9.766 1.00 50.43 C ATOM 189 O GLY A 38 88.254 −9.248 −9.168 1.00 51.26 O ATOM 190 N ARG A 39 87.222 −10.115 −10.960 1.00 49.14 N ATOM 191 CA ARG A 39 87.106 −8.811 −11.615 1.00 48.54 C ATOM 192 C ARG A 39 85.884 −8.066 −11.060 1.00 47.80 C ATOM 193 O ARG A 39 84.876 −8.689 −10.717 1.00 47.58 O ATOM 194 CB ARG A 39 86.973 −8.991 −13.135 1.00 47.72 C ATOM 195 N VAL A 40 85.975 −6.740 −10.976 1.00 46.88 N ATOM 196 CA VAL A 40 84.872 −5.940 −10.455 1.00 46.37 C ATOM 197 C VAL A 40 84.383 −4.864 −11.421 1.00 45.86 C ATOM 198 O VAL A 40 85.169 −4.049 −11.909 1.00 45.70 O ATOM 199 CB VAL A 40 85.268 −5.258 −9.127 1.00 46.76 C ATOM 200 CG1 VAL A 40 84.140 −4.323 −8.648 1.00 46.23 C ATOM 201 CG2 VAL A 40 85.559 −6.324 −8.075 1.00 46.01 C ATOM 202 N ASP A 41 83.079 −4.872 −11.689 1.00 45.56 N ATOM 203 CA ASP A 41 82.458 −3.885 −12.570 1.00 45.56 C ATOM 204 C ASP A 41 80.972 −3.757 −12.231 1.00 45.60 C ATOM 205 O ASP A 41 80.517 −4.264 −11.201 1.00 45.05 O ATOM 206 CB ASP A 41 82.627 −4.287 −14.039 1.00 45.40 C ATOM 207 CG ASP A 41 81.851 −5.543 −14.399 1.00 45.94 C ATOM 208 OD1 ASP A 41 81.894 −5.949 −15.584 1.00 47.24 O ATOM 209 OD2 ASP A 41 81.201 −6.129 −13.507 1.00 46.40 O ATOM 210 N GLY A 42 80.226 −3.082 −13.103 1.00 45.52 N ATOM 211 CA GLY A 42 78.803 −2.902 −12.885 1.00 45.62 C ATOM 212 C GLY A 42 77.992 −3.371 −14.076 1.00 46.37 C ATOM 213 O GLY A 42 78.498 −3.432 −15.194 1.00 46.33 O ATOM 214 N VAL A 43 76.736 −3.725 −13.831 1.00 47.09 N ATOM 215 CA VAL A 43 75.833 −4.176 −14.883 1.00 47.46 C ATOM 216 C VAL A 43 74.413 −3.793 −14.527 1.00 47.90 C ATOM 217 O VAL A 43 74.084 −3.654 −13.351 1.00 48.34 O ATOM 218 CB VAL A 43 75.876 −5.698 −15.085 1.00 47.31 C ATOM 219 CG1 VAL A 43 77.025 −6.052 −15.978 1.00 48.06 C ATOM 220 CG2 VAL A 43 75.988 −6.404 −13.754 1.00 46.61 C ATOM 221 N ARG A 44 73.573 −3.634 −15.542 1.00 48.06 N ATOM 222 CA ARG A 44 72.192 −3.243 −15.319 1.00 48.74 C ATOM 223 C ARG A 44 71.206 −4.396 −15.200 1.00 49.88 C ATOM 224 O ARG A 44 70.122 −4.220 −14.648 1.00 50.17 O ATOM 225 CB ARG A 44 71.749 −2.268 −16.412 1.00 47.88 C ATOM 226 CG ARG A 44 72.389 −0.900 −16.258 1.00 47.04 C ATOM 227 CD ARG A 44 72.229 −0.029 −17.481 1.00 45.80 C ATOM 228 NE ARG A 44 72.842 1.279 −17.268 1.00 45.57 N ATOM 229 CZ ARG A 44 73.279 2.064 −18.245 1.00 45.12 C ATOM 230 NH1 ARG A 44 73.173 1.665 −19.506 1.00 45.80 N ATOM 231 NH2 ARG A 44 73.824 3.242 −17.966 1.00 43.95 N ATOM 232 N GLU A 45 71.578 −5.576 −15.687 1.00 50.58 N ATOM 233 CA GLU A 45 70.686 −6.731 −15.619 1.00 52.24 C ATOM 234 C GLU A 45 70.476 −7.247 −14.192 1.00 53.19 C ATOM 235 O GLU A 45 71.344 −7.911 −13.617 1.00 53.26 O ATOM 236 CB GLU A 45 71.215 −7.865 −16.505 1.00 52.83 C ATOM 237 N LYS A 46 69.306 −6.947 −13.634 1.00 53.61 N ATOM 238 CA LYS A 46 68.965 −7.367 −12.283 1.00 53.94 C ATOM 239 C LYS A 46 69.011 −8.886 −12.097 1.00 53.99 C ATOM 240 O LYS A 46 68.992 −9.379 −10.969 1.00 54.53 O ATOM 241 CB LYS A 46 67.571 −6.842 −11.918 1.00 53.70 C ATOM 242 N SER A 47 69.091 −9.625 −13.198 1.00 53.70 N ATOM 243 CA SER A 47 69.110 −11.086 −13.132 1.00 53.88 C ATOM 244 C SER A 47 70.499 −11.699 −12.976 1.00 53.81 C ATOM 245 O SER A 47 70.630 −12.877 −12.648 1.00 54.39 O ATOM 246 CB SER A 47 68.437 −11.674 −14.379 1.00 53.87 C ATOM 247 N ASP A 48 71.537 −10.904 −13.209 1.00 53.60 N ATOM 248 CA ASP A 48 72.902 −11.401 −13.100 1.00 53.26 C ATOM 249 C ASP A 48 73.153 −12.030 −11.729 1.00 52.56 C ATOM 250 O ASP A 48 72.925 −11.403 −10.694 1.00 52.29 O ATOM 251 CB ASP A 48 73.895 −10.259 −13.363 1.00 54.16 C ATOM 252 CG ASP A 48 75.329 −10.746 −13.472 1.00 55.48 C ATOM 253 OD1 ASP A 48 76.155 −10.039 −14.093 1.00 56.03 O ATOM 254 OD2 ASP A 48 75.633 −11.831 −12.931 1.00 56.13 O ATOM 255 N PRO A 49 73.626 −13.289 −11.709 1.00 52.00 N ATOM 256 CA PRO A 49 73.908 −14.015 −10.466 1.00 50.81 C ATOM 257 C PRO A 49 75.125 −13.514 −9.687 1.00 49.76 C ATOM 258 O PRO A 49 75.337 −13.915 −8.545 1.00 49.74 O ATOM 259 CB PRO A 49 74.083 −15.450 −10.948 1.00 51.73 C ATOM 260 CG PRO A 49 74.740 −15.249 −12.294 1.00 51.98 C ATOM 261 CD PRO A 49 73.903 −14.136 −12.885 1.00 52.08 C ATOM 262 N HIS A 50 75.913 −12.630 −10.288 1.00 48.41 N ATOM 263 CA HIS A 50 77.100 −12.118 −9.611 1.00 47.20 C ATOM 264 C HIS A 50 77.963 −10.738 −8.956 1.00 45.56 C ATOM 265 O HIS A 50 77.965 −10.094 −8.645 1.00 44.52 O ATOM 266 CB HIS A 50 78.280 −12.116 −10.578 1.00 48.84 C ATOM 267 CG HIS A 50 78.506 −13.439 −11.238 1.00 50.65 C ATOM 268 ND1 HIS A 50 78.526 −14.625 −10.535 1.00 51.45 N ATOM 269 CD2 HIS A 50 78.703 −13.765 −12.536 1.00 50.93 C ATOM 270 CE1 HIS A 50 78.725 −15.626 −11.374 1.00 51.59 C ATOM 271 NE2 HIS A 50 78.834 −15.131 −12.594 1.00 51.88 N ATOM 272 N ILE A 51 75.729 −10.286 −8.751 1.00 44.07 N ATOM 273 CA ILE A 51 75.506 −9.003 −8.095 1.00 42.96 C ATOM 274 C ILE A 51 74.869 −9.212 −6.724 1.00 42.25 C ATOM 275 O ILE A 51 74.588 −8.247 −6.005 1.00 41.38 O ATOM 276 CB ILE A 51 74.623 −8.063 −8.938 1.00 42.32 C ATOM 277 CG1 ILE A 51 73.259 −8.700 −9.187 1.00 42.29 C ATOM 278 CG2 ILE A 51 75.324 −7.743 −10.243 1.00 42.67 C ATOM 279 CD1 ILE A 51 72.237 −7.734 −9.762 1.00 43.48 C ATOM 280 N LYS A 52 74.636 −10.475 −6.370 1.00 41.29 N ATOM 281 CA LYS A 52 74.070 −10.805 −5.068 1.00 40.84 C ATOM 282 C LYS A 52 75.232 −10.757 −4.078 1.00 39.49 C ATOM 283 O LYS A 52 76.151 −11.580 −4.143 1.00 39.35 O ATOM 284 CB LYS A 52 73.442 −12.196 −5.099 1.00 42.75 C ATOM 285 CG LYS A 52 72.764 −12.568 −3.808 1.00 45.60 C ATOM 286 CD LYS A 52 72.076 −13.923 −3.898 1.00 47.67 C ATOM 287 CE LYS A 52 71.517 −14.326 −2.541 1.00 49.65 C ATOM 288 NZ LYS A 52 70.843 −15.651 −2.558 1.00 51.56 N ATOM 289 N LEU A 53 75.198 −9.776 −3.180 1.00 36.84 N ATOM 290 CA LEU A 53 76.270 −9.589 −2.213 1.00 34.80 C ATOM 291 C LEU A 53 75.875 −9.831 −0.765 1.00 34.19 C ATOM 292 O LEU A 53 74.700 −9.783 −0.406 1.00 35.12 O ATOM 293 CB LEU A 53 76.820 −8.178 −2.348 1.00 34.31 C ATOM 294 CG LEU A 53 77.297 −7.809 −3.744 1.00 33.98 C ATOM 295 CD1 LEU A 53 77.548 −6.324 −3.823 1.00 33.55 C ATOM 296 CD2 LEU A 53 78.561 −8.590 −4.056 1.00 34.91 C ATOM 297 N GLN A 54 76.875 −10.085 0.069 1.00 32.74 N ATOM 298 CA GLN A 54 76.642 −10.326 1.487 1.00 32.06 C ATOM 299 C GLN A 54 77.473 −9.353 2.305 1.00 31.38 C ATOM 300 O GLN A 54 78.703 −9.459 2.315 1.00 30.82 O ATOM 301 CB GLN A 54 77.062 −11.748 1.869 1.00 32.52 C ATOM 302 CG GLN A 54 76.733 −12.126 3.307 1.00 32.29 C ATOM 303 CD GLN A 54 75.241 −12.187 3.551 1.00 34.18 C ATOM 304 OE1 GLN A 54 74.533 −13.005 2.954 1.00 34.26 O ATOM 305 NE2 GLN A 54 74.748 −11.316 4.424 1.00 33.63 N ATOM 306 N LEU A 55 76.822 −8.410 2.985 1.00 30.29 N ATOM 307 CA LEU A 55 77.561 −7.456 3.816 1.00 30.86 C ATOM 308 C LEU A 55 77.673 −8.028 5.233 1.00 30.05 C ATOM 309 O LEU A 55 76.807 −8.780 5.679 1.00 29.32 O ATOM 310 CB LEU A 55 76.862 −6.086 3.852 1.00 31.28 C ATOM 311 CG LEU A 55 76.483 −5.369 2.537 1.00 33.52 C ATOM 312 CD1 LEU A 55 76.469 −3.868 2.778 1.00 32.75 C ATOM 313 CD2 LEU A 55 77.478 −5.687 1.427 1.00 33.68 C ATOM 314 N GLN A 56 78.746 −7.682 5.930 1.00 28.63 N ATOM 315 CA GLN A 56 78.962 −8.173 7.282 1.00 28.77 C ATOM 316 C GLN A 56 79.827 −7.164 8.016 1.00 29.04 C ATOM 317 O GLN A 56 80.889 −6.790 7.522 1.00 28.60 O ATOM 318 CB GLN A 56 79.658 −9.545 7.229 1.00 28.70 C ATOM 319 CG GLN A 56 80.009 −10.173 8.586 1.00 29.29 C ATOM 320 CD GLN A 56 78.798 −10.400 9.469 1.00 28.66 C ATOM 321 OE1 GLN A 56 77.906 −11.192 9.143 1.00 29.16 O ATOM 322 NE2 GLN A 56 78.754 −9.695 10.597 1.00 29.84 N ATOM 323 N ALA A 57 79.362 −6.714 9.178 1.00 29.57 N ATOM 324 CA ALA A 57 80.104 −5.744 9.977 1.00 30.66 C ATOM 325 C ALA A 57 81.261 −6.418 10.721 1.00 31.59 C ATOM 326 O ALA A 57 81.094 −7.491 11.295 1.00 31.05 O ATOM 327 CB ALA A 57 79.162 −5.072 10.977 1.00 30.28 C ATOM 328 N GLU A 58 82.430 −5.783 10.708 1.00 32.12 N ATOM 329 CA GLU A 58 83.595 −6.330 11.391 1.00 33.18 C ATOM 330 C GLU A 58 83.752 −5.580 12.713 1.00 33.89 C ATOM 331 O GLU A 58 84.270 −6.119 13.695 1.00 33.53 O ATOM 332 CB GLU A 58 84.845 −6.173 10.515 1.00 34.27 C ATOM 333 CG GLU A 58 85.985 −7.131 10.859 1.00 35.60 C ATOM 334 CD GLU A 58 85.594 −8.601 10.725 1.00 37.03 C ATOM 335 OE1 GLU A 58 84.964 −8.980 9.715 1.00 37.39 O ATOM 336 OE2 GLU A 58 85.926 −9.387 11.635 1.00 39.38 O ATOM 337 N GLU A 59 83.309 −4.325 12.710 1.00 34.07 N ATOM 338 CA GLU A 59 83.308 −3.467 13.891 1.00 34.95 C ATOM 339 C GLU A 59 82.302 −2.353 13.593 1.00 33.54 C ATOM 340 O GLU A 59 81.825 −2.236 12.465 1.00 33.43 O ATOM 341 CB GLU A 59 84.707 −2.904 14.195 1.00 36.91 C ATOM 342 CG GLU A 59 85.182 −1.759 13.322 1.00 40.94 C ATOM 343 CD GLU A 59 86.539 −1.224 13.774 1.00 43.27 C ATOM 344 OE1 GLU A 59 87.532 −1.977 13.689 1.00 45.02 O ATOM 345 OE2 GLU A 59 86.615 −0.058 14.225 1.00 44.36 O ATOM 346 N ARG A 60 81.969 −1.550 14.593 1.00 32.58 N ATOM 347 CA ARG A 60 80.991 −0.486 14.413 1.00 32.17 C ATOM 348 C ARG A 60 81.227 0.369 13.154 1.00 31.15 C ATOM 349 O ARG A 60 82.287 0.978 12.988 1.00 30.43 O ATOM 350 CB ARG A 60 80.981 0.381 15.676 1.00 33.58 C ATOM 351 CG ARG A 60 79.844 1.365 15.781 1.00 36.07 C ATOM 352 CD ARG A 60 79.939 2.142 17.087 1.00 38.02 C ATOM 353 NE ARG A 60 79.379 3.472 16.921 1.00 42.32 N ATOM 354 CZ ARG A 60 80.065 4.601 17.059 1.00 44.12 C ATOM 355 NH1 ARG A 60 81.351 4.574 17.384 1.00 44.60 N ATOM 356 NH2 ARG A 60 79.466 5.761 16.829 1.00 46.46 N ATOM 357 N GLY A 61 80.245 0.383 12.253 1.00 29.90 N ATOM 358 CA GLY A 61 80.356 1.185 11.043 1.00 28.83 C ATOM 359 C GLY A 61 81.330 0.720 9.972 1.00 28.80 C ATOM 360 O GLY A 61 81.550 1.430 8.986 1.00 28.16 O ATOM 361 N VAL A 62 81.913 −0.467 10.148 1.00 28.29 N ATOM 362 CA VAL A 62 82.861 −1.000 9.171 1.00 27.10 C ATOM 363 C VAL A 62 82.384 −2.354 8.646 1.00 26.34 C ATOM 364 O VAL A 62 82.059 −3.248 9.422 1.00 25.88 O ATOM 365 CB VAL A 62 84.265 −1.161 9.799 1.00 28.53 C ATOM 366 CG1 VAL A 62 85.279 −1.603 8.723 1.00 29.17 C ATOM 367 CG2 VAL A 62 84.702 0.152 10.450 1.00 28.29 C ATOM 368 N VAL A 63 82.343 −2.517 7.328 1.00 25.99 N ATOM 369 CA VAL A 63 81.878 −3.781 6.762 1.00 25.26 C ATOM 370 C VAL A 63 82.788 −4.378 5.695 1.00 26.19 C ATOM 371 O VAL A 63 83.677 −3.704 5.157 1.00 26.01 O ATOM 372 CB VAL A 63 80.474 −3.634 6.109 1.00 24.65 C ATOM 373 CG1 VAL A 63 79.509 −2.926 7.065 1.00 25.24 C ATOM 374 CG2 VAL A 63 80.587 −2.856 4.794 1.00 22.71 C ATOM 375 N SER A 64 82.552 −5.655 5.405 1.00 26.88 N ATOM 376 CA SER A 64 83.263 −6.358 4.341 1.00 27.68 C ATOM 377 C SER A 64 82.119 −6.687 3.375 1.00 27.92 C ATOM 378 O SER A 64 80.979 −6.878 3.804 1.00 28.11 O ATOM 379 CB SER A 64 83.946 −7.646 4.846 1.00 27.31 C ATOM 380 OG SER A 64 83.020 −8.615 5.315 1.00 27.80 O ATOM 381 N ILE A 65 82.415 −6.712 2.082 1.00 27.99 N ATOM 382 CA ILE A 65 81.410 −6.996 1.068 1.00 29.29 C ATOM 383 C ILE A 65 81.827 −8.241 0.264 1.00 31.00 C ATOM 384 O ILE A 65 82.841 −8.223 −0.439 1.00 29.42 O ATOM 385 CB ILE A 65 81.258 −5.786 0.121 1.00 29.51 C ATOM 386 CG1 ILE A 65 80.756 −4.565 0.908 1.00 30.05 C ATOM 387 CG2 ILE A 65 80.277 −6.117 −0.990 1.00 30.34 C ATOM 388 CD1 ILE A 65 80.874 −3.234 0.160 1.00 30.18 C ATOM 389 N LYS A 66 81.032 −9.306 0.356 1.00 31.83 N ATOM 390 CA LYS A 66 81.353 −10.560 −0.317 1.00 34.62 C ATOM 391 C LYS A 66 80.397 −10.993 −1.434 1.00 35.76 C ATOM 392 O LYS A 66 79.179 −11.031 −1.251 1.00 34.62 O ATOM 393 CB LYS A 66 81.451 −11.681 0.737 1.00 35.88 C ATOM 394 CG LYS A 66 81.735 −13.089 0.193 1.00 36.63 C ATOM 395 CD LYS A 66 81.757 −14.123 1.321 1.00 37.90 C ATOM 396 CE LYS A 66 81.989 −15.544 0.806 1.00 39.28 C ATOM 397 NZ LYS A 66 82.226 −16.531 1.919 1.00 39.38 N ATOM 398 N GLY A 67 80.961 −11.316 −2.597 1.00 37.32 N ATOM 399 CA GLY A 67 80.146 −11.789 −3.707 1.00 39.35 C ATOM 400 C GLY A 67 79.760 −13.231 −3.407 1.00 41.10 C ATOM 401 O GLY A 67 80.625 −14.104 −3.319 1.00 41.10 O ATOM 402 N VAL A 68 78.469 −13.488 −3.233 1.00 42.27 N ATOM 403 CA VAL A 68 78.006 −14.831 −2.908 1.00 44.02 C ATOM 404 C VAL A 68 78.433 −15.881 −3.933 1.00 45.16 C ATOM 405 O VAL A 68 79.007 −16.906 −3.560 1.00 45.69 O ATOM 406 CB VAL A 68 76.465 −14.869 −2.754 1.00 44.56 C ATOM 407 CG1 VAL A 68 76.006 −16.280 −2.426 1.00 44.70 C ATOM 408 CG2 VAL A 68 76.032 −13.921 −1.639 1.00 45.21 C ATOM 409 N SER A 69 78.164 −15.631 −5.214 1.00 45.89 N ATOM 410 CA SER A 69 78.533 −16.582 −6.270 1.00 46.52 C ATOM 411 C SER A 69 80.036 −16.769 −6.398 1.00 46.52 C ATOM 412 O SER A 69 80.538 −17.889 −6.308 1.00 46.68 O ATOM 413 CB SER A 69 77.974 −16.146 −7.630 1.00 47.12 C ATOM 414 OG SER A 69 76.629 −16.568 −7.798 1.00 47.66 O ATOM 415 N ALA A 70 80.749 −15.670 −6.609 1.00 46.10 N ATOM 416 CA ALA A 70 82.193 −15.717 −6.762 1.00 46.16 C ATOM 417 C ALA A 70 82.905 −16.199 −5.498 1.00 46.34 C ATOM 418 O ALA A 70 84.060 −16.625 −5.556 1.00 46.73 O ATOM 419 CB ALA A 70 82.710 −14.344 −7.161 1.00 46.03 C ATOM 420 N ASN A 71 82.214 −16.134 −4.362 1.00 46.13 N ATOM 421 CA ASN A 71 82.791 −16.540 −3.080 1.00 46.22 C ATOM 422 C ASN A 71 84.099 −15.780 −2.820 1.00 45.32 C ATOM 423 O ASN A 71 85.074 −16.345 −2.323 1.00 44.86 O ATOM 424 CB ASN A 71 83.025 −18.061 −3.059 1.00 47.52 C ATOM 425 CG ASN A 71 83.496 −18.578 −1.692 1.00 49.37 C ATOM 426 OD1 ASN A 71 82.985 −18.172 −0.639 1.00 49.71 O ATOM 427 ND2 ASN A 71 84.464 −19.494 −1.709 1.00 49.93 N ATOM 428 N ARG A 72 84.100 −14.492 −3.165 1.00 44.62 N ATOM 429 CA ARG A 72 85.259 −13.620 −2.980 1.00 43.24 C ATOM 430 C ARG A 72 84.849 −12.325 −2.265 1.00 43.09 C ATOM 431 O ARG A 72 83.665 −11.965 −2.247 1.00 42.61 O ATOM 432 CB ARG A 72 85.890 −13.286 −4.331 1.00 42.91 C ATOM 433 N TYR A 73 85.836 −11.637 −1.684 1.00 41.68 N ATOM 434 CA TYR A 73 85.616 −10.398 −0.941 1.00 40.49 C ATOM 435 C TYR A 73 86.114 −9.166 −1.696 1.00 40.25 C ATOM 436 O TYR A 73 87.253 −9.145 −2.180 1.00 40.29 O ATOM 437 CB TYR A 73 86.337 −10.447 0.417 1.00 39.59 C ATOM 438 CG TYR A 73 85.871 −11.523 1.371 1.00 39.87 C ATOM 439 CD1 TYR A 73 86.428 −12.813 1.341 1.00 40.03 C ATOM 440 CD2 TYR A 73 84.869 −11.260 2.310 1.00 39.69 C ATOM 441 CE1 TYR A 73 85.988 −13.818 2.228 1.00 39.43 C ATOM 442 CE2 TYR A 73 84.422 −12.252 3.196 1.00 39.45 C ATOM 443 CZ TYR A 73 84.983 −13.528 3.148 1.00 39.35 C ATOM 444 OH TYR A 73 84.513 −14.506 4.000 1.00 38.23 O ATOM 445 N LEU A 74 85.273 −8.137 −1.780 1.00 39.02 N ATOM 446 CA LEU A 74 85.656 −6.899 −2.460 1.00 38.07 C ATOM 447 C LEU A 74 86.859 −6.288 −1.750 1.00 38.59 C ATOM 448 O LEU A 74 86.963 −6.346 −0.524 1.00 38.50 O ATOM 449 CB LEU A 74 84.515 −5.887 −2.435 1.00 36.96 C ATOM 450 CG LEU A 74 84.825 −4.568 −3.149 1.00 37.24 C ATOM 451 CD1 LEU A 74 84.673 −4.774 −4.656 1.00 35.39 C ATOM 452 CD2 LEU A 74 83.870 −3.465 −2.661 1.00 35.55 C ATOM 453 N ALA A 75 87.768 −5.702 −2.521 1.00 39.32 N ATOM 454 CA ALA A 75 88.951 −5.085 −1.942 1.00 40.14 C ATOM 455 C ALA A 75 89.471 −3.946 −2.809 1.00 40.56 C ATOM 456 O ALA A 75 89.246 −3.917 −4.012 1.00 39.49 O ATOM 457 CB ALA A 75 90.038 −6.134 −1.746 1.00 40.67 C ATOM 458 N MET A 76 90.147 −2.996 −2.178 1.00 42.11 N ATOM 459 CA MET A 76 90.722 −1.874 −2.898 1.00 44.44 C ATOM 460 C MET A 76 92.229 −1.900 −2.681 1.00 45.54 C ATOM 461 O MET A 76 92.697 −1.861 −1.541 1.00 45.20 O ATOM 462 CB MET A 76 90.168 −0.547 −2.398 1.00 44.84 C ATOM 463 CG MET A 76 90.637 0.619 −3.253 1.00 46.00 C ATOM 464 SD MET A 76 90.147 2.212 −2.611 1.00 48.70 S ATOM 465 CE MET A 76 88.435 2.315 −3.268 1.00 47.92 C ATOM 466 N LYS A 77 92.975 −1.969 −3.783 1.00 46.80 N ATOM 467 CA LYS A 77 94.435 −2.024 −3.749 1.00 48.49 C ATOM 468 C LYS A 77 95.082 −0.653 −3.525 1.00 49.55 C ATOM 469 O LYS A 77 94.408 0.381 −3.539 1.00 49.41 O ATOM 470 CB LYS A 77 94.964 −2.643 −5.047 1.00 48.04 C ATOM 471 N GLU A 78 96.397 −0.658 −3.323 1.00 50.66 N ATOM 472 CA GLU A 78 97.152 0.568 −3.073 1.00 51.87 C ATOM 473 C GLU A 78 97.065 1.601 −4.200 1.00 52.55 C ATOM 474 O GLU A 78 97.148 2.804 −3.947 1.00 53.06 O ATOM 475 CB GLU A 78 98.625 0.235 −2.798 1.00 51.76 C ATOM 476 N ASP A 79 96.902 1.140 −5.437 1.00 53.11 N ATOM 477 CA ASP A 79 96.815 2.061 −6.569 1.00 54.03 C ATOM 478 C ASP A 79 95.384 2.535 −6.819 1.00 53.96 C ATOM 479 O ASP A 79 95.123 3.263 −7.780 1.00 54.29 O ATOM 480 CB ASP A 79 97.378 1.410 −7.843 1.00 54.74 C ATOM 481 CG ASP A 79 96.600 0.177 −8.265 1.00 56.27 C ATOM 482 OD1 ASP A 79 96.970 −0.438 −9.292 1.00 56.58 O ATOM 483 OD2 ASP A 79 95.622 −0.181 −7.572 1.00 56.94 O ATOM 484 N GLY A 80 94.462 2.116 −5.954 1.00 53.27 N ATOM 485 CA GLY A 80 93.072 2.516 −6.089 1.00 52.72 C ATOM 486 C GLY A 80 92.219 1.628 −6.977 1.00 51.96 C ATOM 487 O GLY A 80 91.103 1.994 −7.330 1.00 52.61 O ATOM 488 N ARG A 81 92.733 0.460 −7.337 1.00 50.93 N ATOM 489 CA ARG A 81 91.991 −0.459 −8.192 1.00 50.23 C ATOM 490 C ARG A 81 91.097 −1.379 7.362 1.00 49.57 C ATOM 491 O ARG A 81 91.411 −1.700 6.216 1.00 48.23 O ATOM 492 CB ARG A 81 92.967 −1.303 −9.023 1.00 50.47 C ATOM 493 N LEU A 82 89.983 −1.807 7.942 1.00 49.42 N ATOM 494 CA LEU A 82 89.078 −2.697 7.228 1.00 49.88 C ATOM 495 C LEU A 82 89.174 −4.124 7.746 1.00 50.11 C ATOM 496 O LEU A 82 89.298 −4.352 8.950 1.00 50.11 O ATOM 497 CB LEU A 82 87.624 −2.217 7.339 1.00 49.49 C ATOM 498 CG LEU A 82 87.231 −0.941 6.587 1.00 49.70 C ATOM 499 CD1 LEU A 82 85.707 −0.868 6.496 1.00 49.71 C ATOM 500 CD2 LEU A 82 87.834 −0.946 5.186 1.00 49.10 C ATOM 501 N LEU A 83 89.111 −5.078 6.822 1.00 50.38 N ATOM 502 CA LEU A 83 89.177 −6.497 7.160 1.00 50.58 C ATOM 503 C LEU A 83 88.544 −7.305 6.020 1.00 49.82 C ATOM 504 O LEU A 83 88.265 −6.758 4.956 1.00 49.94 O ATOM 505 CB LEU A 83 90.642 −6.906 −7.385 1.00 51.17 C ATOM 506 CG LEU A 83 91.614 −6.724 −6.211 1.00 52.27 C ATOM 507 CD1 LEU A 83 91.549 −7.951 −5.307 1.00 52.55 C ATOM 508 CD2 LEU A 83 93.034 −6.537 −6.726 1.00 52.55 C ATOM 509 N ALA A 84 88.307 −8.594 −6.250 1.00 49.65 N ATOM 510 CA ALA A 84 87.704 −9.466 −5.240 1.00 49.61 C ATOM 511 C ALA A 84 88.662 −10.602 −4.857 1.00 49.88 C ATOM 512 O ALA A 84 89.048 −11.414 −5.701 1.00 49.96 O ATOM 513 CB ALA A 84 86.403 −10.038 −5.769 1.00 49.70 C ATOM 514 N SER A 85 89.018 −10.659 −3.576 1.00 49.72 N ATOM 515 CA SER A 85 89.959 −11.646 −3.048 1.00 49.33 C ATOM 516 C SER A 85 89.334 −12.919 −2.471 1.00 49.28 C ATOM 517 O SER A 85 88.257 −12.884 −1.865 1.00 48.71 O ATOM 518 CB SER A 85 90.827 −10.977 −1.973 1.00 49.44 C ATOM 519 OG SER A 85 91.783 −11.875 −1.445 1.00 50.34 O ATOM 520 N LYS A 86 90.031 −14.039 −2.652 1.00 48.86 N ATOM 521 CA LYS A 86 89.572 −15.329 −2.142 1.00 48.51 C ATOM 522 C LYS A 86 89.579 −15.294 −0.619 1.00 47.67 C ATOM 523 O LYS A 86 88.656 −15.787 0.032 1.00 47.20 O ATOM 524 CB LYS A 86 90.488 −16.462 −2.624 1.00 48.89 C ATOM 525 N SER A 87 90.626 −14.710 −0.052 1.00 46.44 N ATOM 526 CA SER A 87 90.717 −14.619 1.392 1.00 46.63 C ATOM 527 C SER A 87 90.715 −13.157 1.845 1.00 46.26 C ATOM 528 O SER A 87 91.195 −12.266 1.142 1.00 46.06 O ATOM 529 CB SER A 87 91.969 −15.349 1.913 1.00 47.09 C ATOM 530 OG SER A 87 93.166 −14.666 1.568 1.00 48.04 O ATOM 531 N VAL A 88 90.169 −12.930 3.035 1.00 45.87 N ATOM 532 CA VAL A 88 90.054 −11.599 3.618 1.00 45.54 C ATOM 533 C VAL A 88 91.377 −10.961 4.026 1.00 45.45 C ATOM 534 O VAL A 88 92.168 −11.576 4.729 1.00 45.96 O ATOM 535 CB VAL A 88 89.149 −11.634 4.872 1.00 45.92 C ATOM 536 CG1 VAL A 88 88.924 −10.222 5.400 1.00 46.37 C ATOM 537 CG2 VAL A 88 87.833 −12.306 4.542 1.00 45.73 C ATOM 538 N THR A 89 91.609 −9.725 3.583 1.00 45.26 N ATOM 539 CA THR A 89 92.818 −8.985 3.949 1.00 45.23 C ATOM 540 C THR A 89 92.389 −7.606 4.453 1.00 44.98 C ATOM 541 O THR A 89 91.206 −7.283 4.445 1.00 44.71 O ATOM 542 CB THR A 89 93.794 −8.799 2.761 1.00 45.77 C ATOM 543 OG1 THR A 89 93.386 −7.683 1.960 1.00 46.09 O ATOM 544 CG2 THR A 89 93.825 −10.059 1.896 1.00 46.51 C ATOM 545 N ASP A 90 93.344 −6.794 4.890 1.00 45.15 N ATOM 546 CA ASP A 90 93.025 −5.472 5.411 1.00 45.66 C ATOM 547 C ASP A 90 92.492 −4.491 4.366 1.00 44.55 C ATOM 548 O ASP A 90 92.098 −3.371 4.701 1.00 44.62 O ATOM 549 CB ASP A 90 94.246 −4.860 6.093 1.00 48.43 C ATOM 550 CG ASP A 90 94.072 −4.755 7.586 1.00 51.37 C ATOM 551 OD1 ASP A 90 92.930 −4.490 8.016 1.00 53.54 O ATOM 552 OD2 ASP A 90 95.067 −4.923 8.331 1.00 53.90 O ATOM 553 N GLU A 91 92.494 −4.906 3.106 1.00 42.88 N ATOM 554 CA GLU A 91 92.010 −4.063 2.020 1.00 41.63 C ATOM 555 C GLU A 91 90.560 −4.426 1.685 1.00 40.40 C ATOM 556 O GLU A 91 90.006 −3.965 0.686 1.00 39.79 O ATOM 557 CB GLU A 91 92.896 −4.256 0.778 1.00 40.78 C ATOM 558 N CYS A 92 89.948 −5.248 2.531 1.00 39.24 N ATOM 559 CA CYS A 92 88.581 −5.693 2.298 1.00 38.89 C ATOM 560 C CYS A 92 87.542 −5.075 3.240 1.00 37.51 C ATOM 561 O CYS A 92 86.391 −5.508 3.256 1.00 37.21 O ATOM 562 CB CYS A 92 88.532 −7.224 2.377 1.00 38.66 C ATOM 563 SG CYS A 92 89.608 −8.074 1.156 1.00 40.15 S ATOM 564 N PHE A 93 87.948 −4.065 4.007 1.00 36.12 N ATOM 565 CA PHE A 93 87.052 −3.400 4.953 1.00 36.26 C ATOM 566 C PHE A 93 86.765 −1.931 4.603 1.00 35.98 C ATOM 567 O PHE A 93 87.683 −1.162 4.292 1.00 35.24 O ATOM 568 CB PHE A 93 87.622 −3.514 6.366 1.00 36.32 C ATOM 569 CG PHE A 93 87.740 −4.929 6.837 1.00 37.73 C ATOM 570 CD1 PHE A 93 86.599 −5.710 7.001 1.00 36.77 C ATOM 571 CD2 PHE A 93 88.994 −5.510 7.040 1.00 37.62 C ATOM 572 CE1 PHE A 93 86.694 −7.053 7.354 1.00 38.45 C ATOM 573 CE2 PHE A 93 89.104 −6.855 7.394 1.00 38.74 C ATOM 574 CZ PHE A 93 87.954 −7.630 7.551 1.00 38.47 C ATOM 575 N PHE A 94 85.486 −1.552 4.682 1.00 34.88 N ATOM 576 CA PHE A 94 85.050 −0.204 4.329 1.00 33.78 C ATOM 577 C PHE A 94 84.087 0.448 5.320 1.00 33.14 C ATOM 578 O PHE A 94 83.169 −0.196 5.834 1.00 33.33 O ATOM 579 CB PHE A 94 84.357 −0.238 2.969 1.00 34.11 C ATOM 580 CG PHE A 94 85.166 −0.885 1.889 1.00 34.92 C ATOM 581 CD1 PHE A 94 86.025 −0.130 1.101 1.00 33.99 C ATOM 582 CD2 PHE A 94 85.074 −2.261 1.664 1.00 35.17 C ATOM 583 CE1 PHE A 94 86.785 −0.733 0.097 1.00 34.50 C ATOM 584 CE2 PHE A 94 85.833 −2.874 0.662 1.00 35.02 C ATOM 585 CZ PHE A 94 86.692 −2.106 −0.123 1.00 33.91 C ATOM 586 N PHE A 95 84.294 1.732 5.575 1.00 31.91 N ATOM 587 CA PHE A 95 83.402 2.477 6.457 1.00 31.86 C ATOM 588 C PHE A 95 82.091 2.646 5.695 1.00 29.92 C ATOM 589 O PHE A 95 82.086 3.158 4.579 1.00 28.74 O ATOM 590 CB PHE A 95 83.964 3.875 6.771 1.00 32.18 C ATOM 591 CG PHE A 95 85.103 3.880 7.751 1.00 34.26 C ATOM 592 CD1 PHE A 95 86.421 3.966 7.315 1.00 34.86 C ATOM 593 CD2 PHE A 95 84.856 3.838 9.117 1.00 34.93 C ATOM 594 CE1 PHE A 95 87.475 4.019 8.232 1.00 35.24 C ATOM 595 CE2 PHE A 95 85.907 3.887 10.037 1.00 36.08 C ATOM 596 CZ PHE A 95 87.216 3.980 9.592 1.00 35.03 C ATOM 597 N GLU A 96 80.992 2.193 6.282 1.00 29.95 N ATOM 598 CA GLU A 96 79.684 2.328 5.647 1.00 30.89 C ATOM 599 C GLU A 96 78.984 3.529 6.280 1.00 31.23 C ATOM 600 O GLU A 96 78.910 3.637 7.500 1.00 30.95 O ATOM 601 CB GLU A 96 78.843 1.059 5.855 1.00 29.09 C ATOM 602 CG GLU A 96 77.449 1.150 5.233 1.00 29.15 C ATOM 603 CD GLU A 96 76.613 −0.107 5.441 1.00 29.45 C ATOM 604 OE1 GLU A 96 76.354 −0.451 6.609 1.00 30.47 O ATOM 605 OE2 GLU A 96 76.218 −0.749 4.438 1.00 28.03 O ATOM 606 N ARG A 97 78.476 4.423 5.445 1.00 32.89 N ATOM 607 CA ARG A 97 77.795 5.624 5.931 1.00 35.01 C ATOM 608 C ARG A 97 76.514 5.940 5.156 1.00 35.02 C ATOM 609 O ARG A 97 76.487 5.891 3.928 1.00 34.22 O ATOM 610 CB ARG A 97 78.734 6.833 5.825 1.00 37.51 C ATOM 611 CG ARG A 97 78.022 8.186 5.923 1.00 41.64 C ATOM 612 CD ARG A 97 77.836 8.617 7.366 1.00 44.41 C ATOM 613 NE ARG A 97 79.087 9.126 7.922 1.00 46.59 N ATOM 614 CZ ARG A 97 79.681 10.245 7.513 1.00 48.01 C ATOM 615 NH1 ARG A 97 79.131 10.976 6.544 1.00 48.75 N ATOM 616 NH2 ARG A 97 80.825 10.633 8.068 1.00 47.89 N ATOM 617 N LEU A 98 75.450 6.246 5.887 1.00 35.75 N ATOM 618 CA LEU A 98 74.189 6.641 5.267 1.00 36.00 C ATOM 619 C LEU A 98 74.273 8.168 5.164 1.00 35.58 C ATOM 620 O LEU A 98 74.272 8.855 6.178 1.00 35.92 O ATOM 621 CB LEU A 98 72.999 6.218 6.145 1.00 35.97 C ATOM 622 CG LEU A 98 71.600 6.714 5.726 1.00 36.46 C ATOM 623 CD1 LEU A 98 71.358 6.425 4.249 1.00 35.99 C ATOM 624 CD2 LEU A 98 70.523 6.034 6.583 1.00 36.05 C ATOM 625 N GLU A 99 74.384 8.691 3.948 1.00 36.12 N ATOM 626 CA GLU A 99 74.493 10.132 3.755 1.00 36.63 C ATOM 627 C GLU A 99 73.152 10.840 3.913 1.00 37.62 C ATOM 628 O GLU A 99 72.088 10.206 3.864 1.00 35.83 O ATOM 629 CB GLU A 99 75.081 10.437 2.379 1.00 37.25 C ATOM 630 CG GLU A 99 76.460 9.820 2.153 1.00 38.74 C ATOM 631 CD GLU A 99 77.476 10.222 3.217 1.00 39.43 C ATOM 632 OE1 GLU A 99 78.589 9.666 3.192 1.00 40.37 O ATOM 633 OE2 GLU A 99 77.173 11.088 4.070 1.00 39.18 O ATOM 634 N SER A 100 73.212 12.159 4.099 1.00 38.04 N ATOM 635 CA SER A 100 72.011 12.970 4.281 1.00 38.26 C ATOM 636 C SER A 100 71.055 12.856 3.093 1.00 37.38 C ATOM 637 O SER A 100 69.850 13.072 3.239 1.00 37.46 O ATOM 638 CB SER A 100 72.394 14.438 4.527 1.00 38.36 C ATOM 639 OG SER A 100 73.181 14.952 3.463 1.00 40.12 O ATOM 640 N ASN A 101 71.590 12.506 1.925 1.00 36.22 N ATOM 641 CA ASN A 101 70.767 12.341 0.728 1.00 34.84 C ATOM 642 C ASN A 101 70.080 10.973 0.689 1.00 33.40 C ATOM 643 O ASN A 101 69.352 10.667 −0.254 1.00 33.62 O ATOM 644 CB ASN A 101 71.620 12.516 −0.526 1.00 35.95 C ATOM 645 CG ASN A 101 72.956 11.783 −0.434 1.00 38.04 C ATOM 646 OD1 ASN A 101 73.042 10.666 0.091 1.00 36.23 O ATOM 647 ND2 ASN A 101 74.008 12.412 −0.959 1.00 38.32 N ATOM 648 N ASN A 102 70.320 10.162 1.718 1.00 32.04 N ATOM 649 CA ASN A 102 69.752 8.822 1.844 1.00 31.07 C ATOM 650 C ASN A 102 70.351 7.711 0.971 1.00 30.18 C ATOM 651 O ASN A 102 69.705 6.678 0.750 1.00 27.66 O ATOM 652 CB ASN A 102 68.237 8.844 1.634 1.00 32.35 C ATOM 653 CG ASN A 102 67.487 9.206 2.896 1.00 34.59 C ATOM 654 OD1 ASN A 102 68.012 9.072 4.010 1.00 34.67 O ATOM 655 ND2 ASN A 102 66.246 9.655 2.734 1.00 35.07 N ATOM 656 N TYR A 103 71.564 7.934 0.466 1.00 28.14 N ATOM 657 CA TYR A 103 72.280 6.916 −0.309 1.00 27.47 C ATOM 658 C TYR A 103 73.419 6.488 0.608 1.00 26.83 C ATOM 659 O TYR A 103 73.727 7.195 1.568 1.00 25.26 O ATOM 660 CB TYR A 103 72.874 7.485 −1.600 1.00 27.20 C ATOM 661 CG TYR A 103 71.882 7.684 −2.719 1.00 28.12 C ATOM 662 CD1 TYR A 103 71.564 6.640 −3.586 1.00 27.59 C ATOM 663 CD2 TYR A 103 71.281 8.930 −2.932 1.00 27.54 C ATOM 664 CE1 TYR A 103 70.685 6.830 −4.638 1.00 28.35 C ATOM 665 CE2 TYR A 103 70.395 9.130 −3.981 1.00 28.24 C ATOM 666 CZ TYR A 103 70.101 8.080 −4.828 1.00 28.25 C ATOM 667 OH TYR A 103 69.215 8.265 −5.856 1.00 28.55 O ATOM 668 N ASN A 104 74.032 5.343 0.313 1.00 25.83 N ATOM 669 CA ASN A 104 75.146 4.842 1.112 1.00 25.48 C ATOM 670 C ASN A 104 76.486 5.082 0.417 1.00 24.49 C ATOM 671 O ASN A 104 76.544 5.176 −0.803 1.00 24.92 O ATOM 672 CB ASN A 104 75.006 3.333 1.337 1.00 25.94 C ATOM 673 CG ASN A 104 73.980 2.983 2.400 1.00 27.69 C ATOM 674 OD1 ASN A 104 73.342 3.860 2.998 1.00 25.70 O ATOM 675 ND2 ASN A 104 73.819 1.680 2.646 1.00 26.43 N ATOM 676 N THR A 105 77.555 5.186 1.198 1.00 24.18 N ATOM 677 CA THR A 105 78.901 5.317 0.636 1.00 24.45 C ATOM 678 C THR A 105 79.805 4.316 1.370 1.00 24.99 C ATOM 679 O THR A 105 79.577 3.995 2.542 1.00 23.75 O ATOM 680 GB THR A 105 79.534 6.703 0.838 1.00 23.48 C ATOM 681 OG1 THR A 105 79.479 7.037 2.230 1.00 24.08 O ATOM 682 CG2 THR A 105 78.852 7.752 −0.026 1.00 23.94 C ATOM 683 N TYR A 106 80.828 3.839 0.672 1.00 25.52 N ATOM 684 CA TYR A 106 81.768 2.873 1.222 1.00 27.52 C ATOM 685 C TYR A 106 83.191 3.402 1.052 1.00 29.31 C ATOM 686 O TYR A 106 83.715 3.461 −0.064 1.00 29.05 O ATOM 687 CB TYR A 106 81.577 1.531 0.504 1.00 26.36 C ATOM 688 CG TYR A 106 80.223 0.933 0.807 1.00 24.59 C ATOM 689 CD1 TYR A 106 79.982 0.278 2.024 1.00 23.67 C ATOM 690 CD2 TYR A 106 79.149 1.120 −0.065 1.00 23.83 C ATOM 691 CE1 TYR A 106 78.690 −0.169 2.367 1.00 24.28 C ATOM 692 CE2 TYR A 106 77.852 0.682 0.268 1.00 24.28 C ATOM 693 CZ TYR A 106 77.628 0.044 1.479 1.00 23.75 C ATOM 694 OH TYR A 106 76.338 −0.348 1.807 1.00 23.41 O ATOM 695 N ARG A 107 83.793 3.804 2.167 1.00 31.22 N ATOM 696 CA ARG A 107 85.142 4.369 2.182 1.00 33.44 C ATOM 697 C ARG A 107 86.175 3.400 2.788 1.00 33.71 C ATOM 698 O ARG A 107 85.979 2.870 3.874 1.00 32.90 O ATOM 699 CB ARG A 107 85.110 5.693 2.961 1.00 33.34 C ATOM 700 CG ARG A 107 86.390 6.517 2.919 1.00 33.84 C ATOM 701 CD ARG A 107 86.147 7.883 3.550 1.00 33.44 C ATOM 702 NE ARG A 107 85.639 7.773 4.919 1.00 33.98 N ATOM 703 CZ ARG A 107 86.396 7.548 5.991 1.00 35.38 C ATOM 704 NH1 ARG A 107 87.712 7.415 5.861 1.00 37.25 N ATOM 705 NH2 ARG A 107 85.840 7.418 7.191 1.00 34.53 N ATOM 706 N SER A 108 87.266 3.177 2.060 1.00 36.11 N ATOM 707 CA SER A 108 88.345 2.270 2.475 1.00 37.06 C ATOM 708 C SER A 108 88.890 2.572 3.866 1.00 37.88 C ATOM 709 O SER A 108 89.251 3.713 4.162 1.00 37.86 O ATOM 710 CB SER A 108 89.494 2.342 1.464 1.00 37.14 C ATOM 711 OG SER A 108 90.533 1.433 1.779 1.00 38.83 O ATOM 712 N ARG A 109 88.957 1.555 4.724 1.00 38.90 N ATOM 713 CA ARG A 109 89.485 1.779 6.063 1.00 40.45 C ATOM 714 C ARG A 109 91.011 1.889 6.005 1.00 41.31 C ATOM 715 O ARG A 109 91.630 2.487 6.886 1.00 40.95 O ATOM 716 CB ARG A 109 89.078 0.657 7.020 1.00 40.32 C ATOM 717 CG ARG A 109 89.395 0.986 8.476 1.00 41.68 C ATOM 718 CD ARG A 109 88.858 −0.060 9.446 1.00 42.89 C ATOM 719 NE ARG A 109 89.418 −1.384 9.187 1.00 45.20 N ATOM 720 CZ ARG A 109 89.221 −2.452 9.959 1.00 45.77 C ATOM 721 NH1 ARG A 109 88.471 −2.362 11.049 1.00 46.70 N ATOM 722 NH2 ARG A 109 89.783 −3.615 9.648 1.00 45.83 N ATOM 723 N LYS A 110 91.604 1.319 4.959 1.00 42.40 N ATOM 724 CA LYS A 110 93.061 1.363 4.779 1.00 44.16 C ATOM 725 C LYS A 110 93.474 2.688 4.128 1.00 44.71 C ATOM 726 O LYS A 110 94.231 3.472 4.711 1.00 44.66 O ATOM 727 CB LYS A 110 93.522 0.188 3.908 1.00 43.41 C ATOM 728 N TYR A 111 92.972 2.928 2.918 1.00 44.79 N ATOM 729 CA TYR A 111 93.257 4.159 2.184 1.00 45.33 C ATOM 730 C TYR A 111 92.041 5.041 2.440 1.00 45.58 C ATOM 731 O TYR A 111 91.143 5.160 1.606 1.00 45.68 O ATOM 732 CB TYR A 111 93.417 3.834 0.704 1.00 46.39 C ATOM 733 CG TYR A 111 94.310 2.631 0.495 1.00 48.08 C ATOM 734 CD1 TYR A 111 95.651 2.659 0.881 1.00 48.44 C ATOM 735 CD2 TYR A 111 93.797 1.440 −0.016 1.00 48.53 C ATOM 736 CE1 TYR A 111 96.457 1.528 0.770 1.00 49.53 C ATOM 737 CE2 TYR A 111 94.591 0.303 −0.131 1.00 49.37 C ATOM 738 CZ TYR A 111 95.920 0.351 0.266 1.00 50.10 C ATOM 739 OH TYR A 111 96.695 −0.787 0.186 1.00 50.23 O ATOM 740 N THR A 112 92.037 5.652 3.620 1.00 45.88 N ATOM 741 CA THR A 112 90.937 6.477 4.112 1.00 45.92 C ATOM 742 C THR A 112 90.372 7.631 3.291 1.00 46.09 C ATOM 743 O THR A 112 89.499 8.354 3.783 1.00 46.15 O ATOM 744 CB THR A 112 91.274 7.047 5.485 1.00 45.93 C ATOM 745 OG1 THR A 112 92.262 8.072 5.337 1.00 46.22 O ATOM 746 CG2 THR A 112 91.805 5.952 6.395 1.00 46.03 C ATOM 747 N SER A 113 90.826 7.819 2.059 1.00 45.29 N ATOM 748 CA SER A 113 90.295 8.924 1.270 1.00 44.93 C ATOM 749 C SER A 113 89.594 8.456 0.006 1.00 43.95 C ATOM 750 O SER A 113 88.935 9.245 −0.670 1.00 43.68 O ATOM 751 CB SER A 113 91.417 9.870 0.869 1.00 46.51 C ATOM 752 OG SER A 113 92.182 9.282 −0.168 1.00 48.39 O ATOM 753 N TRP A 114 89.746 7.177 −0.319 1.00 42.46 N ATOM 754 CA TRP A 114 89.140 6.628 −1.521 1.00 41.49 C ATOM 755 C TRP A 114 87.816 5.892 −1.270 1.00 40.48 C ATOM 756 O TRP A 114 87.626 5.255 −0.233 1.00 39.86 O ATOM 757 CB TRP A 114 90.136 5.697 −2.227 1.00 41.54 C ATOM 758 N TYR A 115 86.916 5.986 −2.246 1.00 39.44 N ATOM 759 CA TYR A 115 85.598 5.364 −2.180 1.00 38.58 C ATOM 760 C TYR A 115 85.381 4.306 −3.250 1.00 37.61 C ATOM 761 O TYR A 115 85.971 4.359 −4.324 1.00 38.60 O ATOM 762 CB TYR A 115 84.489 6.413 −2.377 1.00 39.18 C ATOM 763 CG TYR A 115 84.357 7.433 −1.277 1.00 38.67 C ATOM 764 CD1 TYR A 115 85.127 8.597 −1.277 1.00 39.24 C ATOM 765 CD2 TYR A 115 83.477 7.223 −0.221 1.00 38.75 C ATOM 766 CE1 TYR A 115 85.022 9.532 −0.243 1.00 39.67 C ATOM 767 CE2 TYR A 115 83.362 8.143 0.818 1.00 39.61 C ATOM 768 CZ TYR A 115 84.137 9.300 0.804 1.00 40.08 C ATOM 769 OH TYR A 115 84.014 10.209 1.836 1.00 39.83 O ATOM 770 N VAL A 116 84.514 3.349 −2.945 1.00 36.63 N ATOM 771 CA VAL A 116 84.136 2.320 −3.899 1.00 35.26 C ATOM 772 C VAL A 116 83.257 3.123 −4.847 1.00 36.10 C ATOM 773 O VAL A 116 82.389 3.872 −4.394 1.00 36.77 O ATOM 774 CB VAL A 116 83.267 1.221 −3.231 1.00 33.90 C ATOM 775 CG1 VAL A 116 82.773 0.220 −4.281 1.00 31.71 C ATOM 776 CG2 VAL A 116 84.068 0.515 −2.151 1.00 33.37 C ATOM 777 N ALA A 117 83.463 2.980 −6.147 1.00 36.82 N ATOM 778 CA ALA A 117 82.676 3.747 −7.096 1.00 37.68 C ATOM 779 C ALA A 117 82.654 3.144 −8.486 1.00 38.75 C ATOM 780 O ALA A 117 83.542 2.378 −8.866 1.00 38.92 O ATOM 781 CB ALA A 117 83.212 5.180 −7.161 1.00 37.78 C ATOM 782 N LEU A 118 81.621 3.496 −9.242 1.00 39.82 N ATOM 783 CA LEU A 118 81.461 3.014 −10.606 1.00 40.49 C ATOM 784 C LEU A 118 81.371 4.200 −11.551 1.00 41.61 C ATOM 785 O LEU A 118 80.875 5.258 −11.166 1.00 42.32 O ATOM 786 CB LEU A 118 80.200 2.167 −10.723 1.00 40.77 C ATOM 787 CG LEU A 118 80.254 0.818 −10.000 1.00 42.07 C ATOM 788 CD1 LEU A 118 78.951 0.057 −10.239 1.00 41.45 C ATOM 789 CD2 LEU A 118 81.446 0.003 −10.516 1.00 41.56 C ATOM 790 N LYS A 119 81.858 4.022 −12.778 1.00 42.45 N ATOM 791 CA LYS A 119 81.834 5.078 −13.788 1.00 43.49 C ATOM 792 C LYS A 119 80.565 4.962 −14.622 1.00 44.00 C ATOM 793 O LYS A 119 79.932 3.905 −14.655 1.00 44.67 O ATOM 794 CB LYS A 119 83.063 4.968 −14.708 1.00 42.89 C ATOM 795 N ARG A 120 80.203 6.049 −15.299 1.00 44.73 N ATOM 796 CA ARG A 120 79.006 6.076 −16.135 1.00 45.11 C ATOM 797 C ARG A 120 79.049 4.988 −17.199 1.00 45.13 C ATOM 798 O ARG A 120 78.019 4.613 −17.761 1.00 45.32 O ATOM 799 CB ARG A 120 78.860 7.450 −16.802 1.00 44.67 C ATOM 800 N THR A 121 80.243 4.469 −17.455 1.00 46.00 N ATOM 801 CA THR A 121 80.428 3.437 −18.466 1.00 46.87 C ATOM 802 C THR A 121 80.083 2.048 −17.950 1.00 47.24 C ATOM 803 O THR A 121 79.722 1.159 −18.720 1.00 47.43 O ATOM 804 CB THR A 121 81.878 3.422 −18.956 1.00 47.67 C ATOM 805 OG1 THR A 121 82.719 2.880 −17.929 1.00 48.94 O ATOM 806 CG2 THR A 121 82.344 4.848 −19.287 1.00 47.63 C ATOM 807 N GLY A 122 80.194 1.857 −16.643 1.00 48.13 N ATOM 808 CA GLY A 122 79.900 0.554 −16.076 1.00 48.96 C ATOM 809 C GLY A 122 81.164 −0.088 −15.537 1.00 49.43 C ATOM 810 O GLY A 122 81.137 −1.182 −14.966 1.00 49.53 O ATOM 811 N GLN A 123 82.285 0.594 −15.736 1.00 49.50 N ATOM 812 CA GLN A 123 83.561 0.104 −15.246 1.00 49.94 C ATOM 813 C GLN A 123 83.794 0.816 −13.918 1.00 49.63 C ATOM 814 O GLN A 123 83.316 1.933 −13.721 1.00 49.09 O ATOM 815 CB GLN A 123 84.675 0.432 −16.248 1.00 51.19 C ATOM 816 CG GLN A 123 84.625 −0.387 −17.542 1.00 52.46 C ATOM 817 CD GLN A 123 84.983 −1.856 −17.329 1.00 54.02 C ATOM 818 OE1 GLN A 123 86.025 −2.176 −16.742 1.00 54.84 O ATOM 819 NE2 GLN A 123 84.127 −2.755 −17.812 1.00 53.61 N ATOM 820 N TYR A 124 84.508 0.174 −12.998 1.00 49.42 N ATOM 821 CA TYR A 124 84.753 0.804 −11.709 1.00 49.47 C ATOM 822 C TYR A 124 85.580 2.060 −11.910 1.00 48.95 C ATOM 823 O TYR A 124 86.123 2.286 −12.988 1.00 48.14 O ATOM 824 CB TYR A 124 85.463 −0.162 −10.749 1.00 51.35 C ATOM 825 CG TYR A 124 86.908 −0.453 −11.080 1.00 52.93 C ATOM 826 CD1 TYR A 124 87.909 0.477 −10.798 1.00 53.68 C ATOM 827 CD2 TYR A 124 87.278 −1.664 −11.662 1.00 54.20 C ATOM 828 CE1 TYR A 124 89.241 0.211 −11.085 1.00 54.73 C ATOM 829 CE2 TYR A 124 88.612 −1.941 −11.954 1.00 55.22 C ATOM 830 CZ TYR A 124 89.587 −0.998 −11.661 1.00 55.25 C ATOM 831 OH TYR A 124 90.909 −1.263 −11.936 1.00 56.45 O ATOM 832 N LYS A 125 85.667 2.875 −10.865 1.00 48.65 N ATOM 833 CA LYS A 125 86.417 4.120 −10.914 1.00 49.19 C ATOM 834 C LYS A 125 87.553 4.062 −9.898 1.00 49.55 C ATOM 835 O LYS A 125 87.334 3.697 −8.740 1.00 49.81 O ATOM 836 CB LYS A 125 85.483 5.295 −10.598 1.00 49.88 C ATOM 837 CG LYS A 125 86.112 6.672 −10.754 1.00 50.85 C ATOM 838 CD LYS A 125 85.061 7.782 −10.628 1.00 51.23 C ATOM 839 CE LYS A 125 85.663 9.162 −10.862 1.00 51.49 C ATOM 840 NZ LYS A 125 84.656 10.243 −10.685 1.00 51.35 N ATOM 841 N LEU A 126 88.762 4.409 −10.331 1.00 49.75 N ATOM 842 CA LEU A 126 89.926 4.381 −9.455 1.00 50.08 C ATOM 843 C LEU A 126 89.642 5.119 −8.163 1.00 50.74 C ATOM 844 O LEU A 126 89.212 6.271 −8.181 1.00 50.88 O ATOM 845 CB LEU A 126 91.133 5.015 −10.150 1.00 50.72 C ATOM 846 N GLY A 127 89.886 4.452 −7.042 1.00 51.26 N ATOM 847 CA GLY A 127 89.647 5.074 −5.754 1.00 52.31 C ATOM 848 C GLY A 127 90.309 6.432 −5.628 1.00 53.41 C ATOM 849 O GLY A 127 89.778 7.332 −4.977 1.00 53.62 O ATOM 850 N SER A 128 91.469 6.587 −6.258 1.00 54.05 N ATOM 851 CA SER A 128 92.212 7.841 −6.196 1.00 54.57 C ATOM 852 C SER A 128 91.509 9.002 −6.902 1.00 54.32 C ATOM 853 O SER A 128 91.834 10.167 −6.670 1.00 54.14 O ATOM 854 CB SER A 128 93.608 7.634 −6.786 1.00 55.37 C ATOM 855 OG SER A 128 93.545 6.824 −7.945 1.00 57.14 O ATOM 856 N LYS A 129 90.538 8.682 −7.752 1.00 53.92 N ATOM 857 CA LYS A 129 89.801 9.703 −8.489 1.00 53.25 C ATOM 858 C LYS A 129 88.405 9.964 −7.909 1.00 52.55 C ATOM 859 O LYS A 129 87.572 10.605 −8.552 1.00 52.29 O ATOM 860 CB LYS A 129 89.680 9.283 −9.961 1.00 53.64 C ATOM 861 N THR A 130 88.152 9.481 −6.695 1.00 51.39 N ATOM 862 CA THR A 130 86.847 9.674 −6.072 1.00 50.01 C ATOM 863 C THR A 130 86.860 10.805 −5.058 1.00 50.56 C ATOM 864 O THR A 130 87.914 11.188 −4.546 1.00 51.07 O ATOM 865 CB THR A 130 86.351 8.396 −5.361 1.00 48.77 C ATOM 866 OG1 THR A 130 87.193 8.114 −4.237 1.00 46.90 O ATOM 867 CG2 THR A 130 86.357 7.219 −6.315 1.00 46.34 C ATOM 868 N GLY A 131 85.670 11.330 −4.775 1.00 50.61 N ATOM 869 CA GLY A 131 85.526 12.424 −3.830 1.00 50.27 C ATOM 870 C GLY A 131 84.149 12.386 −3.200 1.00 50.50 C ATOM 871 O GLY A 131 83.225 11.829 −3.793 1.00 50.45 O ATOM 872 N PRO A 132 83.973 12.987 −2.011 1.00 50.77 N ATOM 873 CA PRO A 132 82.700 13.018 −1.282 1.00 51.13 C ATOM 874 C PRO A 132 81.453 13.563 −1.979 1.00 51.41 C ATOM 875 O PRO A 132 80.328 13.166 −1.638 1.00 52.28 O ATOM 876 CB PRO A 132 83.048 13.790 −0.008 1.00 51.20 C ATOM 877 CG PRO A 132 84.179 14.648 −0.419 1.00 51.10 C ATOM 878 CD PRO A 132 85.006 13.725 −1.271 1.00 51.01 C ATOM 879 N GLY A 133 81.629 14.445 −2.956 1.00 50.67 N ATOM 880 CA GLY A 133 80.466 14.997 −3.626 1.00 49.53 C ATOM 881 C GLY A 133 80.120 14.351 −4.952 1.00 49.10 C ATOM 882 O GLY A 133 79.163 14.769 −5.608 1.00 49.41 O ATOM 883 N GLN A 134 80.873 13.328 −5.350 1.00 48.03 N ATOM 884 CA GLN A 134 80.631 12.665 −6.634 1.00 46.42 C ATOM 885 C GLN A 134 79.401 11.764 −6.653 1.00 45.21 C ATOM 886 O GLN A 134 78.978 11.236 −5.624 1.00 45.24 O ATOM 887 CB GLN A 134 81.847 11.826 −7.069 1.00 46.96 C ATOM 888 CG GLN A 134 83.204 12.511 −6.966 1.00 47.47 C ATOM 889 CD GLN A 134 84.304 11.760 −7.722 1.00 48.07 C ATOM 890 OE1 GLN A 134 84.137 10.603 −8.111 1.00 47.30 O ATOM 891 NE2 GLN A 134 85.436 12.424 −7.925 1.00 48.32 N ATOM 892 N LYS A 135 78.849 11.586 −7.848 1.00 43.48 N ATOM 893 CA LYS A 135 77.683 10.736 −8.060 1.00 42.04 C ATOM 894 C LYS A 135 78.104 9.262 −8.174 1.00 40.40 C ATOM 895 O LYS A 135 77.295 8.355 −7.952 1.00 39.47 O ATOM 896 CB LYS A 135 76.958 11.165 −9.339 1.00 42.66 C ATOM 897 CG LYS A 135 75.740 10.333 −9.657 1.00 44.25 C ATOM 898 CD LYS A 135 74.998 10.872 −10.872 1.00 46.61 C ATOM 899 CE LYS A 135 73.761 10.029 −11.161 1.00 46.93 C ATOM 900 NZ LYS A 135 72.944 10.547 −12.304 1.00 49.32 N ATOM 901 N ALA A 136 79.373 9.040 −8.512 1.00 38.08 N ATOM 902 CA ALA A 136 79.924 7.695 −8.678 1.00 36.96 C ATOM 903 C ALA A 136 80.080 6.879 −7.381 1.00 34.83 C ATOM 904 O ALA A 136 80.202 5.653 −7.438 1.00 35.66 O ATOM 905 CB ALA A 136 81.275 7.781 −9.407 1.00 36.48 C ATOM 906 N ILE A 137 80.070 7.546 −6.227 1.00 32.81 N ATOM 907 CA ILE A 137 80.218 6.859 −4.945 1.00 31.45 C ATOM 908 C ILE A 137 78.891 6.572 −4.214 1.00 30.17 C ATOM 909 O ILE A 137 78.897 5.983 −3.130 1.00 28.56 O ATOM 910 CB ILE A 137 81.117 7.675 −3.957 1.00 31.54 C ATOM 911 CG1 ILE A 137 80.335 8.871 −3.399 1.00 31.63 C ATOM 912 CG2 ILE A 137 82.378 8.184 −4.671 1.00 32.38 C ATOM 913 CD1 ILE A 137 81.052 9.626 −2.286 1.00 29.61 C ATOM 914 N LEU A 138 77.765 6.983 −4.795 1.00 29.06 N ATOM 915 CA LEU A 138 76.462 6.786 −4.139 1.00 28.39 C ATOM 916 C LEU A 138 75.759 5.489 −4.504 1.00 27.29 C ATOM 917 O LEU A 138 75.437 5.253 −5.667 1.00 26.85 O ATOM 918 CB LEU A 138 75.535 7.969 −4.431 1.00 26.97 C ATOM 919 CG LEU A 138 76.149 9.310 −4.017 1.00 28.21 C ATOM 920 CD1 LEU A 138 75.281 10.467 −4.525 1.00 27.23 C ATOM 921 CD2 LEU A 138 76.293 9.368 −2.497 1.00 27.43 C ATOM 922 N PHE A 139 75.516 4.655 −3.495 1.00 26.91 N ATOM 923 CA PHE A 139 74.851 3.368 −3.706 1.00 26.74 C ATOM 924 C PHE A 139 73.584 3.210 −2.866 1.00 27.02 C ATOM 925 O PHE A 139 73.475 3.730 −1.758 1.00 25.58 O ATOM 926 CB PHE A 139 75.801 2.198 −3.383 1.00 27.16 C ATOM 927 CG PHE A 139 76.989 2.089 −4.311 1.00 27.58 C ATOM 928 CD1 PHE A 139 78.119 2.893 −4.130 1.00 27.23 C ATOM 929 CD2 PHE A 139 76.973 1.179 −5.375 1.00 27.34 C ATOM 930 CE1 PHE A 139 79.228 2.786 −5.007 1.00 27.33 C ATOM 931 CE2 PHE A 139 78.064 1.066 −6.253 1.00 26.45 C ATOM 932 CZ PHE A 139 79.192 1.868 −6.070 1.00 26.09 C ATOM 933 N LEU A 140 72.638 2.450 −3.402 1.00 26.95 N ATOM 934 CA LEU A 140 71.385 2.199 −2.723 1.00 27.05 C ATOM 935 C LEU A 140 71.262 0.701 −2.504 1.00 27.88 C ATOM 936 O LEU A 140 71.153 −0.058 −3.461 1.00 28.79 O ATOM 937 CB LEU A 140 70.228 2.708 −3.591 1.00 26.81 C ATOM 938 CG LEU A 140 68.802 2.552 −3.055 1.00 26.55 C ATOM 939 CD1 LEU A 140 68.691 3.334 −1.760 1.00 27.17 C ATOM 940 CD2 LEU A 140 67.784 3.057 −4.090 1.00 25.60 C ATOM 941 N PRO A 141 71.287 0.246 −1.239 1.00 28.65 N ATOM 942 CA PRO A 141 71.171 −1.201 −1.015 1.00 30.03 C ATOM 943 C PRO A 141 69.762 −1.677 −1.358 1.00 30.80 C ATOM 944 O PRO A 141 68.777 −1.062 −0.945 1.00 31.23 O ATOM 945 CB PRO A 141 71.502 −1.341 0.472 1.00 29.16 C ATOM 946 CG PRO A 141 70.894 −0.089 1.053 1.00 29.20 C ATOM 947 CD PRO A 141 71.285 0.987 0.035 1.00 28.56 C ATOM 948 N MET A 142 69.670 −2.758 −2.124 1.00 32.42 N ATOM 949 CA MET A 142 68.378 −3.298 −2.531 1.00 34.31 C ATOM 950 C MET A 142 68.296 −4.795 −2.277 1.00 35.79 C ATOM 951 O MET A 142 69.318 −5.486 −2.227 1.00 36.15 O ATOM 952 CB MET A 142 68.143 −3.025 −4.018 1.00 34.61 C ATOM 953 CG MET A 142 68.149 −1.553 −4.402 1.00 33.78 C ATOM 954 SD MET A 142 67.851 −1.331 −6.157 1.00 34.38 S ATOM 955 CE MET A 142 66.113 −1.835 −6.255 1.00 34.37 C ATOM 956 N SER A 143 67.075 −5.291 −2.132 1.00 37.37 N ATOM 957 CA SER A 143 66.848 −6.707 −1.883 1.00 39.58 C ATOM 958 C SER A 143 67.342 −7.591 −3.020 1.00 40.67 C ATOM 959 O SER A 143 67.277 −7.215 −4.193 1.00 39.83 O ATOM 960 CB SER A 143 65.360 −6.966 −1.652 1.00 39.84 C ATOM 961 OG SER A 143 65.143 −8.328 −1.337 1.00 41.58 O ATOM 962 N ALA A 144 67.842 −8.770 −2.662 1.00 42.94 N ATOM 963 CA ALA A 144 68.327 −9.715 −3.659 1.00 45.52 C ATOM 964 C ALA A 144 67.165 −10.596 −4.135 1.00 47.20 C ATOM 965 O ALA A 144 67.364 −11.740 −4.528 1.00 48.00 O ATOM 966 CB ALA A 144 69.453 −10.571 −3.083 1.00 44.42 C ATOM 967 N LYS A 145 65.954 −10.037 −4.103 1.00 49.35 N ATOM 968 CA LYS A 145 64.739 −10.732 −4.536 1.00 50.42 C ATOM 969 C LYS A 145 64.599 −12.067 −3.830 1.00 51.05 C ATOM 970 O LYS A 145 64.318 −12.015 −2.615 1.00 51.85 O ATOM 971 CB LYS A 145 64.749 −10.954 −6.053 1.00 50.92 C TER 972 LYS A 145 ATOM 973 N HIS B 16 29.691 59.874 −5.987 1.00 41.20 N ATOM 974 CA HIS B 16 30.532 60.667 −6.938 1.00 40.87 C ATOM 975 C HIS B 16 32.001 60.521 −6.563 1.00 39.74 C ATOM 976 O HIS B 16 32.413 60.901 −5.467 1.00 39.06 O ATOM 977 CB HIS B 16 30.131 62.149 −6.894 1.00 41.47 C ATOM 978 N PHE B 17 32.783 59.981 −7.489 1.00 38.43 N ATOM 979 CA PHE B 17 34.203 59.742 −7.270 1.00 37.73 C ATOM 980 C PHE B 17 35.047 60.975 −6.928 1.00 37.15 C ATOM 981 O PHE B 17 36.062 60.855 −6.240 1.00 36.85 O ATOM 982 CB PHE B 17 34.784 59.027 −8.494 1.00 36.91 C ATOM 983 CG PHE B 17 34.834 59.876 −9.724 1.00 35.74 C ATOM 984 CD1 PHE B 17 35.928 60.696 −9.969 1.00 35.10 C ATOM 985 CD2 PHE B 17 33.794 59.855 −10.646 1.00 35.94 C ATOM 986 CE1 PHE B 17 35.988 61.480 −11.112 1.00 35.16 C ATOM 987 CE2 PHE B 17 33.846 60.640 −11.800 1.00 36.07 C ATOM 988 CZ PHE B 17 34.944 61.453 −12.032 1.00 35.19 C ATOM 989 N LYS B 18 34.641 62.154 −7.392 1.00 37.23 N ATOM 990 CA LYS B 18 35.420 63.355 −7.092 1.00 38.08 C ATOM 991 C LYS B 18 35.185 63.943 −5.698 1.00 38.08 C ATOM 992 O LYS B 18 35.948 64.798 −5.244 1.00 38.20 O ATOM 993 CB LYS B 18 35.231 64.432 −8.171 1.00 39.65 C ATOM 994 CG LYS B 18 33.845 64.545 −8.774 1.00 42.73 C ATOM 995 CD LYS B 18 33.890 65.478 −9.994 1.00 43.91 C ATOM 996 CE LYS B 18 32.555 65.512 −10.725 1.00 44.63 C ATOM 997 NZ LYS B 18 32.139 64.155 −11.160 1.00 46.27 N ATOM 998 N ASP B 19 34.158 63.462 −5.007 1.00 37.77 N ATOM 999 CA ASP B 19 33.864 63.942 −3.661 1.00 38.47 C ATOM 1000 C ASP B 19 34.811 63.344 −2.620 1.00 38.55 C ATOM 1001 O ASP B 19 35.267 62.202 −2.763 1.00 37.81 O ATOM 1002 CB ASP B 19 32.431 63.580 −3.263 1.00 39.90 C ATOM 1003 CG ASP B 19 31.384 64.268 −4.122 1.00 41.14 C ATOM 1004 OD1 ASP B 19 30.214 63.826 −4.091 1.00 41.72 O ATOM 1005 OD2 ASP B 19 31.724 65.253 −4.814 1.00 42.42 O ATOM 1006 N PRO B 20 35.132 64.121 −1.566 1.00 38.54 N ATOM 1007 CA PRO B 20 36.016 63.650 −0.497 1.00 38.26 C ATOM 1008 C PRO B 20 35.346 62.480 0.226 1.00 37.93 C ATOM 1009 O PRO B 20 34.129 62.302 0.135 1.00 37.55 O ATOM 1010 CB PRO B 20 36.182 64.886 0.397 1.00 39.27 C ATOM 1011 CG PRO B 20 34.945 65.690 0.133 1.00 39.95 C ATOM 1012 CD PRO B 20 34.776 65.539 −1.361 1.00 39.71 C ATOM 1013 N LYS B 21 36.128 61.684 0.945 1.00 37.56 N ATOM 1014 CA LYS B 21 35.566 60.514 1.624 1.00 38.03 C ATOM 1015 C LYS B 21 36.277 60.213 2.922 1.00 37.58 C ATOM 1016 O LYS B 21 37.356 60.736 3.195 1.00 37.36 O ATOM 1017 CB LYS B 21 35.718 59.232 0.773 1.00 38.55 C ATOM 1018 CG LYS B 21 35.458 59.310 −0.726 1.00 40.40 C ATOM 1019 CD LYS B 21 36.141 58.119 −1.403 1.00 42.66 C ATOM 1020 CE LYS B 21 36.004 58.118 −2.931 1.00 45.28 C ATOM 1021 NZ LYS B 21 34.693 57.570 −3.390 1.00 46.79 N ATOM 1022 N ARG B 22 35.660 59.338 3.705 1.00 36.89 N ATOM 1023 CA ARG B 22 36.254 58.875 4.942 1.00 36.76 C ATOM 1024 C ARG B 22 36.607 57.442 4.575 1.00 35.99 C ATOM 1025 O ARG B 22 35.878 56.812 3.807 1.00 36.59 O ATOM 1026 CB ARG B 22 35.244 58.835 6.088 1.00 37.88 C ATOM 1027 CG ARG B 22 34.503 60.125 6.396 1.00 40.72 C ATOM 1028 CD ARG B 22 33.663 59.899 7.650 1.00 42.38 C ATOM 1029 NE ARG B 22 32.359 60.562 7.626 1.00 45.73 N ATOM 1030 CZ ARG B 22 32.137 61.830 7.961 1.00 46.48 C ATOM 1031 NH1 ARG B 22 33.137 62.608 8.355 1.00 48.50 N ATOM 1032 NH2 ARG B 22 30.904 62.320 7.909 1.00 47.02 N ATOM 1033 N LEU B 23 37.725 56.938 5.085 1.00 34.47 N ATOM 1034 CA LEU B 23 38.119 55.559 4.824 1.00 32.66 C ATOM 1035 C LEU B 23 37.990 54.799 6.142 1.00 33.01 C ATOM 1036 O LEU B 23 38.799 54.979 7.059 1.00 33.02 O ATOM 1037 CB LEU B 23 39.557 55.479 4.311 1.00 31.69 C ATOM 1038 CG LEU B 23 39.832 55.862 2.851 1.00 31.92 C ATOM 1039 CD1 LEU B 23 41.324 55.644 2.544 1.00 31.01 C ATOM 1040 CD2 LEU B 23 38.968 55.019 1.914 1.00 30.24 C ATOM 1041 N TYR B 24 36.957 53.958 6.223 1.00 31.84 N ATOM 1042 CA TYR B 24 36.651 53.158 7.408 1.00 30.77 C ATOM 1043 C TYR B 24 37.390 51.815 7.406 1.00 30.86 C ATOM 1044 O TYR B 24 37.290 51.042 6.457 1.00 30.57 O ATOM 1045 CB TYR B 24 35.118 52.950 7.489 1.00 29.83 C ATOM 1046 CG TYR B 24 34.605 51.982 8.548 1.00 28.06 C ATOM 1047 CD1 TYR B 24 34.689 50.601 8.359 1.00 29.06 C ATOM 1048 CD2 TYR B 24 34.010 52.447 9.728 1.00 27.71 C ATOM 1049 CE1 TYR B 24 34.191 49.701 9.314 1.00 28.51 C ATOM 1050 CE2 TYR B 24 33.509 51.559 10.691 1.00 27.43 C ATOM 1051 CZ TYR B 24 33.601 50.184 10.475 1.00 29.33 C ATOM 1052 OH TYR B 24 33.092 49.285 11.398 1.00 29.90 O ATOM 1053 N CYS B 25 38.135 51.537 8.471 1.00 30.52 N ATOM 1054 CA CYS B 25 38.871 50.279 8.547 1.00 31.88 C ATOM 1055 C CYS B 25 38.055 49.198 9.254 1.00 32.26 C ATOM 1056 O CYS B 25 37.610 49.374 10.384 1.00 32.63 O ATOM 1057 CB CYS B 25 40.216 50.459 9.272 1.00 30.70 C ATOM 1058 SG CYS B 25 41.232 48.937 9.279 1.00 33.39 S ATOM 1059 N LYS B 26 37.859 48.077 8.571 1.00 34.00 N ATOM 1060 CA LYS B 26 37.091 46.978 9.135 1.00 35.65 C ATOM 1061 C LYS B 26 37.692 46.542 10.477 1.00 36.77 C ATOM 1062 O LYS B 26 36.969 46.136 11.383 1.00 36.34 O ATOM 1063 CB LYS B 26 37.069 45.794 8.168 1.00 35.74 C ATOM 1064 CG LYS B 26 36.256 44.622 8.690 1.00 37.36 C ATOM 1065 CD LYS B 26 36.371 43.407 7.796 1.00 38.54 C ATOM 1066 CE LYS B 26 35.480 42.287 8.311 1.00 40.15 C ATOM 1067 NZ LYS B 26 35.677 41.049 7.509 1.00 41.23 N ATOM 1068 N ASN B 27 39.014 46.636 10.602 1.00 37.35 N ATOM 1069 CA ASN B 27 39.681 46.250 11.843 1.00 37.78 C ATOM 1070 C ASN B 27 39.415 47.295 12.930 1.00 37.79 C ATOM 1071 O ASN B 27 39.999 48.383 12.927 1.00 38.21 O ATOM 1072 CB ASN B 27 41.187 46.103 11.617 1.00 39.72 C ATOM 1073 CG ASN B 27 41.887 45.400 12.773 1.00 43.31 C ATOM 1074 OD1 ASN B 27 43.125 45.404 12.872 1.00 43.49 O ATOM 1075 ND2 ASN B 27 41.100 44.782 13.648 1.00 43.66 N ATOM 1076 N GLY B 28 38.511 46.971 13.847 1.00 36.80 N ATOM 1077 CA GLY B 28 38.188 47.883 14.926 1.00 36.61 C ATOM 1078 C GLY B 28 37.208 48.999 14.605 1.00 36.56 C ATOM 1079 O GLY B 28 36.657 49.622 15.511 1.00 36.62 O ATOM 1080 N GLY B 29 36.992 49.272 13.324 1.00 37.24 N ATOM 1081 CA GLY B 29 36.057 50.322 12.956 1.00 37.20 C ATOM 1082 C GLY B 29 36.577 51.741 13.129 1.00 37.22 C ATOM 1083 O GLY B 29 35.836 52.630 13.548 1.00 37.21 O ATOM 1084 N PHE B 30 37.848 51.957 12.807 1.00 37.85 N ATOM 1085 CA PHE B 30 38.458 53.288 12.919 1.00 38.68 C ATOM 1086 C PHE B 30 38.508 53.977 11.559 1.00 38.10 C ATOM 1087 O PHE B 30 38.687 53.325 10.536 1.00 38.20 O ATOM 1088 CB PHE B 30 39.905 53.201 13.426 1.00 38.81 C ATOM 1089 CG PHE B 30 40.049 52.642 14.812 1.00 39.31 C ATOM 1090 CD1 PHE B 30 40.339 51.294 15.005 1.00 38.57 C ATOM 1091 CD2 PHE B 30 39.932 53.473 15.923 1.00 38.57 C ATOM 1092 CE1 PHE B 30 40.514 50.779 16.285 1.00 39.12 C ATOM 1093 CE2 PHE B 30 40.105 52.972 17.211 1.00 38.92 C ATOM 1094 CZ PHE B 30 40.397 51.621 17.396 1.00 38.67 C ATOM 1095 N PHE B 31 38.365 55.295 11.559 1.00 38.30 N ATOM 1096 CA PHE B 31 38.446 56.074 10.331 1.00 38.10 C ATOM 1097 C PHE B 31 39.883 56.547 10.186 1.00 38.64 C ATOM 1098 O PHE B 31 40.445 57.103 11.134 1.00 38.89 O ATOM 1099 CB PHE B 31 37.531 57.280 10.421 1.00 37.10 C ATOM 1100 CG PHE B 31 36.095 56.938 10.295 1.00 36.88 C ATOM 1101 CD1 PHE B 31 35.551 56.637 9.047 1.00 34.97 C ATOM 1102 CD2 PHE B 31 35.285 56.873 11.419 1.00 36.08 C ATOM 1103 CE1 PHE B 31 34.217 56.277 8.928 1.00 35.59 C ATOM 1104 CE2 PHE B 31 33.942 56.510 11.306 1.00 37.12 C ATOM 1105 CZ PHE B 31 33.410 56.211 10.055 1.00 34.95 C ATOM 1106 N LEU B 32 40.485 56.323 9.020 1.00 38.61 N ATOM 1107 CA LEU B 32 41.870 56.749 8.791 1.00 38.97 C ATOM 1108 C LEU B 32 41.958 58.253 9.036 1.00 39.72 C ATOM 1109 O LEU B 32 41.170 59.023 8.482 1.00 39.68 O ATOM 1110 CB LEU B 32 42.307 56.424 7.356 1.00 38.43 C ATOM 1111 CG LEU B 32 43.787 56.609 6.994 1.00 38.14 C ATOM 1112 CD1 LEU B 32 44.664 55.726 7.877 1.00 37.20 C ATOM 1113 CD2 LEU B 32 44.004 56.257 5.530 1.00 37.43 C ATOM 1114 N ARG B 33 42.910 58.672 9.870 1.00 40.78 N ATOM 1115 CA ARG B 33 43.067 60.094 10.197 1.00 41.49 C ATOM 1116 C ARG B 33 44.449 60.658 9.872 1.00 41.79 C ATOM 1117 O ARG B 33 45.470 60.040 10.165 1.00 41.69 O ATOM 1118 CB ARG B 33 42.753 60.316 11.683 1.00 41.87 C ATOM 1119 CG ARG B 33 42.997 61.734 12.173 1.00 42.16 C ATOM 1120 CD ARG B 33 42.468 61.952 13.587 1.00 41.66 C ATOM 1121 NE ARG B 33 43.170 61.161 14.597 1.00 42.10 N ATOM 1122 CZ ARG B 33 42.870 61.180 15.897 1.00 41.89 C ATOM 1123 NH1 ARG B 33 41.884 61.947 16.341 1.00 39.60 N ATOM 1124 NH2 ARG B 33 43.557 60.434 16.759 1.00 40.90 N ATOM 1125 N ILE B 34 44.474 61.836 9.258 1.00 43.37 N ATOM 1126 CA ILE B 34 45.733 62.497 8.904 1.00 44.60 C ATOM 1127 C ILE B 34 45.829 63.834 9.632 1.00 45.66 C ATOM 1128 O ILE B 34 45.142 64.793 9.290 1.00 45.68 O ATOM 1129 CB ILE B 34 45.859 62.710 7.362 1.00 44.79 C ATOM 1130 CG1 ILE B 34 46.101 61.357 6.680 1.00 44.68 C ATOM 1131 CG2 ILE B 34 47.006 63.679 7.035 1.00 43.70 C ATOM 1132 CD1 ILE B 34 46.242 61.429 5.182 1.00 45.23 C ATOM 1133 N HIS B 35 46.683 63.865 10.654 1.00 47.90 N ATOM 1134 CA HIS B 35 46.910 65.050 11.488 1.00 49.69 C ATOM 1135 C HIS B 35 47.663 66.169 10.779 1.00 50.18 C ATOM 1136 O HIS B 35 48.477 65.917 9.885 1.00 49.89 O ATOM 1137 CB HIS B 35 47.708 64.667 12.733 1.00 50.95 C ATOM 1138 CG HIS B 35 46.961 63.794 13.687 1.00 52.79 C ATOM 1139 ND1 HIS B 35 45.939 64.266 14.483 1.00 53.73 N ATOM 1140 CD2 HIS B 35 47.094 62.480 13.982 1.00 53.11 C ATOM 1141 CE1 HIS B 35 45.476 63.280 15.230 1.00 54.07 C ATOM 1142 NE2 HIS B 35 46.160 62.186 14.945 1.00 54.33 N ATOM 1143 N PRO B 36 47.421 67.424 11.197 1.00 50.94 N ATOM 1144 CA PRO B 36 48.080 68.588 10.601 1.00 51.39 C ATOM 1145 C PRO B 36 49.603 68.500 10.634 1.00 51.71 C ATOM 1146 O PRO B 36 50.266 68.999 9.729 1.00 51.94 O ATOM 1147 CB PRO B 36 47.541 69.748 11.430 1.00 51.36 C ATOM 1148 CG PRO B 36 46.158 69.284 11.773 1.00 51.50 C ATOM 1149 CD PRO B 36 46.408 67.851 12.181 1.00 50.68 C ATOM 1150 N ASP B 37 50.155 67.863 11.666 1.00 52.35 N ATOM 1151 CA ASP B 37 51.607 67.736 11.767 1.00 53.06 C ATOM 1152 C ASP B 37 52.169 66.505 11.064 1.00 52.67 C ATOM 1153 O ASP B 37 53.354 66.194 11.192 1.00 52.98 O ATOM 1154 CB ASP B 37 52.071 67.776 13.236 1.00 54.79 C ATOM 1155 CG ASP B 37 51.464 66.676 14.086 1.00 56.33 C ATOM 1156 OD1 ASP B 37 50.224 66.656 14.243 1.00 56.83 O ATOM 1157 OD2 ASP B 37 52.236 65.837 14.607 1.00 57.53 O ATOM 1158 N GLY B 38 51.318 65.804 10.318 1.00 52.01 N ATOM 1159 CA GLY B 38 51.781 64.642 9.579 1.00 50.97 C ATOM 1160 C GLY B 38 51.694 63.265 10.214 1.00 50.53 C ATOM 1161 O GLY B 38 52.146 62.289 9.610 1.00 50.78 O ATOM 1162 N ARG B 39 51.130 63.162 11.414 1.00 49.98 N ATOM 1163 CA ARG B 39 51.006 61.857 12.069 1.00 50.01 C ATOM 1164 C ARG B 39 49.785 61.117 11.513 1.00 48.98 C ATOM 1165 O ARG B 39 48.775 61.743 11.176 1.00 48.74 O ATOM 1166 CB ARG B 39 50.866 62.023 13.592 1.00 51.16 C ATOM 1167 CG ARG B 39 52.179 62.313 14.318 1.00 53.76 C ATOM 1168 CD ARG B 39 51.976 62.563 15.817 1.00 55.43 C ATOM 1169 NE ARG B 39 51.143 63.738 16.080 1.00 57.14 N ATOM 1170 CZ ARG B 39 49.822 63.706 16.244 1.00 57.89 C ATOM 1171 NH1 ARG B 39 49.150 64.831 16.470 1.00 57.92 N ATOM 1172 NH2 ARG B 39 49.172 62.549 16.201 1.00 58.81 N ATOM 1173 N VAL B 40 49.879 59.793 11.423 1.00 47.61 N ATOM 1174 CA VAL B 40 48.777 58.994 10.897 1.00 46.88 C ATOM 1175 C VAL B 40 48.288 57.919 11.871 1.00 46.13 C ATOM 1176 O VAL B 40 49.074 57.114 12.370 1.00 45.77 O ATOM 1177 CB VAL B 40 49.176 58.321 9.550 1.00 46.91 C ATOM 1178 CG1 VAL B 40 48.069 57.355 9.077 1.00 46.28 C ATOM 1179 CG2 VAL B 40 49.421 59.399 8.493 1.00 45.41 C ATOM 1180 N ASP B 41 46.983 57.923 12.132 1.00 45.81 N ATOM 1181 CA ASP B 41 46.360 56.946 13.025 1.00 45.94 C ATOM 1182 C ASP B 41 44.877 56.811 12.679 1.00 45.67 C ATOM 1183 O ASP B 41 44.429 57.306 11.642 1.00 45.16 O ATOM 1184 CB ASP B 41 46.515 57.376 14.490 1.00 45.68 C ATOM 1185 CG ASP B 41 45.744 58.641 14.815 1.00 46.42 C ATOM 1186 OD1 ASP B 41 45.810 59.094 15.981 1.00 47.24 O ATOM 1187 OD2 ASP B 41 45.073 59.188 13.916 1.00 46.74 O ATOM 1188 N GLY B 42 44.128 56.143 13.553 1.00 45.79 N ATOM 1189 CA GLY B 42 42.707 55.956 13.333 1.00 45.89 C ATOM 1190 C GLY B 42 41.901 56.424 14.527 1.00 46.60 C ATOM 1191 O GLY B 42 42.416 56.488 15.644 1.00 46.61 O ATOM 1192 N VAL B 43 40.643 56.774 14.286 1.00 47.12 N ATOM 1193 CA VAL B 43 39.735 57.224 15.336 1.00 47.40 C ATOM 1194 C VAL B 43 38.317 56.844 14.975 1.00 48.03 C ATOM 1195 O VAL B 43 37.985 56.718 13.795 1.00 48.35 O ATOM 1196 CB VAL B 43 39.767 58.745 15.542 1.00 47.09 C ATOM 1197 CG1 VAL B 43 40.850 59.099 16.524 1.00 47.34 C ATOM 1198 CG2 VAL B 43 39.976 59.452 14.219 1.00 45.89 C ATOM 1199 N ARG B 44 37.480 56.684 15.991 1.00 48.67 N ATOM 1200 CA ARG B 44 36.099 56.291 15.776 1.00 49.72 C ATOM 1201 C ARG B 44 35.109 57.447 15.655 1.00 50.61 C ATOM 1202 O ARG B 44 34.020 57.274 15.110 1.00 50.99 O ATOM 1203 CB ARG B 44 35.671 55.316 16.879 1.00 49.25 C ATOM 1204 CG ARG B 44 36.431 53.989 16.811 1.00 49.05 C ATOM 1205 CD ARG B 44 36.035 53.017 17.909 1.00 48.64 C ATOM 1206 NE ARG B 44 36.670 51.714 17.715 1.00 49.15 N ATOM 1207 CZ ARG B 44 37.108 50.942 18.706 1.00 49.17 C ATOM 1208 NH1 ARG B 44 36.982 51.347 19.965 1.00 49.60 N ATOM 1209 NH2 ARG B 44 37.671 49.768 18.443 1.00 48.11 N ATOM 1210 N GLU B 45 35.487 58.628 16.129 1.00 51.32 N ATOM 1211 CA GLU B 45 34.590 59.770 16.061 1.00 52.99 C ATOM 1212 C GLU B 45 34.382 60.301 14.639 1.00 53.72 C ATOM 1213 O GLU B 45 35.247 60.970 14.067 1.00 53.64 O ATOM 1214 CB GLU B 45 35.094 60.885 16.981 1.00 54.62 C ATOM 1215 CG GLU B 45 34.103 62.022 17.153 1.00 56.11 C ATOM 1216 CD GLU B 45 32.668 61.533 17.166 1.00 57.20 C ATOM 1217 OE1 GLU B 45 32.367 60.568 17.904 1.00 58.01 O ATOM 1218 OE2 GLU B 45 31.838 62.115 16.436 1.00 57.95 O ATOM 1219 N LYS B 46 33.212 60.001 14.081 1.00 53.86 N ATOM 1220 CA LYS B 46 32.863 60.425 12.732 1.00 54.06 C ATOM 1221 C LYS B 46 32.912 61.941 12.542 1.00 54.13 C ATOM 1222 O LYS B 46 32.890 62.429 11.411 1.00 54.29 O ATOM 1223 CB LYS B 46 31.465 59.911 12.377 1.00 53.90 C ATOM 1224 N SER B 47 32.993 62.682 13.641 1.00 54.05 N ATOM 1225 CA SER B 47 33.013 64.142 13.573 1.00 54.44 C ATOM 1226 C SER B 47 34.403 64.755 13.425 1.00 54.13 C ATOM 1227 O SER B 47 34.536 65.932 13.092 1.00 54.74 O ATOM 1228 CB SER B 47 32.328 64.728 14.811 1.00 55.19 C ATOM 1229 OG SER B 47 32.215 66.138 14.708 1.00 57.49 O ATOM 1230 N ASP B 48 35.438 63.964 13.668 1.00 53.76 N ATOM 1231 CA ASP B 48 36.802 64.460 13.560 1.00 53.29 C ATOM 1232 C ASP B 48 37.058 65.080 12.186 1.00 52.62 C ATOM 1233 O ASP B 48 36.837 64.444 11.157 1.00 52.61 O ATOM 1234 CB ASP B 48 37.790 63.320 13.832 1.00 54.05 C ATOM 1235 CG ASP B 48 39.219 63.808 13.965 1.00 55.08 C ATOM 1236 OD1 ASP B 48 39.994 63.167 14.711 1.00 55.65 O ATOM 1237 OD2 ASP B 48 39.569 64.825 13.324 1.00 54.58 O ATOM 1238 N PRO B 49 37.526 66.340 12.158 1.00 52.10 N ATOM 1239 CA PRO B 49 37.813 67.060 10.910 1.00 50.74 C ATOM 1240 C PRO B 49 39.037 66.568 10.134 1.00 49.71 C ATOM 1241 O PRO B 49 39.256 66.979 8.997 1.00 50.41 O ATOM 1242 CB PRO B 49 37.962 68.504 11.378 1.00 51.63 C ATOM 1243 CG PRO B 49 38.574 68.337 12.738 1.00 51.61 C ATOM 1244 CD PRO B 49 37.745 67.216 13.325 1.00 52.05 C ATOM 1245 N HIS B 50 39.825 65.685 10.737 1.00 48.05 N ATOM 1246 CA HIS B 50 41.026 65.163 10.088 1.00 46.32 C ATOM 1247 C HIS B 50 40.866 63.790 9.411 1.00 44.99 C ATOM 1248 O HIS B 50 41.856 63.141 9.085 1.00 44.20 O ATOM 1249 CB HIS B 50 42.173 65.102 11.104 1.00 46.22 C ATOM 1250 N ILE B 51 39.628 63.344 9.209 1.00 43.86 N ATOM 1251 CA ILE B 51 39.394 62.066 8.544 1.00 42.57 C ATOM 1252 C ILE B 51 38.772 62.280 7.163 1.00 41.66 C ATOM 1253 O ILE B 51 38.504 61.316 6.441 1.00 40.77 O ATOM 1254 CB ILE B 51 38.477 61.141 9.371 1.00 42.29 C ATOM 1255 CG1 ILE B 51 37.116 61.801 9.584 1.00 42.59 C ATOM 1256 CG2 ILE B 51 39.148 60.807 10.695 1.00 42.29 C ATOM 1257 CD1 ILE B 51 36.040 60.839 10.067 1.00 44.12 C ATOM 1258 N LYS B 52 38.536 63.542 6.804 1.00 40.51 N ATOM 1259 CA LYS B 52 37.975 63.871 5.496 1.00 39.40 C ATOM 1260 C LYS B 52 39.143 63.807 4.521 1.00 38.70 C ATOM 1261 O LYS B 52 40.060 64.632 4.582 1.00 39.00 O ATOM 1262 CB LYS B 52 37.360 65.276 5.492 1.00 38.94 C ATOM 1263 N LEU B 53 39.107 62.824 3.622 1.00 36.69 N ATOM 1264 CA LEU B 53 40.179 62.627 2.657 1.00 34.75 C ATOM 1265 C LEU B 53 39.783 62.879 1.209 1.00 34.22 C ATOM 1266 O LEU B 53 38.610 62.835 0.852 1.00 36.06 O ATOM 1267 CB LEU B 53 40.710 61.203 2.775 1.00 34.22 C ATOM 1268 CG LEU B 53 41.174 60.750 4.153 1.00 33.71 C ATOM 1269 CD1 LEU B 53 41.431 59.259 4.133 1.00 33.62 C ATOM 1270 CD2 LEU B 53 42.430 61.507 4.533 1.00 34.34 C ATOM 1271 N GLN B 54 40.778 63.127 0.370 1.00 32.84 N ATOM 1272 CA GLN B 54 40.533 63.363 −1.044 1.00 31.93 C ATOM 1273 C GLN B 54 41.373 62.404 −1.865 1.00 31.30 C ATOM 1274 O GLN B 54 42.598 62.530 −1.886 1.00 30.03 O ATOM 1275 CB GLN B 54 40.916 64.793 −1.439 1.00 32.97 C ATOM 1276 CG GLN B 54 40.549 65.155 −2.877 1.00 33.02 C ATOM 1277 CD GLN B 54 39.042 65.222 −3.080 1.00 34.77 C ATOM 1278 OE1 GLN B 54 38.352 66.036 −2.455 1.00 35.07 O ATOM 1279 NE2 GLN B 54 38.522 64.362 −3.946 1.00 34.98 N ATOM 1280 N LEU B 55 40.729 61.446 −2.533 1.00 30.73 N ATOM 1281 CA LEU B 55 41.475 60.498 −3.375 1.00 31.57 C ATOM 1282 C LEU B 55 41.591 61.069 −4.786 1.00 30.56 C ATOM 1283 O LEU B 55 40.724 61.818 −5.234 1.00 30.71 O ATOM 1284 CB LEU B 55 40.783 59.127 −3.430 1.00 32.23 C ATOM 1285 CG LEU B 55 40.429 58.411 −2.113 1.00 35.23 C ATOM 1286 CD1 LEU B 55 40.135 56.946 −2.398 1.00 34.62 C ATOM 1287 CD2 LEU B 55 41.576 58.513 −1.118 1.00 34.97 C ATOM 1288 N GLN B 56 42.666 60.721 −5.482 1.00 30.02 N ATOM 1289 CA GLN B 56 42.886 61.211 −6.837 1.00 29.32 C ATOM 1290 C GLN B 56 43.742 60.202 −7.575 1.00 29.63 C ATOM 1291 O GLN B 56 44.809 59.829 −7.094 1.00 29.46 O ATOM 1292 CB GLN B 56 43.597 62.579 −6.789 1.00 29.41 C ATOM 1293 CG GLN B 56 43.917 63.203 −8.146 1.00 29.62 C ATOM 1294 CD GLN B 56 42.684 63.475 −8.982 1.00 28.94 C ATOM 1295 OE1 GLN B 56 41.830 64.275 −8.611 1.00 29.99 O ATOM 1296 NE2 GLN B 56 42.583 62.799 −10.122 1.00 30.33 N ATOM 1297 N ALA B 57 43.272 59.749 −8.733 1.00 29.97 N ATOM 1298 CA ALA B 57 44.016 58.779 −9.534 1.00 30.63 C ATOM 1299 C ALA B 57 45.177 59.458 −10.267 1.00 31.45 C ATOM 1300 O ALA B 57 45.013 60.545 −10.821 1.00 31.11 O ATOM 1301 CB ALA B 57 43.082 58.116 −10.545 1.00 29.39 C ATOM 1302 N GLU B 58 46.342 58.816 −10.262 1.00 32.00 N ATOM 1303 CA GLU B 58 47.521 59.361 −10.935 1.00 32.70 C ATOM 1304 C GLU B 58 47.660 58.627 −12.267 1.00 33.16 C ATOM 1305 O GLU B 58 48.173 59.169 −13.249 1.00 32.46 O ATOM 1306 CB GLU B 58 48.769 59.141 −10.075 1.00 34.03 C ATOM 1307 CG GLU B 58 49.957 60.027 −10.445 1.00 35.07 C ATOM 1308 CD GLU B 58 49.636 61.517 −10.331 1.00 36.28 C ATOM 1309 OE1 GLU B 58 48.984 61.930 −9.346 1.00 36.31 O ATOM 1310 OE2 GLU B 58 50.041 62.280 −11.231 1.00 38.59 O ATOM 1311 N GLU B 59 47.221 57.372 −12.264 1.00 33.20 N ATOM 1312 CA GLU B 59 47.200 56.526 −13.450 1.00 34.42 C ATOM 1313 C GLU B 59 46.210 55.405 −13.136 1.00 33.04 C ATOM 1314 O GLU B 59 45.739 55.293 −12.004 1.00 32.98 O ATOM 1315 CB GLU B 59 48.591 55.983 −13.806 1.00 36.51 C ATOM 1316 CG GLU B 59 49.109 54.811 −12.999 1.00 40.45 C ATOM 1317 CD GLU B 59 50.435 54.299 −13.555 1.00 42.69 C ATOM 1318 OE1 GLU B 59 51.397 55.097 −13.619 1.00 44.62 O ATOM 1319 OE2 GLU B 59 50.519 53.112 −13.939 1.00 43.75 O ATOM 1320 N ARG B 60 45.878 54.599 −14.133 1.00 32.15 N ATOM 1321 CA ARG B 60 44.906 53.534 −13.955 1.00 32.04 C ATOM 1322 C ARG B 60 45.142 52.685 −12.703 1.00 30.69 C ATOM 1323 O ARG B 60 46.201 52.078 −12.546 1.00 30.48 O ATOM 1324 CB ARG B 60 44.896 52.664 −15.217 1.00 33.28 C ATOM 1325 CG ARG B 60 43.791 51.648 −15.275 1.00 35.74 C ATOM 1326 CD ARG B 60 43.852 50.864 −16.568 1.00 37.31 C ATOM 1327 NE ARG B 60 43.209 49.579 −16.370 1.00 41.07 N ATOM 1328 CZ ARG B 60 43.776 48.408 −16.628 1.00 42.59 C ATOM 1329 NH1 ARG B 60 45.010 48.349 −17.113 1.00 42.37 N ATOM 1330 NH2 ARG B 60 43.113 47.292 −16.359 1.00 44.09 N ATOM 1331 N GLY B 61 44.160 52.670 −11.802 1.00 29.44 N ATOM 1332 CA GLY B 61 44.270 51.867 −10.594 1.00 28.64 C ATOM 1333 C GLY B 61 45.239 52.336 −9.518 1.00 28.44 C ATOM 1334 O GLY B 61 45.447 51.631 −8.518 1.00 28.45 O ATOM 1335 N VAL B 62 45.837 53.510 −9.705 1.00 27.68 N ATOM 1336 CA VAL B 62 46.772 54.041 −8.716 1.00 27.03 C ATOM 1337 C VAL B 62 46.289 55.398 −8.188 1.00 26.84 C ATOM 1338 O VAL B 62 45.970 56.298 −8.961 1.00 27.29 O ATOM 1339 CB VAL B 62 48.183 54.198 −9.320 1.00 27.60 C ATOM 1340 CG1 VAL B 62 49.179 54.609 −8.220 1.00 27.44 C ATOM 1341 CG2 VAL B 62 48.617 52.884 −9.993 1.00 27.44 C ATOM 1342 N VAL B 63 46.244 55.555 −6.870 1.00 26.76 N ATOM 1343 CA VAL B 63 45.775 56.816 −6.296 1.00 26.49 C ATOM 1344 C VAL B 63 46.693 57.419 −5.240 1.00 27.04 C ATOM 1345 O VAL B 63 47.592 56.750 −4.717 1.00 26.79 O ATOM 1346 CB VAL B 63 44.386 56.666 −5.614 1.00 25.62 C ATOM 1347 CG1 VAL B 63 43.406 55.941 −6.535 1.00 25.75 C ATOM 1348 CG2 VAL B 63 44.540 55.920 −4.290 1.00 24.62 C ATOM 1349 N SER B 64 46.444 58.693 −4.942 1.00 26.91 N ATOM 1350 CA SER B 64 47.163 59.413 −3.896 1.00 27.65 C ATOM 1351 C SER B 64 46.028 59.740 −2.922 1.00 27.63 C ATOM 1352 O SER B 64 44.887 59.936 −3.341 1.00 27.72 O ATOM 1353 CB SER B 64 47.819 60.706 −4.431 1.00 27.51 C ATOM 1354 OG SER B 64 46.879 61.733 −4.711 1.00 26.28 O ATOM 1355 N ILE B 65 46.328 59.758 −1.631 1.00 27.50 N ATOM 1356 CA ILE B 65 45.324 60.045 −0.613 1.00 29.11 C ATOM 1357 C ILE B 65 45.742 61.299 0.182 1.00 30.87 C ATOM 1358 O ILE B 65 46.764 61.293 0.872 1.00 29.58 O ATOM 1359 CB ILE B 65 45.186 58.844 0.348 1.00 28.40 C ATOM 1360 CG1 ILE B 65 44.783 57.594 −0.436 1.00 28.74 C ATOM 1361 CG2 ILE B 65 44.151 59.146 1.414 1.00 29.28 C ATOM 1362 CD1 ILE B 65 44.989 56.288 0.328 1.00 29.28 C ATOM 1363 N LYS B 66 44.942 62.359 0.096 1.00 32.12 N ATOM 1364 CA LYS B 66 45.261 63.615 0.764 1.00 34.36 C ATOM 1365 C LYS B 66 44.308 64.046 1.881 1.00 35.58 C ATOM 1366 O LYS B 66 43.091 64.094 1.693 1.00 35.20 O ATOM 1367 CB LYS B 66 45.346 64.742 −0.285 1.00 35.36 C ATOM 1368 CG LYS B 66 45.677 66.133 0.280 1.00 35.59 C ATOM 1369 CD LYS B 66 45.638 67.209 −0.796 1.00 36.13 C ATOM 1370 CE LYS B 66 46.129 68.554 −0.264 1.00 38.60 C ATOM 1371 NZ LYS B 66 46.176 69.640 −1.304 1.00 37.62 N ATOM 1372 N GLY B 67 44.871 64.365 3.046 1.00 37.05 N ATOM 1373 CA GLY B 67 44.056 64.837 4.155 1.00 38.88 C ATOM 1374 C GLY B 67 43.676 66.283 3.856 1.00 40.81 C ATOM 1375 O GLY B 67 44.544 67.157 3.780 1.00 40.56 O ATOM 1376 N VAL B 68 42.387 66.542 3.667 1.00 41.60 N ATOM 1377 CA VAL B 68 41.929 67.886 3.343 1.00 43.50 C ATOM 1378 C VAL B 68 42.352 68.934 4.371 1.00 44.85 C ATOM 1379 O VAL B 68 42.928 69.957 4.000 1.00 45.14 O ATOM 1380 CB VAL B 68 40.391 67.930 3.175 1.00 44.16 C ATOM 1381 CG1 VAL B 68 39.946 69.329 2.778 1.00 44.07 C ATOM 1382 CG2 VAL B 68 39.958 66.927 2.101 1.00 45.02 C ATOM 1383 N SER B 69 42.080 68.683 5.651 1.00 45.53 N ATOM 1384 CA SER B 69 42.448 69.632 6.709 1.00 46.56 C ATOM 1385 C SER B 69 43.952 69.817 6.842 1.00 46.50 C ATOM 1386 O SER B 69 44.451 70.938 6.752 1.00 46.70 O ATOM 1387 CB SER B 69 41.880 69.193 8.062 1.00 47.39 C ATOM 1388 OG SER B 69 40.546 69.648 8.225 1.00 48.53 O ATOM 1389 N ALA B 70 44.668 68.717 7.059 1.00 46.13 N ATOM 1390 CA ALA B 70 46.116 68.768 7.212 1.00 46.16 C ATOM 1391 C ALA B 70 46.831 69.248 5.946 1.00 46.37 C ATOM 1392 O ALA B 70 47.985 69.674 6.004 1.00 46.38 O ATOM 1393 CB ALA B 70 46.641 67.397 7.612 1.00 45.59 C ATOM 1394 N ASN B 71 46.141 69.181 4.810 1.00 46.18 N ATOM 1395 CA ASN B 71 46.716 69.580 3.530 1.00 46.20 C ATOM 1396 C ASN B 71 48.020 68.816 3.275 1.00 45.29 C ATOM 1397 O ASN B 71 48.998 69.373 2.780 1.00 44.85 O ATOM 1398 CB ASN B 71 46.967 71.094 3.501 1.00 47.58 C ATOM 1399 CG ASN B 71 47.420 71.591 2.129 1.00 49.28 C ATOM 1400 OD1 ASN B 71 46.896 71.171 1.090 1.00 50.06 O ATOM 1401 ND2 ASN B 71 48.388 72.504 2.123 1.00 49.96 N ATOM 1402 N ARG B 72 48.012 67.531 3.618 1.00 44.62 N ATOM 1403 CA ARG B 72 49.169 66.654 3.443 1.00 43.83 C ATOM 1404 C ARG B 72 48.766 65.366 2.719 1.00 43.20 C ATOM 1405 O ARG B 72 47.586 65.001 2.702 1.00 42.97 O ATOM 1406 CB ARG B 72 49.764 66.296 4.805 1.00 44.52 C ATOM 1407 CG ARG B 72 50.427 67.453 5.555 1.00 45.96 C ATOM 1408 CD ARG B 72 50.762 67.031 6.984 1.00 47.04 C ATOM 1409 NE ARG B 72 51.594 68.003 7.687 1.00 47.76 N ATOM 1410 CZ ARG B 72 52.921 68.062 7.593 1.00 48.23 C ATOM 1411 NH1 ARG B 72 53.575 67.199 6.831 1.00 46.93 N ATOM 1412 NH2 ARG B 72 53.593 68.996 8.256 1.00 48.72 N ATOM 1413 N TYR B 73 49.752 64.681 2.134 1.00 41.62 N ATOM 1414 CA TYR B 73 49.518 63.435 1.401 1.00 40.58 C ATOM 1415 C TYR B 73 50.020 62.208 2.156 1.00 39.99 C ATOM 1416 O TYR B 73 51.160 62.185 2.633 1.00 39.66 O ATOM 1417 CB TYR B 73 50.215 63.446 0.029 1.00 40.09 C ATOM 1418 CG TYR B 73 49.784 64.535 −0.919 1.00 40.53 C ATOM 1419 CD1 TYR B 73 50.373 65.807 −0.872 1.00 40.88 C ATOM 1420 CD2 TYR B 73 48.781 64.304 −1.863 1.00 40.46 C ATOM 1421 CE1 TYR B 73 49.971 66.826 −1.747 1.00 40.70 C ATOM 1422 CE2 TYR B 73 48.368 65.313 −2.739 1.00 40.89 C ATOM 1423 CZ TYR B 73 48.966 66.573 −2.673 1.00 40.86 C ATOM 1424 OH TYR B 73 48.535 67.573 −3.511 1.00 40.19 O ATOM 1425 N LEU B 74 49.179 61.180 2.244 1.00 38.79 N ATOM 1426 CA LEU B 74 49.558 59.939 2.919 1.00 37.94 C ATOM 1427 C LEU B 74 50.758 59.334 2.211 1.00 38.53 C ATOM 1428 O LEU B 74 50.857 59.391 0.985 1.00 38.81 O ATOM 1429 CB LEU B 74 48.416 58.926 2.890 1.00 36.70 C ATOM 1430 CG LEU B 74 48.709 57.584 3.569 1.00 36.84 C ATOM 1431 CD1 LEU B 74 48.555 57.742 5.082 1.00 35.17 C ATOM 1432 CD2 LEU B 74 47.747 56.508 3.052 1.00 35.08 C ATOM 1433 N ALA B 75 51.668 58.748 2.981 1.00 39.29 N ATOM 1434 CA ALA B 75 52.854 58.131 2.402 1.00 40.25 C ATOM 1435 C ALA B 75 53.373 56.988 3.262 1.00 40.75 C ATOM 1436 O ALA B 75 53.151 56.962 4.467 1.00 39.83 O ATOM 1437 CB ALA B 75 53.948 59.180 2.223 1.00 40.32 C ATOM 1438 N MET B 76 54.047 56.035 2.632 1.00 42.15 N ATOM 1439 CA MET B 76 54.620 54.920 3.365 1.00 44.74 C ATOM 1440 C MET B 76 56.129 54.945 3.143 1.00 45.67 C ATOM 1441 O MET B 76 56.600 54.917 2.000 1.00 44.81 O ATOM 1442 CB MET B 76 54.050 53.580 2.898 1.00 45.53 C ATOM 1443 CG MET B 76 54.433 52.434 3.831 1.00 47.11 C ATOM 1444 SD MET B 76 54.068 50.811 3.162 1.00 50.36 S ATOM 1445 CE MET B 76 52.275 50.720 3.489 1.00 49.90 C ATOM 1446 N LYS B 77 56.873 55.014 4.246 1.00 47.14 N ATOM 1447 CA LYS B 77 58.335 55.069 4.215 1.00 48.96 C ATOM 1448 C LYS B 77 58.982 53.702 3.985 1.00 49.89 C ATOM 1449 O LYS B 77 58.306 52.670 3.990 1.00 50.27 O ATOM 1450 CB LYS B 77 58.856 55.684 5.520 1.00 48.58 C ATOM 1451 N GLU B 78 60.295 53.707 3.783 1.00 51.15 N ATOM 1452 CA GLU B 78 61.064 52.485 3.535 1.00 52.23 C ATOM 1453 C GLU B 78 60.975 51.445 4.660 1.00 52.96 C ATOM 1454 O GLU B 78 61.069 50.241 4.408 1.00 53.35 O ATOM 1455 CB GLU B 78 62.536 52.844 3.295 1.00 52.49 C ATOM 1456 N ASP B 79 60.806 51.903 5.897 1.00 53.48 N ATOM 1457 CA ASP B 79 60.717 50.981 7.029 1.00 54.58 C ATOM 1458 C ASP B 79 59.285 50.505 7.272 1.00 54.22 C ATOM 1459 O ASP B 79 59.021 49.776 8.231 1.00 54.69 O ATOM 1460 CB ASP B 79 61.269 51.638 8.302 1.00 55.62 C ATOM 1461 CG ASP B 79 60.462 52.847 8.735 1.00 57.57 C ATOM 1462 OD1 ASP B 79 60.791 53.445 9.785 1.00 58.50 O ATOM 1463 OD2 ASP B 79 59.496 53.204 8.025 1.00 58.63 O ATOM 1464 N GLY B 80 58.365 50.926 6.407 1.00 53.35 N ATOM 1465 CA GLY B 80 56.975 50.522 6.542 1.00 52.30 C ATOM 1466 C GLY B 80 56.125 51.410 7.433 1.00 51.35 C ATOM 1467 O GLY B 80 55.015 51.036 7.795 1.00 51.92 O ATOM 1468 N ARG B 81 56.635 52.583 7.788 1.00 50.11 N ATOM 1469 CA ARG B 81 55.894 53.499 8.643 1.00 49.78 C ATOM 1470 C ARG B 81 55.002 54.422 7.814 1.00 49.47 C ATOM 1471 O ARG B 81 55.314 54.743 6.668 1.00 48.44 O ATOM 1472 CB ARG B 81 56.866 54.342 9.482 1.00 49.85 C ATOM 1473 N LEU B 82 53.891 54.854 8.392 1.00 49.08 N ATOM 1474 CA LEU B 82 52.994 55.743 7.672 1.00 49.61 C ATOM 1475 C LEU B 82 53.087 57.170 8.192 1.00 50.01 C ATOM 1476 O LEU B 82 53.215 57.399 9.398 1.00 50.52 O ATOM 1477 CB LEU B 82 51.547 55.258 7.774 1.00 48.91 C ATOM 1478 CG LEU B 82 51.205 53.963 7.044 1.00 48.88 C ATOM 1479 CD1 LEU B 82 49.688 53.840 6.948 1.00 49.36 C ATOM 1480 CD2 LEU B 82 51.808 53.975 5.646 1.00 48.79 C ATOM 1481 N LEU B 83 53.017 58.126 7.271 1.00 50.25 N ATOM 1482 CA LEU B 83 53.084 59.541 7.615 1.00 50.82 C ATOM 1483 C LEU B 83 52.456 60.346 6.474 1.00 50.21 C ATOM 1484 O LEU B 83 52.188 59.796 5.408 1.00 50.58 O ATOM 1485 CB LEU B 83 54.550 59.951 7.833 1.00 51.37 C ATOM 1486 CG LEU B 83 55.481 59.846 6.619 1.00 52.48 C ATOM 1487 CD1 LEU B 83 55.549 61.204 5.932 1.00 52.74 C ATOM 1488 CD2 LEU B 83 56.876 59.411 7.049 1.00 53.20 C ATOM 1489 N ALA B 84 52.212 61.635 6.703 1.00 49.99 N ATOM 1490 CA ALA B 84 51.611 62.510 5.695 1.00 49.47 C ATOM 1491 C ALA B 84 52.570 63.645 5.311 1.00 49.53 C ATOM 1492 O ALA B 84 52.959 64.458 6.154 1.00 49.13 O ATOM 1493 CB ALA B 84 50.308 63.083 6.224 1.00 49.30 C ATOM 1494 N SER B 85 52.922 63.699 4.029 1.00 49.19 N ATOM 1495 CA SER B 85 53.857 64.686 3.496 1.00 48.95 C ATOM 1496 C SER B 85 53.234 65.961 2.929 1.00 48.92 C ATOM 1497 O SER B 85 52.156 65.931 2.329 1.00 48.79 O ATOM 1498 CB SER B 85 54.712 64.025 2.411 1.00 48.86 C ATOM 1499 OG SER B 85 55.596 64.959 1.822 1.00 50.02 O ATOM 1500 N LYS B 86 53.932 67.080 3.112 1.00 48.52 N ATOM 1501 CA LYS B 86 53.471 68.368 2.604 1.00 48.28 C ATOM 1502 C LYS B 86 53.483 68.336 1.083 1.00 47.46 C ATOM 1503 O LYS B 86 52.561 68.836 0.429 1.00 47.12 O ATOM 1504 CB LYS B 86 54.379 69.500 3.100 1.00 48.99 C ATOM 1505 N SER B 87 54.528 67.747 0.517 1.00 46.34 N ATOM 1506 CA SER B 87 54.618 67.660 −0.929 1.00 46.63 C ATOM 1507 C SER B 87 54.620 66.203 −1.394 1.00 46.03 C ATOM 1508 O SER B 87 55.100 65.309 −0.697 1.00 46.08 O ATOM 1509 CB SER B 87 55.862 68.409 −1.446 1.00 47.20 C ATOM 1510 OG SER B 87 57.069 67.802 −1.015 1.00 47.87 O ATOM 1511 N VAL B 88 54.071 65.986 −2.585 1.00 45.84 N ATOM 1512 CA VAL B 88 53.952 64.665 −3.201 1.00 45.45 C ATOM 1513 C VAL B 88 55.286 64.018 −3.580 1.00 45.49 C ATOM 1514 O VAL B 88 56.091 64.630 −4.273 1.00 45.70 O ATOM 1515 CB VAL B 88 53.097 64.753 −4.495 1.00 45.62 C ATOM 1516 CG1 VAL B 88 52.836 63.359 −5.058 1.00 45.86 C ATOM 1517 CG2 VAL B 88 51.796 65.483 −4.214 1.00 45.53 C ATOM 1518 N THR B 89 55.501 62.780 −3.137 1.00 45.33 N ATOM 1519 CA THR B 89 56.715 62.021 −3.458 1.00 45.47 C ATOM 1520 C THR B 89 56.293 60.648 −3.994 1.00 45.02 C ATOM 1521 O THR B 89 55.106 60.327 −3.991 1.00 44.61 O ATOM 1522 CB THR B 89 57.620 61.829 −2.213 1.00 46.28 C ATOM 1523 OG1 THR B 89 58.562 60.779 −2.465 1.00 47.25 O ATOM 1524 CG2 THR B 89 56.803 61.474 −0.988 1.00 46.77 C ATOM 1525 N ASP B 90 57.242 59.835 −4.452 1.00 44.68 N ATOM 1526 CA ASP B 90 56.878 58.529 −4.992 1.00 45.02 C ATOM 1527 C ASP B 90 56.392 57.533 −3.932 1.00 44.14 C ATOM 1528 O ASP B 90 56.014 56.408 −4.260 1.00 44.94 O ATOM 1529 CB ASP B 90 58.035 57.939 −5.807 1.00 47.23 C ATOM 1530 CG ASP B 90 59.237 57.589 −4.952 1.00 49.81 C ATOM 1531 OD1 ASP B 90 59.609 58.415 −4.089 1.00 51.02 O ATOM 1532 OD2 ASP B 90 59.818 56.494 −5.150 1.00 51.45 O ATOM 1533 N GLU B 91 56.387 57.950 −2.671 1.00 42.82 N ATOM 1534 CA GLU B 91 55.921 57.098 −1.582 1.00 41.44 C ATOM 1535 C GLU B 91 54.472 57.465 −1.236 1.00 40.27 C ATOM 1536 O GLU B 91 53.924 57.007 −0.233 1.00 39.81 O ATOM 1537 CB GLU B 91 56.812 57.292 −0.345 1.00 41.01 C ATOM 1538 N CYS B 92 53.860 58.288 −2.083 1.00 39.09 N ATOM 1539 CA CYS B 92 52.494 58.751 −1.868 1.00 39.00 C ATOM 1540 C CYS B 92 51.448 58.126 −2.801 1.00 37.89 C ATOM 1541 O CYS B 92 50.296 58.568 −2.821 1.00 38.22 O ATOM 1542 CB CYS B 92 52.460 60.278 −2.013 1.00 38.86 C ATOM 1543 SG CYS B 92 53.558 61.163 −0.844 1.00 40.00 S ATOM 1544 N PHE B 93 51.846 57.110 −3.561 1.00 36.66 N ATOM 1545 CA PHE B 93 50.941 56.452 −4.502 1.00 36.71 C ATOM 1546 C PHE B 93 50.664 54.981 −4.148 1.00 36.83 C ATOM 1547 O PHE B 93 51.586 54.218 −3.829 1.00 36.31 O ATOM 1548 CB PHE B 93 51.502 56.566 −5.917 1.00 37.11 C ATOM 1549 CG PHE B 93 51.653 57.984 −6.385 1.00 38.68 C ATOM 1550 CD1 PHE B 93 50.530 58.777 −6.598 1.00 38.20 C ATOM 1551 CD2 PHE B 93 52.919 58.542 −6.573 1.00 38.94 C ATOM 1552 CE1 PHE B 93 50.657 60.111 −6.990 1.00 40.31 C ATOM 1553 CE2 PHE B 93 53.060 59.873 −6.965 1.00 40.19 C ATOM 1554 CZ PHE B 93 51.926 60.662 −7.174 1.00 40.04 C ATOM 1555 N PHE B 94 49.389 54.594 −4.230 1.00 35.09 N ATOM 1556 CA PHE B 94 48.963 53.246 −3.873 1.00 33.74 C ATOM 1557 C PHE B 94 47.995 52.597 −4.863 1.00 33.15 C ATOM 1558 O PHE B 94 47.080 53.244 −5.375 1.00 33.22 O ATOM 1559 CB PHE B 94 48.271 53.275 −2.508 1.00 34.11 C ATOM 1560 CG PHE B 94 49.053 53.979 −1.435 1.00 34.05 C ATOM 1561 CD1 PHE B 94 49.905 53.268 −0.596 1.00 33.30 C ATOM 1562 CD2 PHE B 94 48.946 55.361 −1.271 1.00 33.73 C ATOM 1563 CE1 PHE B 94 50.645 53.924 0.395 1.00 33.49 C ATOM 1564 CE2 PHE B 94 49.681 56.027 −0.287 1.00 33.43 C ATOM 1565 CZ PHE B 94 50.535 55.304 0.550 1.00 32.83 C ATOM 1566 N PHE B 95 48.193 51.311 −5.114 1.00 31.95 N ATOM 1567 CA PHE B 95 47.290 50.575 −5.992 1.00 31.76 C ATOM 1568 C PHE B 95 45.979 50.411 −5.241 1.00 30.17 C ATOM 1569 O PHE B 95 45.963 49.892 −4.134 1.00 29.41 O ATOM 1570 CB PHE B 95 47.828 49.174 −6.308 1.00 32.03 C ATOM 1571 CG PHE B 95 48.937 49.158 −7.303 1.00 33.35 C ATOM 1572 CD1 PHE B 95 50.257 48.999 −6.894 1.00 33.74 C ATOM 1573 CD2 PHE B 95 48.666 49.293 −8.656 1.00 33.65 C ATOM 1574 CE1 PHE B 95 51.293 48.970 −7.824 1.00 33.36 C ATOM 1575 CE2 PHE B 95 49.696 49.267 −9.591 1.00 34.75 C ATOM 1576 CZ PHE B 95 51.014 49.103 −9.172 1.00 33.46 C ATOM 1577 N GLU B 96 44.886 50.870 −5.829 1.00 30.27 N ATOM 1578 CA GLU B 96 43.580 50.729 −5.196 1.00 30.73 C ATOM 1579 C GLU B 96 42.888 49.529 −5.832 1.00 31.15 C ATOM 1580 O GLU B 96 42.816 49.426 −7.052 1.00 30.61 O ATOM 1581 CB GLU B 96 42.725 51.989 −5.401 1.00 28.79 C ATOM 1582 CG GLU B 96 41.360 51.916 −4.708 1.00 29.44 C ATOM 1583 CD GLU B 96 40.476 53.138 −4.981 1.00 29.62 C ATOM 1584 OE1 GLU B 96 40.222 53.415 −6.167 1.00 29.90 O ATOM 1585 OE2 GLU B 96 40.039 53.816 −4.016 1.00 28.37 O ATOM 1586 N ARG B 97 42.380 48.634 −4.996 1.00 32.72 N ATOM 1587 CA ARG B 97 41.711 47.423 −5.470 1.00 35.12 C ATOM 1588 C ARG B 97 40.421 47.108 −4.700 1.00 34.90 C ATOM 1589 O ARG B 97 40.381 47.161 −3.475 1.00 33.69 O ATOM 1590 CB ARG B 97 42.672 46.229 −5.336 1.00 37.75 C ATOM 1591 CG ARG B 97 42.010 44.860 −5.501 1.00 41.93 C ATOM 1592 CD ARG B 97 41.947 44.440 −6.962 1.00 44.56 C ATOM 1593 NE ARG B 97 43.232 43.919 −7.422 1.00 46.30 N ATOM 1594 CZ ARG B 97 43.788 42.800 −6.965 1.00 47.02 C ATOM 1595 NH1 ARG B 97 43.173 42.080 −6.032 1.00 46.95 N ATOM 1596 NH2 ARG B 97 44.959 42.396 −7.446 1.00 46.84 N ATOM 1597 N LEU B 98 39.363 46.795 −5.433 1.00 35.86 N ATOM 1598 CA LEU B 98 38.097 46.407 −4.823 1.00 35.99 C ATOM 1599 C LEU B 98 38.170 44.881 −4.716 1.00 35.59 C ATOM 1600 O LEU B 98 38.142 44.190 −5.729 1.00 36.32 O ATOM 1601 CE LEU B 98 36.927 46.832 −5.715 1.00 35.68 C ATOM 1602 CB LEU B 98 35.532 46.361 −5.272 1.00 36.69 C ATOM 1603 CD1 LEU B 98 35.289 46.724 −3.807 1.00 35.91 C ATOM 1604 CD2 LEU B 98 34.474 46.998 −6.161 1.00 35.80 C ATOM 1605 N GLU B 99 38.294 44.363 −3.501 1.00 36.08 N ATOM 1606 CA GLU B 99 38.399 42.922 −3.296 1.00 36.41 C ATOM 1607 C GLU B 99 37.056 42.216 −3.459 1.00 36.93 C ATOM 1608 O GLU B 99 35.999 42.853 −3.419 1.00 34.85 O ATOM 1609 CB GLU B 99 38.985 42.640 −1.909 1.00 36.69 C ATOM 1610 CG GLU B 99 40.353 43.288 −1.679 1.00 38.44 C ATOM 1611 CD GLU B 99 41.396 42.871 −2.711 1.00 38.96 C ATOM 1612 OE1 GLU B 99 42.465 43.507 −2.752 1.00 39.00 O ATOM 1613 OE2 GLU B 99 41.158 41.912 −3.478 1.00 39.79 O ATOM 1614 N SER B 100 37.109 40.897 −3.639 1.00 37.29 N ATOM 1615 CA SER B 100 35.906 40.089 −3.827 1.00 37.99 C ATOM 1616 C SER B 100 34.949 40.199 −2.642 1.00 37.08 C ATOM 1617 O SER B 100 33.740 39.982 −2.787 1.00 37.34 O ATOM 1618 CB SER B 100 36.285 38.623 −4.080 1.00 37.81 C ATOM 1619 OG SER B 100 37.033 38.093 −3.000 1.00 40.53 O ATOM 1620 N ASN B 101 35.487 40.554 −1.477 1.00 36.07 N ATOM 1621 CA ASN B 101 34.680 40.717 −0.269 1.00 34.55 C ATOM 1622 C ASN B 101 33.980 42.084 −0.230 1.00 33.39 C ATOM 1623 O ASN B 101 33.245 42.387 0.713 1.00 33.54 O ATOM 1624 CB ASN B 101 35.563 40.561 0.965 1.00 35.09 C ATOM 1625 CG ASN B 101 36.845 41.385 0.877 1.00 37.41 C ATOM 1626 OD1 ASN B 101 36.826 42.557 0.489 1.00 35.76 O ATOM 1627 ND2 ASN B 101 37.970 40.772 1.255 1.00 38.82 N ATOM 1628 N ASN B 102 34.215 42.893 −1.261 1.00 31.93 N ATOM 1629 CA ASN B 102 33.636 44.228 −1.395 1.00 30.66 C ATOM 1630 C ASN B 102 34.248 45.338 −0.532 1.00 30.24 C ATOM 1631 O ASN B 102 33.610 46.376 −0.317 1.00 28.46 O ATOM 1632 CB ASN B 102 32.120 44.197 −1.171 1.00 31.25 C ATOM 1633 CG ASN B 102 31.344 43.869 −2.442 1.00 33.02 C ATOM 1634 OD1 ASN B 102 31.813 44.124 −3.558 1.00 33.52 O ATOM 1635 ND2 ASN B 102 30.141 43.319 −2.277 1.00 32.99 N ATOM 1636 N TYR B 103 35.469 45.112 −0.037 1.00 28.45 N ATOM 1637 CA TYR B 103 36.197 46.126 0.742 1.00 27.56 C ATOM 1638 C TYR B 103 37.332 46.566 −0.167 1.00 27.29 C ATOM 1639 O TYR B 103 37.645 45.865 −1.132 1.00 26.21 O ATOM 1640 CB TYR B 103 36.809 45.546 2.015 1.00 26.19 C ATOM 1641 CG TYR B 103 35.830 45.340 3.127 1.00 26.10 C ATOM 1642 CD1 TYR B 103 35.504 46.387 3.986 1.00 25.93 C ATOM 1643 CD2 TYR B 103 35.239 44.087 3.345 1.00 25.66 C ATOM 1644 CE1 TYR B 103 34.627 46.199 5.031 1.00 25.67 C ATOM 1645 CE2 TYR B 103 34.355 43.891 4.393 1.00 25.55 C ATOM 1646 CZ TYR B 103 34.056 44.951 5.232 1.00 25.68 C ATOM 1647 OH TYR B 103 33.100 44.781 6.276 1.00 26.38 O ATOM 1648 N ASN B 104 37.940 47.714 0.131 1.00 26.26 N ATOM 1649 CA ASN B 104 39.053 48.213 −0.672 1.00 26.34 C ATOM 1650 C ASN B 104 40.394 47.962 0.026 1.00 25.99 C ATOM 1651 O ASN B 104 40.455 47.867 1.254 1.00 26.46 O ATOM 1652 CB ASN B 104 38.926 49.726 −0.890 1.00 27.44 C ATOM 1653 CG ASN B 104 37.931 50.098 −1.986 1.00 28.73 C ATOM 1654 OD1 ASN B 104 37.230 49.240 −2.548 1.00 25.88 O ATOM 1655 ND2 ASN B 104 37.869 51.392 −2.293 1.00 26.81 N ATOM 1656 N THR B 105 41.462 47.849 −0.758 1.00 25.14 N ATOM 1657 CA THR B 105 42.812 47.708 −0.201 1.00 25.17 C ATOM 1658 C THR B 105 43.709 48.719 −0.924 1.00 25.62 C ATOM 1659 O THR B 105 43.472 49.055 −2.086 1.00 24.52 O ATOM 1660 CB THR B 105 43.430 46.315 −0.422 1.00 24.00 C ATOM 1661 OG1 THR B 105 43.387 46.005 −1.815 1.00 22.68 O ATOM 1662 CG2 THR B 105 42.709 45.256 0.405 1.00 24.52 C ATOM 1663 N TYR B 106 44.730 49.200 −0.226 1.00 26.51 N ATOM 1664 CA TYR B 106 45.665 50.176 −0.776 1.00 28.14 C ATOM 1665 C TYR B 106 47.093 49.648 −0.605 1.00 29.96 C ATOM 1666 O TYR B 106 47.626 49.593 0.506 1.00 28.79 O ATOM 1667 CB TYR B 106 45.468 51.518 −0.059 1.00 27.28 C ATOM 1668 CG TYR B 106 44.113 52.112 −0.362 1.00 25.83 C ATOM 1669 CD1 TYR B 106 43.872 52.753 −1.585 1.00 25.32 C ATOM 1670 CD2 TYR B 106 43.039 51.929 0.508 1.00 25.16 C ATOM 1671 CE1 TYR B 106 42.587 53.187 −1.937 1.00 26.20 C ATOM 1672 CE2 TYR B 106 41.742 52.355 0.167 1.00 24.66 C ATOM 1673 CZ TYR B 106 41.524 52.976 −1.055 1.00 25.22 C ATOM 1674 OH TYR B 106 40.243 53.336 −1.428 1.00 24.70 O ATOM 1675 N ARG B 107 47.686 49.241 −1.723 1.00 31.88 N ATOM 1676 CA ARG B 107 49.032 48.673 −1.744 1.00 34.65 C ATOM 1677 C ARG B 107 50.066 49.651 −2.341 1.00 34.73 C ATOM 1678 O ARG B 107 49.866 50.185 −3.429 1.00 33.56 O ATOM 1679 CB ARG B 107 48.983 47.365 −2.550 1.00 35.15 C ATOM 1680 CG ARG B 107 50.231 46.500 −2.494 1.00 35.99 C ATOM 1681 CD ARG B 107 49.960 45.150 −3.142 1.00 36.01 C ATOM 1682 NE ARG B 107 49.470 45.273 −4.514 1.00 36.49 N ATOM 1683 CZ ARG B 107 50.233 45.574 −5.560 1.00 37.81 C ATOM 1684 NH1 ARG B 107 51.536 45.782 −5.395 1.00 39.30 N ATOM 1685 NH2 ARG B 107 49.698 45.681 −6.774 1.00 37.32 N ATOM 1686 N SER B 108 51.161 49.866 −1.614 1.00 36.73 N ATOM 1687 CA SER B 108 52.238 50.779 −2.024 1.00 37.70 C ATOM 1688 C SER B 108 52.788 50.470 −3.410 1.00 38.57 C ATOM 1689 O SER B 108 53.150 49.327 −3.698 1.00 38.27 O ATOM 1690 CB SER B 108 53.383 50.725 −1.001 1.00 38.05 C ATOM 1691 OG SER B 108 54.424 51.648 −1.302 1.00 39.50 O ATOM 1692 N ARG B 109 52.853 51.482 −4.278 1.00 39.46 N ATOM 1693 CA ARG B 109 53.392 51.241 −5.608 1.00 40.70 C ATOM 1694 C ARG B 109 54.917 51.140 −5.551 1.00 41.47 C ATOM 1695 O ARG B 109 55.534 50.547 −6.434 1.00 41.17 O ATOM 1696 CB ARG B 109 52.987 52.334 −6.595 1.00 41.24 C ATOM 1697 CG ARG B 109 53.367 51.964 −8.020 1.00 43.16 C ATOM 1698 CD ARG B 109 52.808 52.923 −9.043 1.00 45.10 C ATOM 1699 NE ARG B 109 53.312 54.279 −8.854 1.00 47.60 N ATOM 1700 CZ ARG B 109 53.086 55.279 −9.702 1.00 49.05 C ATOM 1701 NH1 ARG B 109 52.363 55.065 −10.797 1.00 50.36 N ATOM 1702 NH2 ARG B 109 53.575 56.490 −9.459 1.00 49.22 N ATOM 1703 N LYS B 110 55.513 51.715 −4.507 1.00 42.37 N ATOM 1704 CA LYS B 110 56.972 51.676 −4.327 1.00 43.78 C ATOM 1705 C LYS B 110 57.383 50.351 −3.678 1.00 44.19 C ATOM 1706 O LYS B 110 58.136 49.563 −4.263 1.00 44.41 O ATOM 1707 CB LYS B 110 57.436 52.843 −3.447 1.00 42.84 C ATOM 1708 N TYR B 111 56.887 50.124 −2.463 1.00 43.84 N ATOM 1709 CA TYR B 111 57.157 48.898 −1.720 1.00 44.25 C ATOM 1710 C TYR B 111 55.946 48.008 −1.995 1.00 44.80 C ATOM 1711 O TYR B 111 55.039 47.896 −1.165 1.00 45.25 O ATOM 1712 CB TYR B 111 57.263 49.210 −0.226 1.00 43.80 C ATOM 1713 N THR B 112 55.952 47.390 −3.174 1.00 44.95 N ATOM 1714 CA THR B 112 54.860 46.554 −3.668 1.00 45.44 C ATOM 1715 C THR B 112 54.283 45.401 −2.841 1.00 45.64 C ATOM 1716 O THR B 112 53.409 44.677 −3.338 1.00 45.80 O ATOM 1717 CB THR B 112 55.218 45.963 −5.038 1.00 45.80 C ATOM 1718 OG1 THR B 112 56.262 44.997 −4.872 1.00 46.43 O ATOM 1719 CG2 THR B 112 55.676 47.056 −5.990 1.00 45.62 C ATOM 1720 N SER B 113 54.731 45.213 −1.603 1.00 44.63 N ATOM 1721 CA SER B 113 54.188 44.111 −0.813 1.00 44.47 C ATOM 1722 C SER B 113 53.490 44.581 0.452 1.00 43.56 C ATOM 1723 O SER B 113 52.829 43.792 1.125 1.00 43.26 O ATOM 1724 CB SER B 113 55.292 43.132 −0.413 1.00 46.21 C ATOM 1725 OG SER B 113 56.054 43.657 0.663 1.00 48.08 O ATOM 1726 N TRP B 114 53.644 45.860 0.774 1.00 42.13 N ATOM 1727 CA TRP B 114 53.042 46.425 1.975 1.00 41.14 C ATOM 1728 C TRP B 114 51.712 47.153 1.722 1.00 40.23 C ATOM 1729 O TRP B 114 51.519 47.793 0.689 1.00 39.96 O ATOM 1730 CB TRP B 114 54.037 47.380 2.653 1.00 40.97 C ATOM 1731 N TYR B 115 50.815 47.061 2.697 1.00 38.98 N ATOM 1732 CA TYR B 115 49.501 47.676 2.624 1.00 38.33 C ATOM 1733 C TYR B 115 49.276 48.732 3.698 1.00 37.50 C ATOM 1734 O TYR B 115 49.862 48.676 4.779 1.00 38.47 O ATOM 1735 CB TYR B 115 48.403 46.615 2.801 1.00 39.08 C ATOM 1736 CG TYR B 115 48.269 45.613 1.679 1.00 39.03 C ATOM 1737 CD1 TYR B 115 49.141 44.527 1.571 1.00 39.34 C ATOM 1738 CD2 TYR B 115 47.256 45.741 0.731 1.00 39.04 C ATOM 1739 CE1 TYR B 115 49.002 43.587 0.541 1.00 39.95 C ATOM 1740 CE2 TYR B 115 47.107 44.818 −0.296 1.00 39.74 C ATOM 1741 CZ TYR B 115 47.980 43.740 −0.390 1.00 40.53 C ATOM 1742 OH TYR B 115 47.809 42.817 −1.404 1.00 40.54 O ATOM 1743 N VAL B 116 48.415 49.693 3.390 1.00 36.06 N ATOM 1744 CA VAL B 116 48.036 50.721 4.345 1.00 35.08 C ATOM 1745 C VAL B 116 47.151 49.925 5.296 1.00 36.04 C ATOM 1746 O VAL B 116 46.270 49.188 4.848 1.00 36.69 O ATOM 1747 CB VAL B 116 47.181 51.821 3.669 1.00 33.88 C ATOM 1748 CG1 VAL B 116 46.617 52.776 4.713 1.00 32.43 C ATOM 1749 CG2 VAL B 116 48.021 52.570 2.655 1.00 33.57 C ATOM 1750 N ALA B 117 47.368 50.059 6.595 1.00 36.87 N ATOM 1751 CA ALA B 117 46.574 49.300 7.542 1.00 38.16 C ATOM 1752 C ALA B 117 46.555 49.898 8.934 1.00 38.91 C ATOM 1753 O ALA B 117 47.447 50.655 9.317 1.00 39.19 O ATOM 1754 CB ALA B 117 47.093 47.863 7.600 1.00 39.05 C ATOM 1755 N LEU B 118 45.520 49.550 9.687 1.00 40.06 N ATOM 1756 CA LEU B 118 45.357 50.030 11.051 1.00 40.46 C ATOM 1757 C LEU B 118 45.278 48.843 11.995 1.00 41.64 C ATOM 1758 O LEU B 118 44.795 47.778 11.607 1.00 42.32 O ATOM 1759 CB LEU B 118 44.083 50.856 11.170 1.00 40.02 C ATOM 1760 CG LEU B 118 44.095 52.196 10.434 1.00 40.80 C ATOM 1761 CD1 LEU B 118 42.780 52.926 10.683 1.00 39.59 C ATOM 1762 CD2 LEU B 118 45.267 53.038 10.928 1.00 40.69 C ATOM 1763 N LYS B 119 45.751 49.027 13.227 1.00 42.66 N ATOM 1764 CA LYS B 119 45.727 47.972 14.238 1.00 43.23 C ATOM 1765 C LYS B 119 44.458 48.088 15.072 1.00 43.75 C ATOM 1766 O LYS B 119 43.825 49.146 15.111 1.00 43.74 O ATOM 1767 CB LYS B 119 46.955 48.083 15.157 1.00 43.19 C ATOM 1768 N ARG B 120 44.093 47.000 15.747 1.00 44.61 N ATOM 1769 CA ARG B 120 42.896 46.980 16.583 1.00 44.95 C ATOM 1770 C ARG B 120 42.940 48.066 17.647 1.00 45.06 C ATOM 1771 O ARG B 120 41.909 48.441 18.204 1.00 45.18 O ATOM 1772 CB ARG B 120 42.734 45.606 17.250 1.00 44.61 C ATOM 1773 N THR B 121 44.135 48.583 17.913 1.00 45.91 N ATOM 1774 CA THR B 121 44.321 49.618 18.924 1.00 46.59 C ATOM 1775 C THR B 121 43.972 51.004 18.404 1.00 47.17 C ATOM 1776 O THR B 121 43.613 51.891 19.177 1.00 47.58 O ATOM 1777 CB THR B 121 45.778 49.672 19.405 1.00 47.28 C ATOM 1778 OG1 THR B 121 46.562 50.406 18.454 1.00 48.03 O ATOM 1779 CG2 THR B 121 46.352 48.258 19.546 1.00 47.34 C ATOM 1780 N GLY B 122 44.089 51.196 17.096 1.00 47.80 N ATOM 1781 CA GLY B 122 43.794 52.496 16.525 1.00 48.54 C ATOM 1782 C GLY B 122 45.062 53.138 15.988 1.00 48.99 C ATOM 1783 O GLY B 122 45.037 54.237 15.424 1.00 49.05 O ATOM 1784 N GLN B 123 46.183 52.455 16.182 1.00 49.01 N ATOM 1785 CA GLN B 123 47.464 52.944 15.696 1.00 48.87 C ATOM 1786 C GLN B 123 47.693 52.235 14.371 1.00 48.83 C ATOM 1787 O GLN B 123 47.209 51.120 14.173 1.00 48.65 O ATOM 1788 CB GLN B 123 48.581 52.600 16.687 1.00 48.91 C ATOM 1789 N TYR B 124 48.415 52.874 13.457 1.00 48.90 N ATOM 1790 CA TYR B 124 48.660 52.250 12.166 1.00 48.84 C ATOM 1791 C TYR B 124 49.484 50.992 12.359 1.00 48.25 C ATOM 1792 O TYR B 124 50.020 50.755 13.436 1.00 47.23 O ATOM 1793 CB TYR B 124 49.361 53.225 11.204 1.00 50.36 C ATOM 1794 CG TYR B 124 50.824 53.505 11.482 1.00 52.03 C ATOM 1795 CD1 TYR B 124 51.801 52.541 11.233 1.00 52.58 C ATOM 1796 CD2 TYR B 124 51.237 54.754 11.949 1.00 53.04 C ATOM 1797 CE1 TYR B 124 53.151 52.811 11.437 1.00 53.50 C ATOM 1798 CE2 TYR B 124 52.588 55.035 12.155 1.00 53.93 C ATOM 1799 CZ TYR B 124 53.537 54.056 11.894 1.00 53.72 C ATOM 1800 OH TYR B 124 54.874 54.326 12.074 1.00 54.97 O ATOM 1801 N LYS B 125 49.572 50.182 11.313 1.00 48.10 N ATOM 1802 CA LYS B 125 50.325 48.943 11.368 1.00 48.65 C ATOM 1803 C LYS B 125 51.458 48.994 10.349 1.00 49.32 C ATOM 1804 O LYS B 125 51.242 49.359 9.192 1.00 49.64 O ATOM 1805 CB LYS B 125 49.395 47.771 11.067 1.00 48.68 C ATOM 1806 CG LYS B 125 50.039 46.410 11.184 1.00 48.74 C ATOM 1807 CD LYS B 125 48.991 45.310 11.063 1.00 48.23 C ATOM 1808 CE LYS B 125 49.618 43.930 11.202 1.00 48.26 C ATOM 1809 NZ LYS B 125 48.602 42.842 11.144 1.00 47.68 N ATOM 1810 N LEU B 126 52.664 48.638 10.783 1.00 50.14 N ATOM 1811 CA LEU B 126 53.829 48.655 9.910 1.00 50.56 C ATOM 1812 C LEU B 126 53.538 47.927 8.616 1.00 51.34 C ATOM 1813 O LEU B 126 53.103 46.778 8.630 1.00 52.07 O ATOM 1814 CB LEU B 126 55.023 47.996 10.603 1.00 51.34 C ATOM 1815 N GLY B 127 53.783 48.593 7.494 1.00 51.69 N ATOM 1816 CA GLY B 127 53.541 47.967 6.211 1.00 52.65 C ATOM 1817 C GLY B 127 54.206 46.608 6.088 1.00 53.66 C ATOM 1818 O GLY B 127 53.682 45.708 5.431 1.00 54.03 O ATOM 1819 N SER B 128 55.361 46.454 6.728 1.00 54.20 N ATOM 1820 CA SER B 128 56.113 45.204 6.680 1.00 54.84 C ATOM 1821 C SER B 128 55.397 44.040 7.365 1.00 54.63 C ATOM 1822 O SER B 128 55.717 42.878 7.118 1.00 54.52 O ATOM 1823 CB SER B 128 57.481 45.409 7.334 1.00 56.09 C ATOM 1824 OG SER B 128 57.335 45.937 8.642 1.00 57.87 O ATOM 1825 N LYS B 129 54.433 44.358 8.225 1.00 54.30 N ATOM 1826 CA LYS B 129 53.674 43.344 8.962 1.00 53.71 C ATOM 1827 C LYS B 129 52.300 43.070 8.350 1.00 53.01 C ATOM 1828 O LYS B 129 51.460 42.427 8.985 1.00 52.53 O ATOM 1829 CB LYS B 129 53.407 43.802 10.392 1.00 54.98 C ATOM 1830 CG LYS B 129 54.592 44.193 11.231 1.00 55.83 C ATOM 1831 CD LYS B 129 54.083 44.822 12.529 1.00 56.88 C ATOM 1832 CE LYS B 129 53.071 43.917 13.240 1.00 57.58 C ATOM 1833 NZ LYS B 129 52.452 44.575 14.433 1.00 58.18 N ATOM 1834 N THR B 130 52.055 43.567 7.143 1.00 51.75 N ATOM 1835 CA THR B 130 50.757 43.373 6.511 1.00 50.23 C ATOM 1836 C THR B 130 50.762 42.235 5.502 1.00 50.55 C ATOM 1837 O THR B 130 51.814 41.848 4.989 1.00 50.97 O ATOM 1838 CB THR B 130 50.285 44.656 5.800 1.00 49.10 C ATOM 1839 OG1 THR B 130 51.169 44.953 4.713 1.00 47.52 O ATOM 1840 CG2 THR B 130 50.258 45.826 6.771 1.00 47.14 C ATOM 1841 N GLY B 131 49.570 41.712 5.223 1.00 50.29 N ATOM 1842 CA GLY B 131 49.421 40.618 4.282 1.00 50.10 C ATOM 1843 C GLY B 131 48.043 40.655 3.649 1.00 50.39 C ATOM 1844 O GLY B 131 47.115 41.205 4.241 1.00 50.38 O ATOM 1845 N PRO B 132 47.871 40.063 2.457 1.00 50.68 N ATOM 1846 CA PRO B 132 46.598 40.031 1.729 1.00 51.12 C ATOM 1847 C PRO B 132 45.353 39.484 2.429 1.00 51.40 C ATOM 1848 O PRO B 132 44.229 39.882 2.090 1.00 52.15 O ATOM 1849 CB PRO B 132 46.946 39.262 0.448 1.00 51.15 C ATOM 1850 CG PRO B 132 48.128 38.453 0.826 1.00 50.96 C ATOM 1851 CD PRO B 132 48.924 39.390 1.684 1.00 50.86 C ATOM 1852 N GLY B 133 45.529 38.605 3.408 1.00 50.66 N ATOM 1853 CA GLY B 133 44.365 38.051 4.078 1.00 49.54 C ATOM 1854 C GLY B 133 44.015 38.694 5.404 1.00 49.16 C ATOM 1855 O GLY B 133 43.060 38.275 6.061 1.00 49.29 O ATOM 1856 N GLN B 134 44.775 39.713 5.800 1.00 48.04 N ATOM 1857 CA GLN B 134 44.543 40.394 7.072 1.00 45.89 C ATOM 1858 C GLN B 134 43.307 41.294 7.090 1.00 44.66 C ATOM 1859 O GLN B 134 42.874 41.813 6.061 1.00 44.65 O ATOM 1860 CB GLN B 134 45.777 41.230 7.462 1.00 46.36 C ATOM 1861 CG GLN B 134 47.047 40.425 7.737 1.00 45.77 C ATOM 1862 CD GLN B 134 48.201 41.282 8.269 1.00 45.99 C ATOM 1863 OE1 GLN B 134 48.006 42.415 8.705 1.00 45.33 O ATOM 1864 NE2 GLN B 134 49.405 40.725 8.250 1.00 45.77 N ATOM 1865 N LYS B 135 42.762 41.474 8.287 1.00 42.83 N ATOM 1866 CA LYS B 135 41.592 42.302 8.531 1.00 41.46 C ATOM 1867 C LYS B 135 42.004 43.784 8.630 1.00 40.03 C ATOM 1868 O LYS B 135 41.193 44.689 8.403 1.00 39.14 O ATOM 1869 CB LYS B 135 40.960 41.825 9.837 1.00 41.75 C ATOM 1870 CG LYS B 135 39.757 42.577 10.320 1.00 43.82 C ATOM 1871 CD LYS B 135 39.174 41.833 11.529 1.00 45.84 C ATOM 1872 CE LYS B 135 38.116 42.655 12.241 1.00 46.02 C ATOM 1873 NZ LYS B 135 37.055 43.059 11.288 1.00 47.20 N ATOM 1874 N ALA B 136 43.274 44.014 8.959 1.00 37.66 N ATOM 1875 CA ALA B 136 43.815 45.360 9.120 1.00 36.75 C ATOM 1876 C ALA B 136 43.970 46.171 7.824 1.00 34.98 C ATOM 1877 O ALA B 136 44.069 47.398 7.880 1.00 35.66 O ATOM 1878 CB ALA B 136 45.152 45.287 9.851 1.00 36.88 C ATOM 1879 N ILE B 137 43.981 45.504 6.670 1.00 32.94 N ATOM 1880 CA ILE B 137 44.122 46.198 5.389 1.00 31.61 C ATOM 1881 C ILE B 137 42.798 46.482 4.660 1.00 30.44 C ATOM 1882 O ILE B 137 42.809 47.069 3.570 1.00 29.05 O ATOM 1883 CB ILE B 137 45.015 45.402 4.389 1.00 31.44 C ATOM 1884 CG1 ILE B 137 44.243 44.200 3.829 1.00 32.15 C ATOM 1885 CG2 ILE B 137 46.284 44.901 5.087 1.00 32.82 C ATOM 1886 CD1 ILE B 137 45.055 43.337 2.865 1.00 30.55 C ATOM 1887 N LEU B 138 41.672 46.081 5.249 1.00 28.88 N ATOM 1888 CA LEU B 138 40.374 46.272 4.591 1.00 28.50 C ATOM 1889 C LEU B 138 39.662 47.565 4.957 1.00 27.52 C ATOM 1890 O LEU B 138 39.334 47.800 6.122 1.00 27.00 O ATOM 1891 CB LEU B 138 39.466 45.067 4.874 1.00 26.78 C ATOM 1892 CG LEU B 138 40.140 43.738 4.484 1.00 27.13 C ATOM 1893 CD1 LEU B 138 39.256 42.552 4.855 1.00 27.13 C ATOM 1894 CD2 LEU B 138 40.417 43.722 2.990 1.00 25.65 C ATOM 1895 N PHE B 139 39.433 48.407 3.950 1.00 26.87 N ATOM 1896 CA PHE B 139 38.753 49.683 4.162 1.00 26.76 C ATOM 1897 C PHE B 139 37.482 49.836 3.318 1.00 27.04 C ATOM 1898 O PHE B 139 37.370 49.311 2.210 1.00 26.13 O ATOM 1899 CB PHE B 139 39.686 50.863 3.852 1.00 27.83 C ATOM 1900 CG PHE B 139 40.900 50.946 4.746 1.00 29.10 C ATOM 1901 CD1 PHE B 139 42.021 50.139 4.513 1.00 28.33 C ATOM 1902 CD2 PHE B 139 40.917 51.825 5.835 1.00 28.94 C ATOM 1903 CE1 PHE B 139 43.144 50.214 5.363 1.00 28.98 C ATOM 1904 CE2 PHE B 139 42.033 51.904 6.687 1.00 27.99 C ATOM 1905 CZ PHE B 139 43.142 51.102 6.453 1.00 27.54 C ATOM 1906 N LEU B 140 36.536 50.597 3.850 1.00 27.21 N ATOM 1907 CA LEU B 140 35.287 50.856 3.162 1.00 27.69 C ATOM 1908 C LEU B 140 35.169 52.353 2.947 1.00 28.23 C ATOM 1909 O LEU B 140 35.067 53.112 3.910 1.00 29.52 O ATOM 1910 CB LEU B 140 34.113 50.362 4.017 1.00 27.73 C ATOM 1911 CG LEU B 140 32.709 50.495 3.427 1.00 28.01 C ATOM 1912 CD1 LEU B 140 32.632 49.651 2.161 1.00 29.66 C ATOM 1913 CD2 LEU B 140 31.660 50.033 4.435 1.00 27.06 C ATOM 1914 N PRO B 141 35.186 52.811 1.688 1.00 29.04 N ATOM 1915 CA PRO B 141 35.069 54.255 1.461 1.00 30.00 C ATOM 1916 C PRO B 141 33.656 54.740 1.805 1.00 31.46 C ATOM 1917 O PRO B 141 32.664 54.133 1.391 1.00 31.39 O ATOM 1918 CB PRO B 141 35.398 54.395 −0.023 1.00 29.25 C ATOM 1919 CG PRO B 141 34.816 53.137 −0.603 1.00 30.27 C ATOM 1920 CD PRO B 141 35.208 52.068 0.414 1.00 29.01 C ATOM 1921 N MET B 142 33.567 55.818 2.574 1.00 32.79 N ATOM 1922 CA MET B 142 32.274 56.367 2.970 1.00 34.51 C ATOM 1923 C MET B 142 32.197 57.862 2.712 1.00 35.90 C ATOM 1924 O MET B 142 33.222 58.551 2.660 1.00 36.05 O ATOM 1925 CB MET B 142 32.019 56.111 4.452 1.00 34.55 C ATOM 1926 CG MET B 142 32.004 54.649 4.832 1.00 34.06 C ATOM 1927 SD MET B 142 31.760 54.424 6.588 1.00 34.95 S ATOM 1928 CE MET B 142 29.969 54.769 6.691 1.00 34.56 C ATOM 1929 N SER B 143 30.977 58.364 2.568 1.00 37.20 N ATOM 1930 CA SER B 143 30.776 59.781 2.313 1.00 39.33 C ATOM 1931 C SER B 143 31.251 60.661 3.460 1.00 40.56 C ATOM 1932 O SER B 143 31.173 60.287 4.635 1.00 39.42 O ATOM 1933 CB SER B 143 29.306 60.086 2.032 1.00 39.65 C ATOM 1934 OG SER B 143 29.157 61.458 1.708 1.00 41.03 O ATOM 1935 N ALA B 144 31.752 61.836 3.102 1.00 42.73 N ATOM 1936 CA ALA B 144 32.230 62.781 4.098 1.00 45.56 C ATOM 1937 C ALA B 144 31.066 63.652 4.578 1.00 47.26 C ATOM 1938 O ALA B 144 31.263 64.793 4.983 1.00 47.91 O ATOM 1939 CB ALA B 144 33.336 63.641 3.517 1.00 45.31 C ATOM 1940 N LYS B 145 29.856 63.091 4.536 1.00 49.15 N ATOM 1941 CA LYS B 145 28.638 63.782 4.968 1.00 50.17 C ATOM 1942 C LYS B 145 28.504 65.124 4.277 1.00 50.66 C ATOM 1943 O LYS B 145 28.219 65.081 3.063 1.00 51.61 O ATOM 1944 CB LYS B 145 28.629 63.982 6.488 1.00 50.30 C TER 1945 LYS B 145 ATOM 1946 N HIS C 16 18.017 33.163 −14.374 1.00 39.92 N ATOM 1947 CA HIS C 16 18.118 32.023 −13.413 1.00 39.24 C ATOM 1948 C HIS C 16 19.197 31.057 −13.899 1.00 38.21 C ATOM 1949 O HIS C 16 19.142 30.556 −15.026 1.00 37.58 O ATOM 1950 CB HIS C 16 16.770 31.305 −13.295 1.00 40.25 C ATOM 1951 N PHE C 17 20.177 30.801 −13.035 1.00 37.36 N ATOM 1952 CA PHE C 17 21.302 29.928 −13.375 1.00 36.68 C ATOM 1953 C PHE C 17 20.941 28.480 −13.734 1.00 36.31 C ATOM 1954 O PHE C 17 21.665 27.835 −14.494 1.00 35.92 O ATOM 1955 CB PHE C 17 22.360 29.960 −12.250 1.00 35.03 C ATOM 1956 CG PHE C 17 21.919 29.317 −10.956 1.00 34.60 C ATOM 1957 CD1 PHE C 17 22.194 27.974 −10.698 1.00 33.86 C ATOM 1958 CD2 PHE C 17 21.265 30.059 −9.984 1.00 32.80 C ATOM 1959 CE1 PHE C 17 21.826 27.380 −9.478 1.00 34.30 C ATOM 1960 CE2 PHE C 17 20.893 29.480 −8.768 1.00 33.73 C ATOM 1961 CZ PHE C 17 21.177 28.133 −8.513 1.00 33.16 C ATOM 1962 N LYS C 18 19.821 27.985 −13.211 1.00 36.17 N ATOM 1963 CA LYS C 18 19.374 26.617 −13.481 1.00 36.04 C ATOM 1964 C LYS C 18 18.752 26.413 −14.865 1.00 36.36 C ATOM 1965 O LYS C 18 18.632 25.282 −15.334 1.00 37.03 O ATOM 1966 CB LYS C 18 18.375 26.186 −12.407 1.00 35.95 C ATOM 1967 CG LYS C 18 18.991 26.092 −11.027 1.00 36.63 C ATOM 1968 CD LYS C 18 17.981 25.710 −9.966 1.00 37.95 C ATOM 1969 CE LYS C 18 16.931 26.797 −9.778 1.00 38.74 C ATOM 1970 NZ LYS C 18 16.200 26.619 −8.501 1.00 36.65 N ATOM 1971 N ASP C 19 18.351 27.503 −15.513 1.00 36.06 N ATOM 1972 CA ASP C 19 17.746 27.414 −16.835 1.00 35.59 C ATOM 1973 C ASP C 19 18.751 27.158 −17.945 1.00 35.43 C ATOM 1974 O ASP C 19 19.900 27.595 −17.874 1.00 35.20 O ATOM 1975 CB ASP C 19 17.003 28.703 −17.174 1.00 35.67 C ATOM 1976 CG ASP C 19 15.749 28.885 −16.356 1.00 36.38 C ATOM 1977 OD1 ASP C 19 15.225 30.011 −16.343 1.00 33.91 O ATOM 1978 OD2 ASP C 19 15.288 27.894 −15.737 1.00 37.85 O ATOM 1979 N PRO C 20 18.326 26.438 −18.990 1.00 35.49 N ATOM 1980 CA PRO C 20 19.204 26.143 −20.123 1.00 35.29 C ATOM 1981 C PRO C 20 19.551 27.448 −20.834 1.00 35.29 C ATOM 1982 O PRO C 20 18.855 28.448 −20.668 1.00 34.84 O ATOM 1983 CB PRO C 20 18.364 25.193 −20.983 1.00 34.82 C ATOM 1984 CG PRO C 20 16.953 25.511 −20.597 1.00 36.19 C ATOM 1985 CD PRO C 20 17.046 25.713 −19.112 1.00 35.72 C ATOM 1986 N LYS C 21 20.624 27.445 −21.616 1.00 35.72 N ATOM 1987 CA LYS C 21 21.045 28.660 −22.304 1.00 36.28 C ATOM 1988 C LYS C 21 21.677 28.399 −23.648 1.00 36.33 C ATOM 1989 O LYS C 21 22.015 27.265 −23.982 1.00 36.72 O ATOM 1990 CB LYS C 21 22.065 29.434 −21.454 1.00 37.40 C ATOM 1991 CG LYS C 21 21.619 29.715 −20.043 1.00 39.17 C ATOM 1992 CD LYS C 21 22.412 30.816 −19.379 1.00 41.94 C ATOM 1993 CE LYS C 21 21.957 30.947 −17.932 1.00 43.48 C ATOM 1994 NZ LYS C 21 20.497 31.251 −17.926 1.00 43.44 N ATOM 1995 N ARG C 22 21.824 29.465 −24.425 1.00 36.01 N ATOM 1996 CA ARG C 22 22.498 29.373 −25.708 1.00 36.72 C ATOM 1997 C ARG C 22 23.820 30.074 −25.415 1.00 35.60 C ATOM 1998 O ARG C 22 23.848 31.032 −24.642 1.00 35.48 O ATOM 1999 CB ARG C 22 21.772 30.163 −26.805 1.00 38.56 C ATOM 2000 CG ARG C 22 20.285 29.887 −27.004 1.00 41.76 C ATOM 2001 CD ARG C 22 19.823 30.641 −28.247 1.00 44.38 C ATOM 2002 NE ARG C 22 18.376 30.820 −28.357 1.00 47.15 N ATOM 2003 CZ ARG C 22 17.491 29.836 −28.488 1.00 48.90 C ATOM 2004 NH1 ARG C 22 17.887 28.565 −28.519 1.00 49.62 N ATOM 2005 NH2 ARG C 22 16.201 30.131 −28.617 1.00 48.90 N ATOM 2006 N LEU C 23 24.911 29.592 −25.994 1.00 34.26 N ATOM 2007 CA LEU C 23 26.205 30.244 −25.804 1.00 33.19 C ATOM 2008 C LEU C 23 26.579 30.892 −27.121 1.00 32.28 C ATOM 2009 O LEU C 23 26.933 30.214 −28.076 1.00 32.68 O ATOM 2010 CB LEU C 23 27.281 29.238 −25.389 1.00 32.98 C ATOM 2011 CG LEU C 23 27.159 28.667 −23.974 1.00 34.44 C ATOM 2012 CD1 LEU C 23 28.171 27.550 −23.772 1.00 33.80 C ATOM 2013 CD2 LEU C 23 27.363 29.788 −22.950 1.00 33.91 C ATOM 2014 N TYR C 24 26.490 32.214 −27.155 1.00 31.86 N ATOM 2015 CA TYR C 24 26.794 33.003 −28.334 1.00 31.36 C ATOM 2016 C TYR C 24 28.282 33.375 −28.397 1.00 31.57 C ATOM 2017 O TYR C 24 28.843 33.900 −27.436 1.00 32.38 O ATOM 2018 CB TYR C 24 25.903 34.249 −28.311 1.00 29.63 C ATOM 2019 CG TYR C 24 26.319 35.366 −29.231 1.00 28.49 C ATOM 2020 CD1 TYR C 24 27.325 36.257 −28.863 1.00 27.87 C ATOM 2021 CD2 TYR C 24 25.692 35.548 −30.464 1.00 27.27 C ATOM 2022 CE1 TYR C 24 27.698 37.313 −29.697 1.00 26.83 C ATOM 2023 CE2 TYR C 24 26.056 36.592 −31.304 1.00 27.20 C ATOM 2024 CZ TYR C 24 27.064 37.475 −30.911 1.00 27.65 C ATOM 2025 OH TYR C 24 27.433 38.517 −31.732 1.00 26.72 O ATOM 2026 N CYS C 25 28.918 33.101 −29.530 1.00 31.53 N ATOM 2027 CA CYS C 25 30.334 33.415 −29.692 1.00 32.33 C ATOM 2028 C CYS C 25 30.514 34.761 −30.384 1.00 32.74 C ATOM 2029 O CYS C 25 29.984 34.994 −31.471 1.00 31.68 O ATOM 2030 CB CYS C 25 31.038 32.319 −30.498 1.00 31.99 C ATOM 2031 SG CYS C 25 32.835 32.485 −30.543 1.00 31.09 S ATOM 2032 N LYS C 26 31.263 35.647 −29.735 1.00 33.99 N ATOM 2033 CA LYS C 26 31.522 36.972 −30.270 1.00 34.44 C ATOM 2034 C LYS C 26 32.167 36.871 −31.652 1.00 35.28 C ATOM 2035 O LYS C 26 31.939 37.717 −32.521 1.00 35.06 O ATOM 2036 CB LYS C 26 32.442 37.759 −29.336 1.00 34.59 C ATOM 2037 CG LYS C 26 32.498 39.236 −29.715 1.00 35.12 C ATOM 2038 CD LYS C 26 33.420 40.032 −28.820 1.00 35.53 C ATOM 2039 CE LYS C 26 33.366 41.500 −29.176 1.00 35.99 C ATOM 2040 NZ LYS C 26 34.484 42.228 −28.523 1.00 38.19 N ATOM 2041 N ASN C 27 32.968 35.830 −31.854 1.00 35.47 N ATOM 2042 CA ASN C 27 33.631 35.631 −33.141 1.00 35.71 C ATOM 2043 C ASN C 27 32.613 35.163 −34.185 1.00 35.15 C ATOM 2044 O ASN C 27 32.194 34.008 −34.179 1.00 34.98 O ATOM 2045 CB ASN C 27 34.756 34.591 −33.007 1.00 35.80 C ATOM 2046 CG ASN C 27 35.814 34.722 −34.103 1.00 36.24 C ATOM 2047 OD1 ASN C 27 36.616 33.811 −34.331 1.00 35.61 O ATOM 2048 ND2 ASN C 27 35.822 35.865 −34.778 1.00 35.41 N ATOM 2049 N GLY C 28 32.199 36.071 −35.065 1.00 35.40 N ATOM 2050 CA GLY C 28 31.241 35.713 −36.101 1.00 35.14 C ATOM 2051 C GLY C 28 29.775 35.667 −35.683 1.00 35.73 C ATOM 2052 O GLY C 28 28.888 35.664 −36.530 1.00 35.03 O ATOM 2053 N GLY C 29 29.507 35.616 −34.385 1.00 36.14 N ATOM 2054 CA GLY C 29 28.127 35.575 −33.934 1.00 37.01 C ATOM 2055 C GLY C 29 27.434 34.237 −34.116 1.00 37.59 C ATOM 2056 O GLY C 29 26.274 34.193 −34.502 1.00 37.83 O ATOM 2057 N PHE C 30 28.138 33.143 −33.841 1.00 38.16 N ATOM 2058 CA PHE C 30 27.554 31.808 −33.962 1.00 38.35 C ATOM 2059 C PHE C 30 27.167 31.274 −32.580 1.00 38.48 C ATOM 2060 O PHE C 30 27.818 31.582 −31.582 1.00 38.33 O ATOM 2061 CB PHE C 30 28.545 30.803 −34.568 1.00 38.56 C ATOM 2062 CG PHE C 30 29.103 31.195 −35.905 1.00 39.05 C ATOM 2063 CD1 PHE C 30 30.360 31.794 −36.001 1.00 38.90 C ATOM 2064 CD2 PHE C 30 28.415 30.886 −37.077 1.00 39.67 C ATOM 2065 CE1 PHE C 30 30.928 32.070 −37.248 1.00 39.02 C ATOM 2066 CE2 PHE C 30 28.970 31.159 −38.329 1.00 39.02 C ATOM 2067 CZ PHE C 30 30.230 31.750 −38.413 1.00 39.48 C ATOM 2068 N PHE C 31 26.114 30.466 −32.535 1.00 38.05 N ATOM 2069 CA PHE C 31 25.672 29.850 −31.292 1.00 37.96 C ATOM 2070 C PHE C 31 26.334 28.470 −31.244 1.00 38.42 C ATOM 2071 O PHE C 31 26.291 27.725 −32.232 1.00 37.44 O ATOM 2072 CB PHE C 31 24.145 29.680 −31.277 1.00 38.03 C ATOM 2073 CG PHE C 31 23.375 30.975 −31.153 1.00 37.65 C ATOM 2074 CD1 PHE C 31 23.471 31.752 −30.003 1.00 37.96 C ATOM 2075 CD2 PHE C 31 22.553 31.412 −32.185 1.00 37.56 C ATOM 2076 CE1 PHE C 31 22.761 32.949 −29.878 1.00 37.78 C ATOM 2077 CE2 PHE C 31 21.834 32.614 −32.070 1.00 38.65 C ATOM 2078 CZ PHE C 31 21.941 33.380 −30.914 1.00 38.29 C ATOM 2079 N LEU C 32 26.954 28.132 −30.112 1.00 38.14 N ATOM 2080 CA LEU C 32 27.603 26.828 −29.973 1.00 38.60 C ATOM 2081 C LEU C 32 26.556 25.736 −30.182 1.00 38.90 C ATOM 2082 O LEU C 32 25.507 25.754 −29.545 1.00 39.37 O ATOM 2083 CB LEU C 32 28.223 26.684 −28.582 1.00 37.82 C ATOM 2084 CG LEU C 32 29.052 25.416 −28.349 1.00 37.38 C ATOM 2085 CD1 LEU C 32 30.177 25.321 −29.380 1.00 37.14 C ATOM 2086 CD2 LEU C 32 29.626 25.447 −26.948 1.00 37.29 C ATOM 2087 N ARG C 33 26.842 24.784 −31.063 1.00 39.19 N ATOM 2088 CA ARG C 33 25.894 23.705 −31.351 1.00 39.63 C ATOM 2089 C ARG C 33 26.445 22.300 −31.098 1.00 39.73 C ATOM 2090 O ARG C 33 27.573 21.986 −31.476 1.00 39.04 O ATOM 2091 CB ARG C 33 25.411 23.804 −32.807 1.00 38.58 C ATOM 2092 CG ARG C 33 24.505 22.652 −33.232 1.00 38.68 C ATOM 2093 CD ARG C 33 23.823 22.919 −34.566 1.00 37.94 C ATOM 2094 NE ARG C 33 24.768 22.961 −35.678 1.00 39.09 N ATOM 2095 CZ ARG C 33 24.405 23.061 −36.957 1.00 40.38 C ATOM 2096 NH1 ARG C 33 23.113 23.131 −37.277 1.00 40.24 N ATOM 2097 NH2 ARG C 33 25.324 23.094 −37.919 1.00 38.84 N ATOM 2098 N ILE C 34 25.637 21.460 −30.459 1.00 40.70 N ATOM 2099 CA ILE C 34 26.033 20.085 −30.163 1.00 42.62 C ATOM 2100 C ILE C 34 25.067 19.125 −30.867 1.00 44.12 C ATOM 2101 O ILE C 34 23.924 18.952 −30.439 1.00 44.15 O ATOM 2102 CB ILE C 34 26.026 19.823 −28.626 1.00 42.18 C ATOM 2103 CG1 ILE C 34 27.040 20.743 −27.934 1.00 41.54 C ATOM 2104 CG2 ILE C 34 26.371 18.375 −28.330 1.00 40.90 C ATOM 2105 CD1 ILE C 34 27.035 20.641 −26.415 1.00 41.02 C ATOM 2106 N HIS C 35 25.542 18.512 −31.949 1.00 45.92 N ATOM 2107 CA HIS C 35 24.744 17.586 −32.749 1.00 47.90 C ATOM 2108 C HIS C 35 24.515 16.233 −32.079 1.00 48.86 C ATOM 2109 O HIS C 35 25.320 15.783 −31.263 1.00 49.13 O ATOM 2110 CB HIS C 35 25.391 17.383 −34.124 1.00 47.30 C ATOM 2111 N PRO C 36 23.402 15.563 −32.429 1.00 50.20 N ATOM 2112 CA PRO C 36 23.035 14.250 −31.878 1.00 50.77 C ATOM 2113 C PRO C 36 24.143 13.201 −31.992 1.00 51.50 C ATOM 2114 O PRO C 36 24.294 12.349 −31.111 1.00 51.79 O ATOM 2115 CB PRO C 36 21.806 13.867 −32.698 1.00 50.84 C ATOM 2116 CG PRO C 36 21.197 15.190 −33.044 1.00 50.69 C ATOM 2117 CD PRO C 36 22.400 16.016 −33.411 1.00 50.54 C ATOM 2118 N ASP C 37 24.915 13.265 −33.077 1.00 51.91 N ATOM 2119 CA ASP C 37 25.997 12.315 −33.303 1.00 52.62 C ATOM 2120 C ASP C 37 27.313 12.710 −32.644 1.00 52.33 C ATOM 2121 O ASP C 37 28.336 12.051 −32.847 1.00 52.14 O ATOM 2122 CB ASP C 37 26.231 12.111 −34.805 1.00 54.39 C ATOM 2123 CG ASP C 37 26.416 13.416 −35.554 1.00 56.02 C ATOM 2124 OD1 ASP C 37 25.401 14.098 −35.811 1.00 57.55 O ATOM 2125 OD2 ASP C 37 27.573 13.762 −35.881 1.00 57.12 O ATOM 2126 N GLY C 38 27.295 13.793 −31.874 1.00 51.58 N ATOM 2127 CA GLY C 38 28.504 14.214 −31.191 1.00 50.83 C ATOM 2128 C GLY C 38 29.416 15.231 −31.858 1.00 49.91 C ATOM 2129 O GLY C 38 30.478 15.545 −31.319 1.00 50.15 O ATOM 2130 N ARG C 39 29.034 15.750 −33.018 1.00 48.93 N ATOM 2131 CA ARG C 39 29.874 16.745 −33.684 1.00 48.00 C ATOM 2132 C ARG C 39 29.622 18.123 −33.063 1.00 47.21 C ATOM 2133 O ARG C 39 28.508 18.412 −32.614 1.00 47.28 O ATOM 2134 CB ARG C 39 29.571 16.786 −35.186 1.00 47.46 C ATOM 2135 N VAL C 40 30.648 18.968 −33.029 1.00 45.62 N ATOM 2136 CA VAL C 40 30.496 20.302 −32.460 1.00 44.73 C ATOM 2137 C VAL C 40 30.904 21.416 −33.426 1.00 44.34 C ATOM 2138 O VAL C 40 31.996 21.400 −33.993 1.00 43.99 O ATOM 2139 CB VAL C 40 31.310 20.451 −31.139 1.00 44.63 C ATOM 2140 CG1 VAL C 40 31.257 21.892 −30.640 1.00 43.57 C ATOM 2141 CG2 VAL C 40 30.753 19.517 −30.078 1.00 43.53 C ATOM 2142 N ASP C 41 30.006 22.380 −33.603 1.00 43.77 N ATOM 2143 CA ASP C 41 30.242 23.528 −34.479 1.00 44.32 C ATOM 2144 C ASP C 41 29.373 24.703 −34.036 1.00 44.17 C ATOM 2145 O ASP C 41 28.788 24.679 −32.956 1.00 43.13 O ATOM 2146 CB ASP C 41 29.919 23.178 −35.944 1.00 44.59 C ATOM 2147 CG ASP C 41 28.456 22.764 −36.160 1.00 45.17 C ATOM 2148 OD1 ASP C 41 28.115 22.409 −37.313 1.00 45.54 O ATOM 2149 OD2 ASP C 41 27.650 22.789 −35.201 1.00 43.95 O ATOM 2150 N GLY C 42 29.285 25.720 −34.888 1.00 44.09 N ATOM 2151 CA GLY C 42 28.478 26.879 −34.577 1.00 44.88 C ATOM 2152 C GLY C 42 27.509 27.198 −35.701 1.00 45.42 C ATOM 2153 O GLY C 42 27.751 26.837 −36.846 1.00 45.76 O ATOM 2154 N VAL C 43 26.400 27.853 −35.367 1.00 45.71 N ATOM 2155 CA VAL C 43 25.396 28.252 −36.350 1.00 46.21 C ATOM 2156 C VAL C 43 24.751 29.554 −35.922 1.00 46.88 C ATOM 2157 O VAL C 43 24.715 29.879 −34.735 1.00 46.84 O ATOM 2158 CB VAL C 43 24.262 27.209 −36.537 1.00 45.90 C ATOM 2159 CG1 VAL C 43 24.832 25.948 −37.106 1.00 46.54 C ATOM 2160 CG2 VAL C 43 23.533 26.952 −35.223 1.00 44.87 C ATOM 2161 N ARG C 44 24.230 30.289 −36.898 1.00 47.36 N ATOM 2162 CA ARG C 44 23.593 31.572 −36.646 1.00 48.59 C ATOM 2163 C ARG C 44 22.088 31.496 −36.368 1.00 49.22 C ATOM 2164 O ARG C 44 21.530 32.391 −35.731 1.00 49.22 O ATOM 2165 CB ARG C 44 23.829 32.511 −37.838 1.00 48.96 C ATOM 2166 CG ARG C 44 25.285 32.907 −38.098 1.00 49.81 C ATOM 2167 CD ARG C 44 25.352 34.051 −39.117 1.00 50.07 C ATOM 2168 NE ARG C 44 26.646 34.735 −39.135 1.00 51.51 N ATOM 2169 CZ ARG C 44 27.766 34.229 −39.649 1.00 52.44 C ATOM 2170 NH1 ARG C 44 27.765 33.024 −40.199 1.00 53.50 N ATOM 2171 NH2 ARG C 44 28.892 34.931 −39.613 1.00 52.25 N ATOM 2172 N GLU C 45 21.432 30.440 −36.844 1.00 49.98 N ATOM 2173 CA GLU C 45 19.983 30.291 −36.665 1.00 50.43 C ATOM 2174 C GLU C 45 19.553 30.052 −35.214 1.00 50.75 C ATOM 2175 O GLU C 45 19.693 28.950 −34.684 1.00 50.31 O ATOM 2176 CB GLU C 45 19.456 29.157 −37.553 1.00 49.68 C ATOM 2177 N LYS C 46 19.015 31.095 −34.588 1.00 51.13 N ATOM 2178 CA LYS C 46 18.563 31.029 −33.203 1.00 51.85 C ATOM 2179 C LYS C 46 17.496 29.955 −32.975 1.00 52.54 C ATOM 2180 O LYS C 46 17.197 29.598 −31.837 1.00 52.62 O ATOM 2181 CB LYS C 46 18.013 32.393 −32.771 1.00 50.92 C ATOM 2182 N SER C 47 16.940 29.436 −34.062 1.00 53.02 N ATOM 2183 CA SER C 47 15.893 28.422 −33.998 1.00 53.18 C ATOM 2184 C SER C 47 16.393 26.980 −33.894 1.00 52.59 C ATOM 2185 O SER C 47 15.634 26.077 −33.533 1.00 52.38 O ATOM 2186 CB SER C 47 14.998 28.559 −35.234 1.00 53.53 C ATOM 2187 OG SER C 47 14.065 27.500 −35.309 1.00 54.44 O ATOM 2188 N ASP C 48 17.662 26.763 −34.218 1.00 51.97 N ATOM 2189 CA ASP C 48 18.233 25.422 −34.168 1.00 51.11 C ATOM 2190 C ASP C 48 18.029 24.762 −32.809 1.00 50.64 C ATOM 2191 O ASP C 48 18.398 25.322 −31.777 1.00 51.03 O ATOM 2192 CB ASP C 48 19.725 25.466 −34.493 1.00 50.52 C ATOM 2193 CG ASP C 48 20.324 24.084 −34.659 1.00 50.05 C ATOM 2194 OD1 ASP C 48 20.996 23.853 −35.684 1.00 50.30 O ATOM 2195 OD2 ASP C 48 20.123 23.228 −33.773 1.00 49.16 O ATOM 2196 N PRO C 49 17.436 23.555 −32.794 1.00 50.16 N ATOM 2197 CA PRO C 49 17.174 22.800 −31.564 1.00 49.31 C ATOM 2198 C PRO C 49 18.416 22.240 −30.865 1.00 48.74 C ATOM 2199 O PRO C 49 18.332 21.775 −29.724 1.00 48.49 O ATOM 2200 CB PRO C 49 16.242 21.685 −32.036 1.00 49.47 C ATOM 2201 CG PRO C 49 16.703 21.441 −33.442 1.00 49.53 C ATOM 2202 CD PRO C 49 16.876 22.853 −33.964 1.00 49.76 C ATOM 2203 N HIS C 50 19.563 22.281 −31.537 1.00 47.05 N ATOM 2204 CA HIS C 50 20.787 21.755 −30.943 1.00 46.14 C ATOM 2205 C HIS C 50 21.742 22.788 −30.324 1.00 44.53 C ATOM 2206 O HIS C 50 22.917 22.493 −30.093 1.00 44.37 O ATOM 2207 CB HIS C 50 21.525 20.893 −31.972 1.00 46.67 C ATOM 2208 CG HIS C 50 20.718 19.726 −32.451 1.00 48.02 C ATOM 2209 ND1 HIS C 50 20.261 18.741 −31.602 1.00 48.41 N ATOM 2210 CD2 HIS C 50 20.243 19.412 −33.680 1.00 48.11 C ATOM 2211 CE1 HIS C 50 19.537 17.874 −32.285 1.00 48.32 C ATOM 2212 NE2 HIS C 50 19.510 18.257 −33.548 1.00 48.66 N ATOM 2213 N ILE C 51 21.237 23.989 −30.052 1.00 42.64 N ATOM 2214 CA ILE C 51 22.047 25.042 −29.430 1.00 41.45 C ATOM 2215 C ILE C 51 21.567 25.291 −28.001 1.00 40.92 C ATOM 2216 O ILE C 51 22.129 26.113 −27.278 1.00 40.64 O ATOM 2217 CB ILE C 51 21.964 26.382 −30.206 1.00 40.29 C ATOM 2218 CG1 ILE C 51 20.518 26.884 −30.221 1.00 39.12 C ATOM 2219 CG2 ILE C 51 22.506 26.207 −31.617 1.00 39.60 C ATOM 2220 CD1 ILE C 51 20.303 28.100 −31.071 1.00 37.67 C ATOM 2221 N LYS C 52 20.508 24.593 −27.604 1.00 40.16 N ATOM 2222 CA LYS C 52 19.976 24.717 −26.253 1.00 39.24 C ATOM 2223 C LYS C 52 20.881 23.885 −25.346 1.00 37.79 C ATOM 2224 O LYS C 52 20.920 22.669 −25.451 1.00 37.86 O ATOM 2225 CB LYS C 52 18.539 24.200 −26.209 1.00 40.26 C ATOM 2226 CG LYS C 52 17.954 24.113 −24.812 1.00 42.44 C ATOM 2227 CD LYS C 52 16.433 24.038 −24.863 1.00 44.69 C ATOM 2228 CE LYS C 52 15.850 23.890 −23.462 1.00 45.74 C ATOM 2229 NZ LYS C 52 14.364 23.999 −23.484 1.00 47.05 N ATOM 2230 N LEU C 53 21.615 24.550 −24.461 1.00 35.96 N ATOM 2231 CA LEU C 53 22.556 23.865 −23.585 1.00 34.34 C ATOM 2232 C LEU C 53 22.210 23.958 −22.106 1.00 33.68 C ATOM 2233 O LEU C 53 21.478 24.845 −21.674 1.00 34.17 O ATOM 2234 CB LEU C 53 23.958 24.432 −23.815 1.00 33.01 C ATOM 2235 CG LEU C 53 24.375 24.500 −25.285 1.00 33.28 C ATOM 2236 CD1 LEU C 53 25.676 25.300 −25.446 1.00 31.49 C ATOM 2237 CD2 LEU C 53 24.518 23.078 −25.826 1.00 32.99 C ATOM 2238 N GLN C 54 22.748 23.032 −21.328 1.00 32.23 N ATOM 2239 CA GLN C 54 22.496 23.037 −19.903 1.00 31.29 C ATOM 2240 C GLN C 54 23.831 23.018 −19.151 1.00 31.12 C ATOM 2241 O GLN C 54 24.582 22.035 −19.214 1.00 30.63 O ATOM 2242 CB GLN C 54 21.616 21.831 −19.527 1.00 30.23 C ATOM 2243 CG GLN C 54 21.285 21.721 −18.049 1.00 31.21 C ATOM 2244 CD GLN C 54 20.529 22.939 −17.505 1.00 33.60 C ATOM 2245 OE1 GLN C 54 19.359 23.173 −17.841 1.00 33.50 O ATOM 2246 NE2 GLN C 54 21.203 23.721 −16.660 1.00 32.61 N ATOM 2247 N LEU C 55 24.132 24.117 −18.458 1.00 30.81 N ATOM 2248 CA LEU C 55 25.365 24.211 −17.682 1.00 31.21 C ATOM 2249 C LUE C 55 25.113 23.681 −16.280 1.00 30.69 C ATOM 2250 O LEU C 55 24.007 23.796 −15.762 1.00 30.33 O ATOM 2251 CB LEU C 55 25.858 25.662 −17.569 1.00 31.94 C ATOM 2252 CG LEU C 55 26.391 26.397 −18.797 1.00 33.07 C ATOM 2253 CD1 LEU C 55 27.101 27.684 −18.361 1.00 33.51 C ATOM 2254 CD2 LEU C 55 27.369 25.517 −19.516 1.00 34.11 C ATOM 2255 N GLN C 56 26.144 23.107 −15.668 1.00 29.95 N ATOM 2256 CA GLN C 56 26.040 22.572 −14.313 1.00 30.16 C ATOM 2257 C GLN C 56 27.417 22.621 −13.646 1.00 29.98 C ATOM 2258 O GLN C 56 28.396 22.125 −14.193 1.00 28.97 O ATOM 2259 CB GLN C 56 25.525 21.126 −14.338 1.00 30.67 C ATOM 2260 CG GLN C 56 25.592 20.398 −12.979 1.00 30.83 C ATOM 2261 CD GLN C 56 24.680 21.001 −11.919 1.00 32.27 C ATOM 2262 OE1 GLN C 56 23.456 21.059 −12.090 1.00 30.94 O ATOM 2263 NE2 GLN C 56 25.272 21.447 −10.812 1.00 31.22 N ATOM 2264 N ALA C 57 27.489 23.231 −12.468 1.00 30.09 N ATOM 2265 CA ALA C 57 28.761 23.334 −11.762 1.00 31.02 C ATOM 2266 C ALA C 57 29.104 22.006 −11.088 1.00 30.87 C ATOM 2267 O ALA C 57 28.238 21.361 −10.493 1.00 30.82 O ATOM 2268 CB ALA C 57 28.701 24.459 −10.717 1.00 30.35 C ATOM 2269 N GLU C 58 30.368 21.602 −11.186 1.00 31.25 N ATOM 2270 CA GLU C 58 30.831 20.348 −10.583 1.00 31.67 C ATOM 2271 C GLU C 58 31.549 20.697 −9.277 1.00 32.32 C ATOM 2272 O GLU C 58 31.546 19.927 −8.312 1.00 32.40 O ATOM 2273 CB GLU C 58 31.790 19.636 −11.540 1.00 31.38 C ATOM 2274 CG GLU C 58 32.028 18.164 −11.239 1.00 33.29 C ATOM 2275 CD GLU C 58 30.737 17.347 −11.170 1.00 33.63 C ATOM 2276 OE1 GLU C 58 29.779 17.659 −11.907 1.00 32.82 O ATOM 2277 OE2 GLU C 58 30.692 16.378 −10.383 1.00 35.39 O ATOM 2278 N GLU C 59 32.166 21.876 −9.279 1.00 32.68 N ATOM 2279 CA GLU C 59 32.892 22.422 −8.140 1.00 33.77 C ATOM 2280 C GLU C 59 32.978 23.932 −8.400 1.00 33.03 C ATOM 2281 O GLU C 59 32.665 24.395 −9.504 1.00 32.28 O ATOM 2282 CB GLU C 59 34.309 21.807 −8.042 1.00 35.98 C ATOM 2283 CG GLU C 59 35.430 22.589 −8.751 1.00 39.17 C ATOM 2284 CD GLU C 59 36.776 21.852 −8.766 1.00 41.17 C ATOM 2285 OE1 GLU C 59 36.912 20.863 −9.509 1.00 40.92 O ATOM 2286 OE2 GLU C 59 37.706 22.258 −8.036 1.00 43.20 O ATOM 2287 N ARG C 60 33.408 24.699 −7.403 1.00 31.97 N ATOM 2288 CA ARG C 60 33.497 26.146 −7.569 1.00 32.57 C ATOM 2289 C ARG C 60 34.213 26.577 −8.855 1.00 32.05 C ATOM 2290 O ARG C 60 35.356 26.198 −9.095 1.00 31.53 O ATOM 2291 CB ARG C 60 34.184 26.788 −6.353 1.00 34.46 C ATOM 2292 CG ARG C 60 34.301 28.305 −6.462 1.00 36.45 C ATOM 2293 CD ARG C 60 34.748 28.940 −5.157 1.00 39.28 C ATOM 2294 NE ARG C 60 35.277 30.277 −5.390 1.00 43.60 N ATOM 2295 CZ ARG C 60 36.568 30.565 −5.524 1.00 44.35 C ATOM 2296 NH1 ARG C 60 37.488 29.612 −5.440 1.00 45.40 N ATOM 2297 NH2 ARG C 60 36.939 31.813 −5.762 1.00 46.19 N ATOM 2298 N GLY C 61 33.524 27.360 −9.684 1.00 31.00 N ATOM 2299 CA GLY C 61 34.111 27.837 −10.927 1.00 29.64 C ATOM 2300 C GLY C 61 34.347 26.824 −12.049 1.00 29.20 C ATOM 2301 O GLY C 61 34.964 27.159 −13.055 1.00 28.82 O ATOM 2302 N VAL C 62 33.864 25.595 −11.889 1.00 28.84 N ATOM 2303 CA VAL C 62 34.033 24.562 −12.907 1.00 28.12 C ATOM 2304 C VAL C 62 32.683 24.014 −13.363 1.00 28.05 C ATOM 2305 O VAL C 62 31.858 23.613 −12.543 1.00 27.91 O ATOM 2306 CB VAL C 62 34.872 23.389 −12.372 1.00 30.05 C ATOM 2307 CG1 VAL C 62 34.900 22.249 −13.396 1.00 29.55 C ATOM 2308 CG2 VAL C 62 36.290 23.876 −12.058 1.00 31.46 C ATOM 2309 N VAL C 63 32.464 23.975 −14.674 1.00 26.85 N ATOM 2310 CA VAL C 63 31.194 23.489 −15.194 1.00 25.70 C ATOM 2311 C VAL C 63 31.299 22.425 −16.288 1.00 26.60 C ATOM 2312 O VAL C 63 32.358 22.231 −16.906 1.00 25.54 O ATOM 2313 CB VAL C 63 30.347 24.656 −15.794 1.00 25.51 C ATOM 2314 CG1 VAL C 63 30.211 25.805 −14.787 1.00 24.24 C ATOM 2315 CG2 VAL C 63 30.992 25.153 −17.101 1.00 24.50 C ATOM 2316 N SER C 64 30.177 21.737 −16.502 1.00 26.80 N ATOM 2317 CA SER C 64 30.036 20.748 −17.563 1.00 27.74 C ATOM 2318 C SER C 64 28.977 21.384 −18.458 1.00 28.09 C ATOM 2319 O SER C 64 28.063 22.044 −17.961 1.00 28.39 O ATOM 2320 CB SER C 64 29.522 19.405 −17.023 1.00 28.22 C ATOM 2321 OG SER C 64 28.186 19.471 −16.558 1.00 28.00 O ATOM 2322 N ILE C 65 29.101 21.211 −19.766 1.00 28.42 N ATOM 2323 CA ILE C 65 28.144 21.787 −20.701 1.00 29.32 C ATOM 2324 C ILE C 65 27.470 20.666 −21.501 1.00 30.69 C ATOM 2325 O ILE C 65 28.122 19.950 −22.261 1.00 30.99 O ATOM 2326 CB ILE C 65 28.863 22.778 −21.640 1.00 28.28 C ATOM 2327 CG1 ILE C 65 29.612 23.823 −20.797 1.00 27.41 C ATOM 2328 CG2 ILE C 65 27.856 23.442 −22.574 1.00 28.34 C ATOM 2329 CD1 ILE C 65 30.471 24.785 −21.597 1.00 24.84 C ATOM 2330 N LYS C 66 26.161 20.523 −21.333 1.00 32.55 N ATOM 2331 CA LYS C 66 25.421 19.447 −21.995 1.00 34.96 C ATOM 2332 C LYS C 66 24.381 19.875 −23.027 1.00 35.82 C ATOM 2333 O LYS C 66 23.536 20.726 −22.753 1.00 36.26 O ATOM 2334 CB LYS C 66 24.751 18.589 −20.913 1.00 37.11 C ATOM 2335 CG LYS C 66 23.960 17.367 −21.383 1.00 38.86 C ATOM 2336 CD LYS C 66 23.401 16.636 −20.159 1.00 41.20 C ATOM 2337 CE LYS C 66 22.492 15.473 −20.527 1.00 42.68 C ATOM 2338 NZ LYS C 66 21.233 15.954 −21.158 1.00 44.01 N ATOM 2339 N GLY C 67 24.454 19.284 −24.218 1.00 37.05 N ATOM 2340 CA GLY C 67 23.482 19.587 −25.254 1.00 38.80 C ATOM 2341 C GLY C 67 22.191 18.873 −24.883 1.00 40.43 C ATOM 2342 O GLY C 67 22.153 17.645 −24.816 1.00 39.87 O ATOM 2343 N VAL C 68 21.133 19.635 −24.626 1.00 41.85 N ATOM 2344 CA VAL C 68 19.856 19.047 −24.236 1.00 43.71 C ATOM 2345 C VAL C 68 19.313 18.054 −25.264 1.00 44.52 C ATOM 2346 O VAL C 68 18.976 16.921 −24.914 1.00 45.01 O ATOM 2347 CB VAL C 68 18.782 20.142 −23.986 1.00 43.95 C ATOM 2348 CG1 VAL C 68 17.489 19.498 −23.480 1.00 44.00 C ATOM 2349 CG2 VAL C 68 19.297 21.159 −22.969 1.00 44.05 C ATOM 2350 N SER C 69 19.232 18.472 −26.527 1.00 45.03 N ATOM 2351 CA SER C 69 18.714 17.599 −27.585 1.00 45.87 C ATOM 2352 C SER C 69 19.587 16.361 −27.804 1.00 45.68 C ATOM 2353 O SER C 69 19.114 15.227 −27.700 1.00 45.84 O ATOM 2354 CB SER C 69 18.575 18.378 −28.901 1.00 44.99 C ATOM 2355 N ALA C 70 20.864 16.588 −28.093 1.00 45.74 N ATOM 2356 CA ALA C 70 21.806 15.505 −28.334 1.00 45.43 C ATOM 2357 C ALA C 70 22.010 14.612 −27.115 1.00 45.74 C ATOM 2358 O ALA C 70 22.471 13.481 −27.242 1.00 46.07 O ATOM 2359 CB ALA C 70 23.135 16.081 −28.770 1.00 46.08 C ATOM 2360 N ASN C 71 21.661 15.122 −25.937 1.00 45.57 N ATOM 2361 CA ASN C 71 21.838 14.385 −24.690 1.00 45.32 C ATOM 2362 C ASN C 71 23.301 13.946 −24.532 1.00 44.61 C ATOM 2363 O ASN C 71 23.583 12.835 −24.070 1.00 44.13 O ATOM 2364 CB ASN C 71 20.911 13.160 −24.637 1.00 45.62 C ATOM 2365 CG ASN C 71 20.814 12.557 −23.236 1.00 46.15 C ATOM 2366 OD1 ASN C 71 20.546 13.264 −22.254 1.00 46.61 O ATOM 2367 ND2 ASN C 71 21.020 11.245 −23.140 1.00 45.81 N ATOM 2368 N ARG C 72 24.221 14.834 −24.917 1.00 43.86 N ATOM 2369 CA ARG C 72 25.662 14.577 −24.824 1.00 43.26 C ATOM 2370 C ARG C 72 26.375 15.733 −24.125 1.00 42.40 C ATOM 2371 O ARG C 72 25.853 16.848 −24.070 1.00 42.22 O ATOM 2372 CB ARG C 72 26.278 14.394 −26.214 1.00 43.88 C ATOM 2373 CG ARG C 72 25.953 13.084 −26.921 1.00 44.93 C ATOM 2374 CD ARG C 72 26.422 13.167 −28.370 1.00 46.45 C ATOM 2375 NE ARG C 72 26.143 11.964 −29.152 1.00 47.61 N ATOM 2376 CZ ARG C 72 27.012 10.977 −29.346 1.00 48.45 C ATOM 2377 NH1 ARG C 72 28.227 11.040 −28.811 1.00 48.67 N ATOM 2378 NH2 ARG C 72 26.671 9.930 −30.091 1.00 48.13 N ATOM 2379 N TYR C 73 27.576 15.457 −23.614 1.00 40.54 N ATOM 2380 CA TYR C 73 28.388 16.443 −22.904 1.00 38.82 C ATOM 2381 C TYR C 73 29.579 16.942 −23.719 1.00 38.37 C ATOM 2382 O TYR C 73 30.329 16.152 −24.289 1.00 37.39 O ATOM 2383 CB TYR C 73 28.899 15.851 −21.586 1.00 37.69 C ATOM 2384 CG TYR C 73 27.804 15.496 −20.602 1.00 37.26 C ATOM 2385 CD1 TYR C 73 27.081 14.305 −20.717 1.00 36.64 C ATOM 2386 CD2 TYR C 73 27.483 16.360 −19.555 1.00 36.86 C ATOM 2387 CE1 TYR C 73 26.066 13.986 −19.806 1.00 37.14 C ATOM 2388 CE2 TYR C 73 26.476 16.054 −18.648 1.00 36.35 C ATOM 2389 CZ TYR C 73 25.771 14.872 −18.776 1.00 36.93 C ATOM 2390 OH TYR C 73 24.762 14.607 −17.880 1.00 36.77 O ATOM 2391 N LEU C 74 29.754 18.259 −23.762 1.00 37.92 N ATOM 2392 CA LEU C 74 30.866 18.866 −24.492 1.00 38.18 C ATOM 2393 C LEU C 74 32.184 18.368 −23.897 1.00 38.61 C ATOM 2394 O LEU C 74 32.295 18.204 −22.685 1.00 38.88 O ATOM 2395 CB LEU C 74 30.797 20.396 −24.376 1.00 38.05 C ATOM 2396 CG LEU C 74 31.824 21.247 −25.131 1.00 38.02 C ATOM 2397 CD1 LEU C 74 31.495 21.250 −26.622 1.00 37.84 C ATOM 2398 CD2 LEU C 74 31.806 22.664 −24.602 1.00 37.13 C ATOM 2399 N ALA C 75 33.178 18.125 −24.744 1.00 39.31 N ATOM 2400 CA ALA C 75 34.475 17.653 −24.274 1.00 40.12 C ATOM 2401 C ALA C 75 35.599 18.081 −25.200 1.00 40.53 C ATOM 2402 O ALA C 75 35.389 18.295 −26.393 1.00 39.68 O ATOM 2403 CB ALA C 75 34.472 16.139 −24.154 1.00 39.77 C ATOM 2404 N MET C 76 36.793 18.215 −24.638 1.00 41.78 N ATOM 2405 CA MET C 76 37.960 18.577 −25.428 1.00 43.24 C ATOM 2406 C MET C 76 38.972 17.445 −25.305 1.00 44.15 C ATOM 2407 O MET C 76 39.382 17.086 −24.200 1.00 43.31 O ATOM 2408 CB MET C 76 38.588 19.870 −24.928 1.00 42.60 C ATOM 2409 CG MET C 76 39.730 20.330 −25.796 1.00 43.03 C ATOM 2410 SD MET C 76 40.561 21.749 −25.111 1.00 43.66 S ATOM 2411 CE MET C 76 39.365 23.044 −25.475 1.00 43.55 C ATOM 2412 N LYS C 77 39.361 16.894 −26.451 1.00 45.65 N ATOM 2413 CA LYS C 77 40.313 15.790 −26.526 1.00 47.16 C ATOM 2414 C LYS C 77 41.769 16.240 −26.378 1.00 48.19 C ATOM 2415 O LYS C 77 42.070 17.436 −26.407 1.00 47.32 O ATOM 2416 CB LYS C 77 40.131 15.075 −27.860 1.00 48.29 C ATOM 2417 CG LYS C 77 38.794 14.376 −28.017 1.00 49.47 C ATOM 2418 CD LYS C 77 38.813 13.040 −27.294 1.00 50.83 C ATOM 2419 CE LYS C 77 37.622 12.185 −27.681 1.00 51.99 C ATOM 2420 NZ LYS C 77 37.832 10.757 −27.326 1.00 52.73 N ATOM 2421 N GLU C 78 42.667 15.267 −26.238 1.00 49.39 N ATOM 2422 CA GLU C 78 44.095 15.528 −26.078 1.00 50.46 C ATOM 2423 C GLU C 78 44.721 16.329 −27.224 1.00 51.02 C ATOM 2424 O GLU C 78 45.667 17.083 −27.006 1.00 51.07 O ATOM 2425 CB GLU C 78 44.850 14.204 −25.903 1.00 50.91 C ATOM 2426 N ASP C 79 44.200 16.169 −28.438 1.00 51.94 N ATOM 2427 CA ASP C 79 44.732 16.894 −29.593 1.00 52.77 C ATOM 2428 C ASP C 79 44.094 18.271 −29.747 1.00 52.81 C ATOM 2429 O ASP C 79 44.385 18.993 −30.702 1.00 53.53 O ATOM 2430 CB ASP C 79 44.513 16.101 −30.887 1.00 53.03 C ATOM 2431 CG ASP C 79 43.048 15.907 −31.210 1.00 53.54 C ATOM 2432 OD1 ASP C 79 42.741 15.465 −32.337 1.00 53.19 O ATOM 2433 OD2 ASP C 79 42.201 16.191 −30.335 1.00 54.33 O ATOM 2434 N GLY C 80 43.213 18.624 −28.816 1.00 52.60 N ATOM 2435 CA GLY C 80 42.558 19.921 −28.873 1.00 51.91 C ATOM 2436 C GLY C 80 41.275 19.969 −29.688 1.00 51.26 C ATOM 2437 O GLY C 80 40.765 21.051 −29.981 1.00 51.15 O ATOM 2438 N ARG C 81 40.744 18.807 −30.055 1.00 50.21 N ATOM 2439 CA ARG C 81 39.512 18.763 −30.836 1.00 49.98 C ATOM 2440 C ARG C 81 38.295 18.757 −29.922 1.00 49.17 C ATOM 2441 O ARG C 81 38.356 18.262 −28.800 1.00 48.55 O ATOM 2442 CB ARG C 81 39.491 17.518 −31.735 1.00 50.35 C ATOM 2443 N LEU C 82 37.187 19.306 −30.405 1.00 48.69 N ATOM 2444 CA LEU C 82 35.960 19.348 −29.613 1.00 48.32 C ATOM 2445 C LEU C 82 34.941 18.320 −30.099 1.00 48.64 C ATOM 2446 O LEU C 82 34.789 18.102 −31.304 1.00 48.30 O ATOM 2447 CB LEU C 82 35.320 20.743 −29.677 1.00 47.29 C ATOM 2448 CG LEU C 82 36.026 21.976 −29.098 1.00 47.17 C ATOM 2449 CD1 LEU C 82 35.140 23.197 −29.319 1.00 46.72 C ATOM 2450 CD2 LEU C 82 36.298 21.796 −27.612 1.00 46.26 C ATOM 2451 N LEU C 83 34.250 17.690 −29.154 1.00 48.75 N ATOM 2452 CA LEU C 83 33.218 16.711 −29.469 1.00 49.23 C ATOM 2453 C LEU C 83 32.286 16.572 −28.264 1.00 49.29 C ATOM 2454 O LEU C 83 32.566 17.117 −27.200 1.00 49.90 O ATOM 2455 CB LEU C 83 33.847 15.365 −29.832 1.00 49.75 C ATOM 2456 CG LEU C 83 34.608 14.566 −28.775 1.00 50.52 C ATOM 2457 CD1 LEU C 83 33.657 13.956 −27.745 1.00 50.21 C ATOM 2458 CD2 LEU C 83 35.369 13.466 −29.495 1.00 51.56 C ATOM 2459 N ALA C 84 31.175 15.860 −28.434 1.00 49.10 N ATOM 2460 CA ALA C 84 30.219 15.668 −27.347 1.00 48.92 C ATOM 2461 C ALA C 84 30.058 14.186 −27.004 1.00 48.88 C ATOM 2462 O ALA C 84 29.679 13.379 −27.852 1.00 49.38 O ATOM 2463 CB ALA C 84 28.880 16.277 −27.720 1.00 48.95 C ATOM 2464 N SER C 85 30.336 13.851 −25.748 1.00 48.54 N ATOM 2465 CA SER C 85 30.277 12.484 −25.249 1.00 48.57 C ATOM 2466 C SER C 85 28.951 12.060 −24.619 1.00 48.60 C ATOM 2467 O SER C 85 28.278 12.852 −23.959 1.00 48.21 O ATOM 2468 CB SER C 85 31.387 12.281 −24.221 1.00 47.92 C ATOM 2469 OG SER C 85 31.239 11.031 −23.585 1.00 49.89 O ATOM 2470 N LYS C 86 28.598 10.793 −24.809 1.00 48.12 N ATOM 2471 CA LYS C 86 27.371 10.254 −24.247 1.00 47.55 C ATOM 2472 C LYS C 86 27.507 10.209 −22.728 1.00 47.26 C ATOM 2473 O LYS C 86 26.563 10.521 −21.997 1.00 47.30 O ATOM 2474 CB LYS C 86 27.112 8.849 −24.795 1.00 47.10 C ATOM 2475 N SER C 87 28.690 9.829 −22.258 1.00 46.30 N ATOM 2476 CA SER C 87 28.941 9.751 −20.826 1.00 46.50 C ATOM 2477 C SER C 87 30.011 10.757 −20.395 1.00 45.67 C ATOM 2478 O SER C 87 30.930 11.069 −21.146 1.00 45.37 O ATOM 2479 CB SER C 87 29.367 8.326 −20.448 1.00 47.59 C ATOM 2480 OG SER C 87 30.485 7.895 −21.213 1.00 47.94 O ATOM 2481 N VAL C 88 29.881 11.245 −19.169 1.00 45.08 N ATOM 2482 CA VAL C 88 30.794 12.226 −18.603 1.00 44.44 C ATOM 2483 C VAL C 88 32.196 11.683 −18.306 1.00 44.01 C ATOM 2484 O VAL C 88 32.337 10.651 −17.660 1.00 44.28 O ATOM 2485 CB VAL C 88 30.198 12.788 −17.293 1.00 44.66 C ATOM 2486 CG1 VAL C 88 31.119 13.850 −16.699 1.00 44.31 C ATOM 2487 CG2 VAL C 88 28.802 13.350 −17.564 1.00 44.59 C ATOM 2488 N THR C 89 33.223 12.383 −18.781 1.00 43.00 N ATOM 2489 CA THR C 89 34.608 11.992 −18.524 1.00 42.40 C ATOM 2490 C THR C 89 35.357 13.227 −18.034 1.00 41.68 C ATOM 2491 O THR C 89 34.782 14.309 −17.974 1.00 40.99 O ATOM 2492 CB THR C 89 35.313 11.464 −19.783 1.00 42.09 C ATOM 2493 OG1 THR C 89 35.446 12.524 −20.734 1.00 42.86 O ATOM 2494 CG2 THR C 89 34.519 10.318 −20.400 1.00 42.59 C ATOM 2495 N ASP C 90 36.633 13.066 −17.689 1.00 41.15 N ATOM 2496 CA ASP C 90 37.443 14.174 −17.191 1.00 41.02 C ATOM 2497 C ASP C 90 37.718 15.258 −18.228 1.00 41.00 C ATOM 2498 O ASP C 90 38.282 16.305 −17.910 1.00 41.60 O ATOM 2499 CB ASP C 90 38.776 13.652 −16.628 1.00 40.89 C ATOM 2500 CG ASP C 90 39.530 12.725 −17.604 1.00 41.99 C ATOM 2501 OD1 ASP C 90 39.161 12.634 −18.802 1.00 40.96 O ATOM 2502 OD2 ASP C 90 40.515 12.089 −17.162 1.00 40.95 O ATOM 2503 N GLU C 91 37.320 15.011 −19.469 1.00 40.62 N ATOM 2504 CA GLU C 91 37.542 15.989 −20.529 1.00 40.60 C ATOM 2505 C GLU C 91 36.272 16.810 −20.769 1.00 38.90 C ATOM 2506 O GLU C 91 36.183 17.563 −21.733 1.00 38.75 O ATOM 2507 CB GLU C 91 37.960 15.276 −21.820 1.00 40.75 C ATOM 2508 CG GLU C 91 39.061 14.251 −21.627 1.00 40.73 C ATOM 2509 CD GLU C 91 39.559 13.672 −22.942 1.00 41.24 C ATOM 2510 OE1 GLU C 91 38.728 13.210 −23.755 1.00 39.80 O ATOM 2511 OE2 GLU C 91 40.788 13.678 −23.159 1.00 42.00 O ATOM 2512 N CYS C 92 35.304 16.667 −19.873 1.00 37.52 N ATOM 2513 CA CYS C 92 34.032 17.374 −19.989 1.00 37.32 C ATOM 2514 C CYS C 92 33.843 18.530 −18.996 1.00 36.94 C ATOM 2515 O CYS C 92 32.738 19.064 −18.875 1.00 36.38 O ATOM 2516 CB CYS C 92 32.877 16.380 −19.822 1.00 37.36 C ATOM 2517 SG CYS C 92 32.820 15.037 −21.053 1.00 37.79 S ATOM 2518 N PHE C 93 34.915 18.918 −18.301 1.00 36.25 N ATOM 2519 CA PHE C 93 34.850 19.988 −17.308 1.00 35.38 C ATOM 2520 C PHE C 93 35.703 21.203 −17.687 1.00 34.84 C ATOM 2521 O PHE C 93 36.850 21.068 −18.115 1.00 34.56 O ATOM 2522 CB PHE C 93 35.241 19.415 −15.938 1.00 36.14 C ATOM 2523 CG PHE C 93 34.295 18.338 −15.452 1.00 37.64 C ATOM 2524 CD1 PHE C 93 32.993 18.660 −15.077 1.00 36.97 C ATOM 2525 CD2 PHE C 93 34.675 16.996 −15.454 1.00 38.01 C ATOM 2526 CE1 PHE C 93 32.077 17.670 −14.718 1.00 38.43 C ATOM 2527 CE2 PHE C 93 33.764 15.993 −15.095 1.00 39.03 C ATOM 2528 CZ PHE C 93 32.459 16.333 −14.727 1.00 39.06 C ATOM 2529 N PHE C 94 35.132 22.393 −17.514 1.00 33.24 N ATOM 2530 CA PHE C 94 35.802 23.627 −17.893 1.00 32.55 C ATOM 2531 C PHE C 94 35.689 24.748 −16.862 1.00 33.00 C ATOM 2532 O PHE C 94 34.622 24.949 −16.262 1.00 32.17 O ATOM 2533 CB PHE C 94 35.203 24.129 −19.202 1.00 31.92 C ATOM 2534 CG PHE C 94 35.190 23.103 −20.300 1.00 31.77 C ATOM 2535 CD1 PHE C 94 36.240 23.030 −21.213 1.00 31.68 C ATOM 2536 CD2 PHE C 94 34.123 22.209 −20.424 1.00 31.56 C ATOM 2537 CE1 PHE C 94 36.229 22.083 −22.238 1.00 32.19 C ATOM 2538 CE2 PHE C 94 34.099 21.256 −21.442 1.00 31.45 C ATOM 2539 CZ PHE C 94 35.156 21.193 −22.354 1.00 32.41 C ATOM 2540 N PHE C 95 36.788 25.479 −16.672 1.00 31.65 N ATOM 2541 CA PHE C 95 36.785 26.605 −15.749 1.00 32.59 C ATOM 2542 C PHE C 95 35.973 27.715 −16.422 1.00 32.18 C ATOM 2543 O PHE C 95 36.285 28.107 −17.544 1.00 31.89 O ATOM 2544 CB PHE C 95 38.203 27.153 −15.502 1.00 32.78 C ATOM 2545 CG PHE C 95 39.113 26.219 −14.754 1.00 33.25 C ATOM 2546 CD1 PHE C 95 40.174 25.588 −15.406 1.00 33.55 C ATOM 2547 CD2 PHE C 95 38.942 26.004 −13.389 1.00 33.39 C ATOM 2548 CE1 PHE C 95 41.060 24.752 −14.701 1.00 33.84 C ATOM 2549 CE2 PHE C 95 39.819 25.170 −12.673 1.00 34.03 C ATOM 2550 CZ PHE C 95 40.881 24.544 −13.333 1.00 33.13 C ATOM 2551 N GLU C 96 34.933 28.205 −15.755 1.00 31.97 N ATOM 2552 CA GLU C 96 34.145 29.292 −16.321 1.00 32.01 C ATOM 2553 C GLU C 96 34.593 30.582 −15.667 1.00 32.86 C ATOM 2554 O GLU C 96 34.685 30.674 −14.438 1.00 31.69 O ATOM 2555 CB GLU C 96 32.644 29.131 −16.070 1.00 30.63 C ATOM 2556 CG GLU C 96 31.826 30.275 −16.687 1.00 30.23 C ATOM 2557 CD GLU C 96 30.391 30.313 −16.195 1.00 31.57 C ATOM 2558 OE1 GLU C 96 30.191 30.709 −15.029 1.00 31.17 O ATOM 2559 OE2 GLU C 96 29.472 29.942 −16.964 1.00 30.53 O ATOM 2560 N ARG C 97 34.858 31.582 −16.497 1.00 33.81 N ATOM 2561 CA ARG C 97 35.288 32.876 −15.996 1.00 36.12 C ATOM 2562 C ARG C 97 34.610 34.050 −16.699 1.00 34.78 C ATOM 2563 O ARG C 97 34.470 34.063 −17.915 1.00 34.00 O ATOM 2564 CB ARG C 97 36.809 33.008 −16.138 1.00 38.79 C ATOM 2565 CG ARG C 97 37.343 34.362 −15.710 1.00 42.82 C ATOM 2566 CD ARG C 97 38.351 34.248 −14.579 1.00 47.40 C ATOM 2567 NE ARG C 97 39.732 34.315 −15.050 1.00 50.42 N ATOM 2568 CZ ARG C 97 40.229 35.309 −15.785 1.00 51.99 C ATOM 2569 NH1 ARG C 97 39.456 36.326 −16.144 1.00 52.03 N ATOM 2570 NH2 ARG C 97 41.508 35.293 −16.153 1.00 53.32 N ATOM 2571 N LEU C 98 34.168 35.023 −15.914 1.00 35.44 N ATOM 2572 CA LEU C 98 33.549 36.233 −16.451 1.00 35.58 C ATOM 2573 C LEU C 98 34.702 37.211 −16.606 1.00 36.26 C ATOM 2574 O LEU C 98 35.252 37.674 −15.612 1.00 37.23 O ATOM 2575 CB LEU C 98 32.537 36.816 −15.469 1.00 34.84 C ATOM 2576 CG LEU C 98 32.101 38.257 −15.784 1.00 36.02 C ATOM 2577 CD1 LEU C 98 31.366 38.301 −17.119 1.00 34.57 C ATOM 2578 CD2 LEU C 98 31.201 38.782 −14.663 1.00 36.07 C ATOM 2579 N GLU C 99 35.086 37.514 −17.842 1.00 37.80 N ATOM 2580 CA GLU C 99 36.204 38.433 −18.084 1.00 38.69 C ATOM 2581 C GLU C 99 35.808 39.884 −17.844 1.00 39.79 C ATOM 2582 O GLU C 99 34.619 40.226 −17.785 1.00 39.34 O ATOM 2583 CB GLU C 99 36.739 38.281 −19.517 1.00 39.78 C ATOM 2584 CG GLU C 99 37.157 36.852 −19.908 1.00 42.32 C ATOM 2585 CD GLU C 99 38.473 36.383 −19.275 1.00 44.17 C ATOM 2586 OE1 GLU C 99 38.778 35.171 −19.365 1.00 44.05 O ATOM 2587 OE2 GLU C 99 39.205 37.216 −18.698 1.00 45.49 O ATOM 2588 N SER C 100 36.821 40.738 −17.713 1.00 40.51 N ATOM 2589 CA SER C 100 36.617 42.165 −17.470 1.00 40.62 C ATOM 2590 C SER C 100 35.794 42.816 −18.572 1.00 39.80 C ATOM 2591 O SER C 100 35.152 43.848 −18.353 1.00 41.01 O ATOM 2592 CB SER C 100 37.971 42.882 −17.356 1.00 42.46 C ATOM 2593 OG SER C 100 38.653 42.906 −18.603 1.00 43.81 O ATOM 2594 N ASN C 101 35.821 42.222 −19.763 1.00 38.39 N ATOM 2595 CA ASN C 101 35.060 42.740 −20.900 1.00 36.37 C ATOM 2596 C ASN C 101 33.584 42.307 −20.845 1.00 35.56 C ATOM 2597 O ASN C 101 32.792 42.648 −21.725 1.00 36.19 O ATOM 2598 CB ASN C 101 35.683 42.244 −22.210 1.00 37.90 C ATOM 2599 N ASN C 102 33.237 41.549 −19.810 1.00 33.69 N ATOM 2600 CA ASN C 102 31.890 41.035 −19.584 1.00 32.91 C ATOM 2601 C ASN C 102 31.418 39.878 −20.473 1.00 31.53 C ATOM 2602 O ASN C 102 30.215 39.656 −20.621 1.00 29.70 O ATOM 2603 CB ASN C 102 30.851 42.162 −19.599 1.00 33.64 C ATOM 2604 CG ASN C 102 30.685 42.813 −18.231 1.00 35.78 C ATOM 2605 OD1 ASN C 102 30.944 42.182 −17.197 1.00 36.62 O ATOM 2606 ND2 ASN C 102 30.239 44.072 −18.214 1.00 35.16 N ATOM 2607 N TYR C 103 32.374 39.156 −21.055 1.00 29.91 N ATOM 2608 CA TYR C 103 32.090 37.975 −21.870 1.00 29.05 C ATOM 2609 C TYR C 103 32.597 36.788 −21.031 1.00 28.17 C ATOM 2610 O TYR C 103 33.392 36.972 −20.113 1.00 28.49 O ATOM 2611 CB TYR C 103 32.843 38.035 −23.201 1.00 28.04 C ATOM 2612 CG TYR C 103 32.186 38.901 −24.268 1.00 28.96 C ATOM 2613 CD1 TYR C 103 31.185 38.385 −25.103 1.00 28.99 C ATOM 2614 CD2 TYR C 103 32.568 40.232 −24.450 1.00 28.27 C ATOM 2615 CE1 TYR C 103 30.587 39.175 −26.096 1.00 28.06 C ATOM 2616 CE2 TYR C 103 31.976 41.027 −25.434 1.00 27.36 C ATOM 2617 CZ TYR C 103 30.995 40.495 −26.249 1.00 28.17 C ATOM 2618 OH TYR C 103 30.430 41.280 −27.220 1.00 27.43 O ATOM 2619 N ASN C 104 32.121 35.584 −21.319 1.00 27.04 N ATOM 2620 CA ASN C 104 32.556 34.393 −20.583 1.00 26.71 C ATOM 2621 C ASN C 104 33.604 33.620 −21.378 1.00 25.89 C ATOM 2622 O ASN C 104 33.641 33.709 −22.606 1.00 24.27 O ATOM 2623 CB ASN C 104 31.385 33.436 −20.349 1.00 26.70 C ATOM 2624 CG ASN C 104 30.573 33.778 −19.126 1.00 27.03 C ATOM 2625 OD1 ASN C 104 30.641 34.883 −18.605 1.00 27.86 O ATOM 2626 ND2 ASN C 104 29.784 32.817 −18.663 1.00 27.30 N ATOM 2627 N THR C 105 34.448 32.871 −20.671 1.00 25.77 N ATOM 2628 CA THR C 105 35.444 32.017 −21.315 1.00 26.79 C ATOM 2629 C THR C 105 35.374 30.659 −20.626 1.00 27.22 C ATOM 2630 O THR C 105 35.037 30.568 −19.434 1.00 26.69 O ATOM 2631 CB THR C 105 36.887 32.561 −21.197 1.00 27.27 C ATOM 2632 OG1 THR C 105 37.277 32.601 −19.819 1.00 27.69 O ATOM 2633 CG2 THR C 105 36.988 33.940 −21.817 1.00 26.48 C ATOM 2634 N TYR C 106 35.683 29.608 −21.383 1.00 27.57 N ATOM 2635 CA TYR C 106 35.649 28.245 −20.868 1.00 28.53 C ATOM 2636 C TYR C 106 36.980 27.560 −21.138 1.00 29.84 C ATOM 2637 O TYR C 106 37.298 27.243 −22.279 1.00 30.42 O ATOM 2638 CB TYR C 106 34.492 27.498 −21.529 1.00 27.19 C ATOM 2639 CG TYR C 106 33.178 28.086 −21.100 1.00 26.37 C ATOM 2640 CD1 TYR C 106 32.607 27.734 −19.871 1.00 24.88 C ATOM 2641 CD2 TYR C 106 32.562 29.082 −21.856 1.00 24.49 C ATOM 2642 CE1 TYR C 106 31.461 28.365 −19.406 1.00 24.93 C ATOM 2643 CE2 TYR C 106 31.419 29.720 −21.397 1.00 24.64 C ATOM 2644 CZ TYR C 106 30.878 29.364 −20.173 1.00 24.07 C ATOM 2645 OH TYR C 106 29.785 30.037 −19.690 1.00 23.81 O ATOM 2646 N ARG C 107 37.747 27.343 −20.071 1.00 31.74 N ATOM 2647 CA ARG C 107 39.068 26.728 −20.159 1.00 33.10 C ATOM 2648 C ARG C 107 39.093 25.297 −19.606 1.00 33.48 C ATOM 2649 O ARG C 107 38.622 25.033 −18.503 1.00 33.37 O ATOM 2650 CB ARG C 107 40.071 27.616 −19.417 1.00 33.24 C ATOM 2651 CG ARG C 107 41.514 27.177 −19.479 1.00 34.14 C ATOM 2652 CD ARG C 107 42.413 28.233 −18.821 1.00 33.47 C ATOM 2653 NE ARG C 107 41.977 28.538 −17.461 1.00 32.49 N ATOM 2654 CZ ARG C 107 42.333 27.851 −16.382 1.00 33.45 C ATOM 2655 NH1 ARG C 107 43.153 26.809 −16.490 1.00 33.22 N ATOM 2656 NH2 ARG C 107 41.850 28.191 −15.192 1.00 32.96 N ATOM 2657 N SER C 108 39.643 24.380 −20.396 1.00 34.74 N ATOM 2658 CA SER C 108 39.735 22.962 −20.030 1.00 35.93 C ATOM 2659 C SER C 108 40.408 22.738 −18.680 1.00 36.71 C ATOM 2660 O SER C 108 41.496 23.261 −18.432 1.00 36.82 O ATOM 2661 CB SER C 108 40.508 22.195 −21.111 1.00 35.40 C ATOM 2662 OG SER C 108 40.722 20.843 −20.748 1.00 33.84 O ATOM 2663 N ARG C 109 39.768 21.966 −17.807 1.00 37.26 N ATOM 2664 CA ARG C 109 40.369 21.695 −16.507 1.00 38.94 C ATOM 2665 C ARG C 109 41.478 20.654 −16.664 1.00 40.40 C ATOM 2666 O ARG C 109 42.385 20.583 −15.835 1.00 41.02 O ATOM 2667 CB ARG C 109 39.326 21.196 −15.496 1.00 38.66 C ATOM 2668 CG ARG C 109 39.879 21.084 −14.063 1.00 37.85 C ATOM 2669 CD ARG C 109 38.814 20.658 −13.055 1.00 37.07 C ATOM 2670 NE ARG C 109 38.218 19.369 −13.402 1.00 37.11 N ATOM 2671 CZ ARG C 109 37.403 18.673 −12.612 1.00 37.27 C ATOM 2672 NH1 ARG C 109 37.072 19.136 −11.417 1.00 37.53 N ATOM 2673 NH2 ARG C 109 36.926 17.500 −13.009 1.00 37.87 N ATOM 2674 N LYS C 110 41.410 19.857 −17.732 1.00 41.49 N ATOM 2675 CA LYS C 110 42.423 18.834 −17.983 1.00 42.63 C ATOM 2676 C LYS C 110 43.628 19.426 −18.720 1.00 42.64 C ATOM 2677 O LYS C 110 44.756 19.351 −18.227 1.00 43.22 O ATOM 2678 CB LYS C 110 41.822 17.668 −18.775 1.00 43.33 C ATOM 2679 CG LYS C 110 42.686 16.403 −18.750 1.00 44.52 C ATOM 2680 CD LYS C 110 41.816 15.148 −18.694 1.00 45.95 C ATOM 2681 CE LYS C 110 42.649 13.872 −18.721 1.00 45.97 C ATOM 2682 NZ LYS C 110 43.302 13.673 −20.041 1.00 46.29 N ATOM 2683 N TYR C 111 43.381 20.013 −19.889 1.00 42.26 N ATOM 2684 CA TYR C 111 44.421 20.650 −20.692 1.00 42.11 C ATOM 2685 C TYR C 111 44.252 22.137 −20.374 1.00 41.74 C ATOM 2686 O TYR C 111 43.661 22.897 −21.144 1.00 41.37 O ATOM 2687 CB TYR C 111 44.177 20.348 −22.178 1.00 42.34 C ATOM 2688 CG TYR C 111 43.874 18.884 −22.420 1.00 43.43 C ATOM 2689 CD1 TYR C 111 44.858 17.905 −22.239 1.00 43.53 C ATOM 2690 CD2 TYR C 111 42.576 18.462 −22.723 1.00 43.58 C ATOM 2691 CE1 TYR C 111 44.553 16.542 −22.341 1.00 43.93 C ATOM 2692 CE2 TYR C 111 42.256 17.098 −22.826 1.00 43.90 C ATOM 2693 CZ TYR C 111 43.248 16.144 −22.630 1.00 44.13 C ATOM 2694 OH TYR C 111 42.937 14.803 −22.687 1.00 43.02 O ATOM 2695 N THR C 112 44.785 22.525 −19.219 1.00 41.67 N ATOM 2696 CA THR C 112 44.666 23.880 −18.681 1.00 42.15 C ATOM 2697 C THR C 112 45.077 25.107 −19.488 1.00 42.41 C ATOM 2698 O THR C 112 45.018 26.214 −18.969 1.00 42.75 O ATOM 2699 CB THR C 112 45.365 23.973 −17.310 1.00 41.69 C ATOM 2700 OG1 THR C 112 46.748 23.631 −17.453 1.00 40.08 O ATOM 2701 CG2 THR C 112 44.696 23.028 −16.311 1.00 40.24 C ATOM 2702 N SER C 113 45.477 24.941 −20.742 1.00 42.56 N ATOM 2703 CA SER C 113 45.861 26.103 −21.531 1.00 42.48 C ATOM 2704 C SER C 113 44.964 26.331 −22.738 1.00 41.74 C ATOM 2705 O SER C 113 45.054 27.367 −23.402 1.00 41.60 O ATOM 2706 CB SER C 113 47.320 25.975 −21.989 1.00 42.76 C ATOM 2707 OG SER C 113 48.202 26.193 −20.903 1.00 43.02 O ATOM 2708 N TRP C 114 44.087 25.374 −23.008 1.00 40.80 N ATOM 2709 CA TRP C 114 43.211 25.476 −24.163 1.00 40.67 C ATOM 2710 C TRP C 114 41.782 25.918 −23.831 1.00 39.23 C ATOM 2711 O TRP C 114 41.236 25.565 −22.787 1.00 39.47 O ATOM 2712 CB TRP C 114 43.223 24.136 −24.910 1.00 42.07 C ATOM 2713 CG TRP C 114 44.638 23.683 −25.263 1.00 44.13 C ATOM 2714 CD1 TRP C 114 45.764 24.473 −25.344 1.00 44.09 C ATOM 2715 CD2 TRP C 114 45.060 22.355 −25.622 1.00 44.26 C ATOM 2716 NE1 TRP C 114 46.850 23.719 −25.729 1.00 44.28 N ATOM 2717 CE2 TRP C 114 46.449 22.419 −25.908 1.00 45.01 C ATOM 2718 CE3 TRP C 114 44.403 21.122 −25.732 1.00 45.00 C ATOM 2719 CZ2 TRP C 114 47.190 21.293 −26.297 1.00 44.84 C ATOM 2720 CZ3 TRP C 114 45.145 19.994 −26.120 1.00 45.55 C ATOM 2721 CH2 TRP C 114 46.522 20.093 −26.396 1.00 45.81 C ATOM 2722 N TYR C 115 41.196 26.700 −24.733 1.00 37.86 N ATOM 2723 CA TYR C 115 39.843 27.225 −24.573 1.00 37.08 C ATOM 2724 C TYR C 115 38.845 26.691 −25.595 1.00 36.26 C ATOM 2725 O TYR C 115 39.210 26.330 −26.710 1.00 36.31 O ATOM 2726 CB TYR C 115 39.833 28.750 −24.711 1.00 36.58 C ATOM 2727 CG TYR C 115 40.567 29.525 −23.645 1.00 36.87 C ATOM 2728 CD1 TYR C 115 41.894 29.920 −23.826 1.00 37.54 C ATOM 2729 CD2 TYR C 115 39.921 29.907 −22.470 1.00 36.57 C ATOM 2730 CE1 TYR C 115 42.561 30.687 −22.857 1.00 37.18 C ATOM 2731 CE2 TYR C 115 40.577 30.670 −21.498 1.00 37.62 C ATOM 2732 CZ TYR C 115 41.896 31.058 −21.700 1.00 37.00 C ATOM 2733 OH TYR C 115 42.538 31.822 −20.753 1.00 38.71 O ATOM 2734 N VAL C 116 37.577 26.650 −25.200 1.00 35.32 N ATOM 2735 CA VAL C 116 36.518 26.241 −26.113 1.00 34.41 C ATOM 2736 C VAL C 116 36.406 27.472 −27.018 1.00 34.62 C ATOM 2737 O VAL C 116 36.361 28.599 −26.529 1.00 33.71 O ATOM 2738 CB VAL C 116 35.200 25.995 −25.350 1.00 34.30 C ATOM 2739 CD1 VAL C 116 34.048 25.822 −26.330 1.00 33.87 C ATOM 2740 CG2 VAL C 116 35.341 24.755 −24.461 1.00 33.16 C ATOM 2741 N ALA C 117 36.385 27.268 −28.330 1.00 34.69 N ATOM 2742 CA ALA C 117 36.341 28.404 −29.241 1.00 35.58 C ATOM 2743 C ALA C 117 35.799 28.052 −30.618 1.00 36.71 C ATOM 2744 O ALA C 117 35.830 26.895 −31.040 1.00 36.73 O ATOM 2745 CB ALA C 117 37.738 28.985 −29.384 1.00 33.52 C ATOM 2746 N LEU C 118 35.316 29.069 −31.319 1.00 36.96 N ATOM 2747 CA LEU C 118 34.790 28.882 −32.657 1.00 38.21 C ATOM 2748 C LEU C 118 35.525 29.796 −33.626 1.00 39.32 C ATOM 2749 O LEU C 118 35.980 30.871 −33.247 1.00 39.31 O ATOM 2750 CB LEU C 118 33.292 29.180 −32.685 1.00 37.82 C ATOM 2751 CG LEU C 118 32.420 28.177 −31.925 1.00 37.61 C ATOM 2752 CD1 LEU C 118 30.980 28.624 −31.995 1.00 37.18 C ATOM 2753 CD2 LEU C 118 32.583 26.778 −32.517 1.00 36.37 C ATOM 2754 N LYS C 119 35.643 29.355 −34.876 1.00 40.72 N ATOM 2755 CA LYS C 119 36.322 30.136 −35.907 1.00 42.14 C ATOM 2756 C LYS C 119 35.323 30.991 −36.664 1.00 42.14 C ATOM 2757 O LYS C 119 34.121 30.726 −36.636 1.00 42.19 O ATOM 2758 CB LYS C 119 37.068 29.212 −36.880 1.00 43.11 C ATOM 2759 CG LYS C 119 37.999 28.252 −36.161 1.00 44.83 C ATOM 2760 CD LYS C 119 39.198 27.812 −36.994 1.00 46.40 C ATOM 2761 CE LYS C 119 38.855 26.720 −37.982 1.00 47.25 C ATOM 2762 NZ LYS C 119 40.088 25.981 −38.401 1.00 47.67 N ATOM 2763 N ARG C 120 35.829 32.022 −37.335 1.00 42.15 N ATOM 2764 CA ARG C 120 34.991 32.935 −38.107 1.00 42.88 C ATOM 2765 C ARG C 120 34.147 32.185 −39.129 1.00 43.19 C ATOM 2766 O ARG C 120 33.133 32.691 −39.598 1.00 43.38 O ATOM 2767 CB ARG C 120 35.859 33.969 −38.829 1.00 42.13 C ATOM 2768 N THR C 121 34.571 30.972 −39.463 1.00 44.11 N ATOM 2769 CA THR C 121 33.868 30.148 −40.437 1.00 44.82 C ATOM 2770 C THR C 121 32.649 29.451 −39.852 1.00 45.53 C ATOM 2771 O THR C 121 31.703 29.138 −40.572 1.00 46.25 O ATOM 2772 CB THR C 121 34.795 29.057 −41.031 1.00 45.19 C ATOM 2773 OG1 THR C 121 35.257 28.190 −39.987 1.00 44.99 O ATOM 2774 CG2 THR C 121 35.990 29.692 −41.719 1.00 44.57 C ATOM 2775 N GLY C 122 32.664 29.208 −38.549 1.00 45.46 N ATOM 2776 CA GLY C 122 31.543 28.523 −37.939 1.00 46.35 C ATOM 2777 C GLY C 122 31.964 27.141 −37.469 1.00 46.95 C ATOM 2778 O GLY C 122 31.180 26.399 −36.872 1.00 47.14 O ATOM 2779 N GLN C 123 33.214 26.798 −37.752 1.00 46.82 N ATOM 2780 CA GLN C 123 33.784 25.524 −37.343 1.00 47.12 C ATOM 2781 C GLN C 123 34.530 25.790 −36.041 1.00 47.36 C ATOM 2782 O GLN C 123 35.039 26.897 −35.828 1.00 46.67 O ATOM 2783 CB GLN C 123 34.764 25.025 −38.407 1.00 47.34 C ATOM 2784 CG GLN C 123 34.134 24.871 −39.785 1.00 48.83 C ATOM 2785 CD GLN C 123 32.958 23.903 −39.779 1.00 49.80 C ATOM 2786 OE1 GLN C 123 33.134 22.705 −39.550 1.00 50.77 O ATOM 2787 NE2 GLN C 123 31.752 24.422 −40.021 1.00 49.73 N ATOM 2788 N TYR C 124 34.599 24.795 −35.162 1.00 46.99 N ATOM 2789 CA TYR C 124 35.301 25.002 −33.907 1.00 47.03 C ATOM 2790 C TYR C 124 36.778 25.268 −34.187 1.00 46.35 C ATOM 2791 O TYR C 124 37.256 25.057 −35.297 1.00 45.97 O ATOM 2792 CB TYR C 124 35.126 23.793 −32.973 1.00 47.14 C ATOM 2793 CG TYR C 124 35.846 22.531 −33.392 1.00 47.82 C ATOM 2794 CD1 TYR C 124 37.238 22.436 −33.318 1.00 48.08 C ATOM 2795 CD2 TYR C 124 35.137 21.427 −33.854 1.00 48.30 C ATOM 2796 CE1 TYR C 124 37.902 21.270 −33.692 1.00 48.67 C ATOM 2797 CE2 TYR C 124 35.790 20.256 −34.228 1.00 49.35 C ATOM 2798 CZ TYR C 124 37.172 20.187 −34.146 1.00 49.55 C ATOM 2799 OH TYR C 124 37.814 19.031 −34.516 1.00 50.42 O ATOM 2800 N LYS C 125 37.492 25.742 −33.178 1.00 46.37 N ATOM 2801 CA LYS C 125 38.906 26.043 −33.314 1.00 46.94 C ATOM 2802 C LYS C 125 39.699 25.130 −32.379 1.00 48.01 C ATOM 2803 O LYS C 125 39.342 24.989 −31.206 1.00 47.58 O ATOM 2804 CB LYS C 125 39.157 27.516 −32.965 1.00 45.51 C ATOM 2805 CG LYS C 125 40.595 27.960 −33.137 1.00 44.49 C ATOM 2806 CD LYS C 125 40.772 29.449 −32.872 1.00 44.14 C ATOM 2807 CE LYS C 125 42.203 29.865 −33.188 1.00 44.33 C ATOM 2808 NZ LYS C 125 42.480 31.317 −33.012 1.00 44.72 N ATOM 2809 N LEU C 126 40.755 24.498 −32.901 1.00 48.86 N ATOM 2810 CA LEU C 126 41.583 23.599 −32.095 1.00 49.57 C ATOM 2811 C LEU C 126 42.010 24.278 −30.805 1.00 50.19 C ATOM 2812 O LEU C 126 42.540 25.394 −30.824 1.00 50.52 O ATOM 2813 CB LEU C 126 42.838 23.163 −32.859 1.00 49.28 C ATOM 2814 CG LEU C 126 42.741 22.054 −33.907 1.00 49.30 C ATOM 2815 CD1 LEU C 126 44.132 21.783 −34.451 1.00 49.33 C ATOM 2816 CD2 LEU C 126 42.161 20.789 −33.300 1.00 48.47 C ATOM 2817 N GLY C 127 41.779 23.600 −29.686 1.00 50.50 N ATOM 2818 CA GLY C 127 42.146 24.159 −28.400 1.00 51.25 C ATOM 2819 C GLY C 127 43.596 24.597 −28.357 1.00 51.49 C ATOM 2820 O GLY C 127 43.936 25.587 −27.706 1.00 51.40 O ATOM 2821 N SER C 128 44.455 23.862 −29.056 1.00 51.91 N ATOM 2822 CA SER C 128 45.881 24.175 −29.086 1.00 52.56 C ATOM 2823 C SER C 128 46.204 25.499 −29.781 1.00 52.60 C ATOM 2824 O SER C 128 47.298 26.040 −29.613 1.00 52.59 O ATOM 2825 CB SER C 128 46.658 23.031 −29.754 1.00 52.18 C ATOM 2826 OG SER C 128 46.170 22.754 −31.056 1.00 52.80 O ATOM 2827 N LYS C 129 45.250 26.023 −30.548 1.00 52.51 N ATOM 2828 CA LYS C 129 45.457 27.279 −31.260 1.00 52.09 C ATOM 2829 C LYS C 129 44.745 28.456 −30.596 1.00 51.76 C ATOM 2830 O LYS C 129 44.621 29.527 −31.195 1.00 52.11 O ATOM 2831 CB LYS C 129 44.982 27.142 −32.711 1.00 52.16 C ATOM 2832 N THR C 130 44.285 28.264 −29.362 1.00 50.68 N ATOM 2833 CA THR C 130 43.578 29.324 −28.640 1.00 49.50 C ATOM 2834 C THR C 130 44.489 30.078 −27.673 1.00 49.62 C ATOM 2835 O THR C 130 45.534 29.570 −27.254 1.00 49.24 O ATOM 2836 CB THR C 130 42.370 28.767 −27.828 1.00 48.35 C ATOM 2837 OG1 THR C 130 42.837 27.886 −26.801 1.00 46.67 O ATOM 2838 CG2 THR C 130 41.419 28.006 −28.737 1.00 47.87 C ATOM 2839 N GLY C 131 44.074 31.294 −27.327 1.00 49.58 N ATOM 2840 CA GLY C 131 44.836 32.128 −26.414 1.00 50.00 C ATOM 2841 C GLY C 131 43.918 33.094 −25.687 1.00 50.38 C ATOM 2842 O GLY C 131 42.841 33.407 −26.192 1.00 50.52 O ATOM 2843 N PRO C 132 44.323 33.602 −24.511 1.00 50.42 N ATOM 2844 CA PRO C 132 43.564 34.541 −23.677 1.00 50.80 C ATOM 2845 C PRO C 132 43.042 35.821 −24.328 1.00 50.86 C ATOM 2846 O PRO C 132 42.005 36.347 −23.916 1.00 51.41 O ATOM 2847 CB PRO C 132 44.537 34.859 −22.543 1.00 50.19 C ATOM 2848 CG PRO C 132 45.333 33.615 −22.426 1.00 50.69 C ATOM 2849 CD PRO C 132 45.608 33.279 −23.871 1.00 50.73 C ATOM 2850 N GLY C 133 43.750 36.334 −25.326 1.00 50.68 N ATOM 2851 CA GLY C 133 43.301 37.569 −25.950 1.00 50.31 C ATOM 2852 C GLY C 133 42.495 37.425 −27.231 1.00 49.78 C ATOM 2853 O GLY C 133 42.092 38.426 −27.832 1.00 50.24 O ATOM 2854 N GLN C 134 42.242 36.188 −27.645 1.00 48.18 N ATOM 2855 CA GLN C 134 41.504 35.929 −28.880 1.00 46.73 C ATOM 2856 C GLN C 134 40.003 36.213 −28.809 1.00 45.05 C ATOM 2857 O GLN C 134 39.380 36.120 −27.750 1.00 45.79 O ATOM 2858 CB GLN C 134 41.719 34.476 −29.312 1.00 46.87 C ATOM 2859 CG GLN C 134 43.099 34.190 −29.882 1.00 47.41 C ATOM 2860 CD GLN C 134 43.388 32.707 −29.971 1.00 47.95 C ATOM 2861 OE1 GLN C 134 42.484 31.904 −30.195 1.00 48.19 O ATOM 2862 NE2 GLN C 134 44.654 32.335 −29.804 1.00 47.92 N ATOM 2863 N LYS C 135 39.434 36.548 −29.960 1.00 42.11 N ATOM 2864 CA LYS C 135 38.012 36.838 −30.088 1.00 40.04 C ATOM 2865 C LYS C 135 37.212 35.530 −30.172 1.00 38.28 C ATOM 2866 O LYS C 135 36.022 35.498 −29.874 1.00 36.96 O ATOM 2867 CB LYS C 135 37.779 37.668 −31.353 1.00 39.93 C ATOM 2868 CG LYS C 135 36.356 38.127 −31.568 1.00 41.26 C ATOM 2869 CD LYS C 135 36.252 38.964 −32.836 1.00 42.03 C ATOM 2870 CE LYS C 135 34.843 39.510 −33.005 1.00 44.12 C ATOM 2871 NZ LYS C 135 34.708 40.444 −34.159 1.00 45.15 N ATOM 2872 N ALA C 136 37.890 34.457 −30.568 1.00 36.67 N ATOM 2873 CA ALA C 136 37.278 33.143 −30.732 1.00 35.40 C ATOM 2874 C ALA C 136 36.852 32.448 −29.442 1.00 34.50 C ATOM 2875 O ALA C 136 36.033 31.534 −29.478 1.00 34.22 O ATOM 2876 CB ALA C 136 38.228 32.240 −31.502 1.00 36.34 C ATOM 2877 N ILE C 137 37.402 32.873 −28.307 1.00 32.81 N ATOM 2878 CA ILE C 137 37.068 32.253 −27.026 1.00 31.85 C ATOM 2879 C ILE C 137 36.030 33.019 −26.185 1.00 30.74 C ATOM 2880 O ILE C 137 35.693 32.594 −25.076 1.00 29.55 O ATOM 2881 CB ILE C 137 38.316 32.100 −26.153 1.00 32.24 C ATOM 2882 CG1 ILE C 137 38.781 33.480 −25.679 1.00 32.05 C ATOM 2883 CG2 ILE C 137 39.426 31.428 −26.951 1.00 32.13 C ATOM 2884 CD1 ILE C 137 39.787 33.421 −24.527 1.00 31.70 C ATOM 2885 N LEU C 138 35.523 34.132 −26.709 1.00 29.05 N ATOM 2886 CA LEU C 138 34.559 34.947 −25.966 1.00 28.81 C ATOM 2887 C LEU C 138 33.101 34.590 −26.244 1.00 28.16 C ATOM 2888 O LEU C 138 32.629 34.695 −27.369 1.00 26.69 O ATOM 2889 CB LEU C 138 34.800 36.422 −26.263 1.00 28.20 C ATOM 2890 CG LEU C 138 36.231 36.912 −25.993 1.00 29.51 C ATOM 2891 CD1 LEU C 138 36.375 38.314 −26.550 1.00 29.14 C ATOM 2892 CD2 LEU C 138 36.564 36.878 −24.489 1.00 28.12 C ATOM 2893 N PHE C 139 32.401 34.171 −25.194 1.00 28.26 N ATOM 2894 CA PHE C 139 31.003 33.770 −25.294 1.00 28.24 C ATOM 2895 C PHE C 139 30.087 34.593 −24.402 1.00 28.66 C ATOM 2896 O PHE C 139 30.485 35.048 −23.329 1.00 28.09 O ATOM 2897 CB PHE C 139 30.848 32.305 −24.886 1.00 27.63 C ATOM 2898 CG PHE C 139 31.420 31.329 −25.871 1.00 28.77 C ATOM 2899 CD1 PHE C 139 32.759 30.978 −25.829 1.00 28.45 C ATOM 2900 CD2 PHE C 139 30.604 30.760 −26.853 1.00 28.64 C ATOM 2901 CE1 PHE C 139 33.285 30.070 −26.751 1.00 29.93 C ATOM 2902 CE2 PHE C 139 31.119 29.857 −27.780 1.00 28.93 C ATOM 2903 CZ PHE C 139 32.463 29.510 −27.729 1.00 29.11 C ATOM 2904 N LEU C 140 28.843 34.746 −24.833 1.00 28.67 N ATOM 2905 CA LEU C 140 27.858 35.477 −24.059 1.00 29.11 C ATOM 2906 C LEU C 140 26.681 34.540 −23.809 1.00 29.71 C ATOM 2907 O LEU C 140 26.002 34.125 −24.746 1.00 30.07 O ATOM 2908 CB LEU C 140 27.397 36.711 −24.836 1.00 30.72 C ATOM 2909 CG LEU C 140 26.598 37.804 −24.121 1.00 32.61 C ATOM 2910 CD1 LEU C 140 27.455 38.462 −23.036 1.00 34.13 C ATOM 2911 CD2 LEU C 140 26.171 38.863 −25.140 1.00 33.01 C ATOM 2912 N PRO C 141 26.439 34.165 −22.545 1.00 30.12 N ATOM 2913 CA PRO C 141 25.309 33.270 −22.279 1.00 31.30 C ATOM 2914 C PRO C 141 23.979 33.993 −22.542 1.00 32.79 C ATOM 2915 O PRO C 141 23.788 35.138 −22.113 1.00 32.92 O ATOM 2916 CB PRO C 141 25.502 32.903 −20.807 1.00 30.88 C ATOM 2917 CG PRO C 141 26.136 34.135 −20.251 1.00 32.30 C ATOM 2918 CD PRO C 141 27.164 34.468 −21.301 1.00 30.47 C ATOM 2919 N MET C 142 23.078 33.335 −23.270 1.00 33.37 N ATOM 2920 CA MET C 142 21.774 33.925 −23.588 1.00 35.47 C ATOM 2921 C MET C 142 20.624 32.966 −23.284 1.00 36.61 C ATOM 2922 O MET C 142 20.794 31.743 −23.269 1.00 36.18 O ATOM 2923 CB MET C 142 21.704 34.330 −25.070 1.00 35.37 C ATOM 2924 CG MET C 142 22.608 35.496 −25.470 1.00 35.81 C ATOM 2925 SD MET C 142 22.635 35.805 −27.272 1.00 36.85 S ATOM 2926 CE MET C 142 21.354 37.092 −27.421 1.00 36.14 C ATOM 2927 N SER C 143 19.449 33.536 −23.048 1.00 38.73 N ATOM 2928 CA SER C 143 18.253 32.756 −22.750 1.00 40.72 C ATOM 2929 C SER C 143 17.892 31.800 −23.874 1.00 41.63 C ATOM 2930 O SER C 143 18.057 32.116 −25.056 1.00 40.60 O ATOM 2931 CB SER C 143 17.060 33.683 −22.515 1.00 41.40 C ATOM 2932 OG SER C 143 15.863 32.937 −22.405 1.00 43.45 O ATOM 2933 N ALA C 144 17.393 30.628 −23.498 1.00 43.48 N ATOM 2934 CA ALA C 144 16.977 29.637 −24.475 1.00 45.83 C ATOM 2935 C ALA C 144 15.525 29.918 −24.880 1.00 47.20 C ATOM 2936 O ALA C 144 14.797 29.011 −25.274 1.00 47.66 O ATOM 2937 CB ALA C 144 17.100 28.250 −23.883 1.00 46.09 C ATOM 2938 N LYS C 145 15.117 31.183 −24.774 1.00 48.47 N ATOM 2939 CA LYS C 145 13.762 31.598 −25.136 1.00 49.70 C ATOM 2940 C LYS C 145 12.717 30.794 −24.379 1.00 50.25 C ATOM 2941 O LYS C 145 12.639 31.010 −23.149 1.00 51.81 O ATOM 2942 CB LYS C 145 13.544 31.434 −26.645 1.00 48.79 C TER 2943 LYS C 145 ATOM 2944 N HIS D 16 54.126 19.899 14.823 1.00 38.67 N ATOM 2945 CA HIS D 16 54.234 21.034 13.858 1.00 38.27 C ATOM 2946 C HIS D 16 55.316 21.999 14.343 1.00 37.14 C ATOM 2947 O HIS D 16 55.264 22.495 15.468 1.00 36.27 O ATOM 2948 CB HIS D 16 52.888 21.755 13.734 1.00 39.12 C ATOM 2949 N PHE D 17 56.295 22.258 13.480 1.00 36.78 N ATOM 2950 CA PHE D 17 57.414 23.139 13.827 1.00 36.50 C ATOM 2951 C PHE D 17 57.042 24.586 14.193 1.00 36.19 C ATOM 2952 O PHE D 17 57.753 25.226 14.970 1.00 36.26 O ATOM 2953 CB PHE D 17 58.472 23.128 12.704 1.00 35.56 C ATOM 2954 CG PHE D 17 58.007 23.745 11.400 1.00 35.39 C ATOM 2955 CD1 PHE D 17 58.315 25.068 11.092 1.00 34.82 C ATOM 2956 CD2 PHE D 17 57.274 23.001 10.482 1.00 34.55 C ATOM 2957 CE1 PHE D 17 57.902 25.643 9.879 1.00 34.72 C ATOM 2958 CE2 PHE D 17 56.856 23.561 9.271 1.00 34.88 C ATOM 2959 CZ PHE D 17 57.173 24.888 8.969 1.00 34.53 C ATOM 2960 N LYS D 18 55.931 25.087 13.651 1.00 36.16 N ATOM 2961 CA LYS D 18 55.465 26.451 13.919 1.00 35.93 C ATOM 2962 C LYS D 18 54.863 26.648 15.307 1.00 36.04 C ATOM 2963 O LYS D 18 54.742 27.773 15.782 1.00 35.87 O ATOM 2964 CB LYS D 18 54.411 26.861 12.887 1.00 36.04 C ATOM 2965 CG LYS D 18 54.918 27.006 11.464 1.00 37.00 C ATOM 2966 CD LYS D 18 53.914 27.766 10.608 1.00 38.12 C ATOM 2967 CE LYS D 18 52.666 26.940 10.305 1.00 38.98 C ATOM 2968 NZ LYS D 18 52.845 26.089 9.097 1.00 38.63 N ATOM 2969 N ASP D 19 54.466 25.556 15.951 1.00 36.18 N ATOM 2970 CA ASP D 19 53.868 25.639 17.276 1.00 35.73 C ATOM 2971 C ASP D 19 54.874 25.897 18.384 1.00 35.80 C ATOM 2972 O ASP D 19 56.032 25.466 18.306 1.00 35.27 O ATOM 2973 CB ASP D 19 53.121 24.347 17.595 1.00 36.20 C ATOM 2974 CG ASP D 19 51.888 24.162 16.735 1.00 36.50 C ATOM 2975 OD1 ASP D 19 51.395 23.022 16.662 1.00 35.39 O ATOM 2976 OD2 ASP D 19 51.412 25.162 16.143 1.00 37.10 O ATOM 2977 N PRO D 20 54.442 26.616 19.431 1.00 35.60 N ATOM 2978 CA PRO D 20 55.310 26.919 20.572 1.00 35.68 C ATOM 2979 C PRO D 20 55.664 25.610 21.271 1.00 35.52 C ATOM 2980 O PRO D 20 54.985 24.598 21.086 1.00 34.34 O ATOM 2981 CB PRO D 20 54.450 27.854 21.428 1.00 35.65 C ATOM 2982 CG PRO D 20 53.052 27.478 21.060 1.00 36.50 C ATOM 2983 CD PRO D 20 53.137 27.283 19.575 1.00 36.19 C ATOM 2984 N LYS D 21 56.723 25.628 22.073 1.00 35.95 N ATOM 2985 CA LYS D 21 57.174 24.416 22.743 1.00 36.41 C ATOM 2986 C LYS D 21 57.799 24.676 24.090 1.00 36.32 C ATOM 2987 O LYS D 21 58.139 25.811 24.422 1.00 36.96 O ATOM 2988 CB LYS D 22 58.222 23.722 21.870 1.00 36.98 C ATOM 2989 CG LYS D 22 57.658 23.001 20.680 1.00 39.76 C ATOM 2990 CD LYS D 21 58.649 22.944 19.546 1.00 42.45 C ATOM 2991 CE LYS D 21 58.146 22.000 18.458 1.00 44.33 C ATOM 2992 NZ LYS D 21 56.697 22.198 18.191 1.00 44.06 N ATOM 2993 N ARG D 22 57.944 23.610 24.866 1.00 35.71 N ATOM 2994 CA ARG D 22 58.618 23.704 26.145 1.00 36.21 C ATOM 2995 C ARG D 22 59.935 22.992 25.851 1.00 35.14 C ATOM 2996 O ARG D 22 59.956 22.033 25.081 1.00 35.57 O ATOM 2997 CB ARG D 22 57.877 22.941 27.246 1.00 37.73 C ATOM 2998 CG ARG D 22 56.414 23.305 27.477 1.00 41.03 C ATOM 2999 CD ARG D 22 55.986 22.704 28.804 1.00 43.60 C ATOM 3000 NE ARG D 22 54.571 22.353 28.919 1.00 46.77 N ATOM 3001 CZ ARG D 22 53.568 23.221 29.012 1.00 48.46 C ATOM 3002 NH1 ARG D 22 53.800 24.533 28.993 1.00 49.57 N ATOM 3003 NH2 ARG D 22 52.328 22.771 29.169 1.00 48.22 N ATOM 3004 N LEU D 23 61.030 23.470 26.423 1.00 34.08 N ATOM 3005 CA LEU D 23 62.327 22.822 26.234 1.00 32.93 C ATOM 3006 C LEU D 23 62.703 22.179 27.556 1.00 32.48 C ATOM 3007 O LEU D 23 63.053 22.865 28.514 1.00 31.86 O ATOM 3008 CB LEU D 23 63.401 23.832 25.826 1.00 32.07 C ATOM 3009 CG LEU D 23 63.322 24.421 24.417 1.00 33.42 C ATOM 3010 CD1 LEU D 23 64.358 25.525 24.263 1.00 32.81 C ATOM 3011 CD2 LEU D 23 63.541 23.314 23.382 1.00 33.14 C ATOM 3012 N TYR D 24 62.621 20.855 27.590 1.00 32.58 N ATOM 3013 CA TYR D 24 62.927 20.072 28.771 1.00 31.77 C ATOM 3014 C TYR D 24 64.417 19.700 28.834 1.00 32.21 C ATOM 3015 O TYR D 24 64.983 19.178 27.868 1.00 32.68 O ATOM 3016 CB TYR D 24 62.042 18.828 28.749 1.00 30.62 C ATOM 3017 CG TYR D 24 62.473 17.713 29.668 1.00 30.23 C ATOM 3018 CD1 TYR D 24 63.520 16.864 29.321 1.00 28.85 C ATOM 3019 CD2 TYR D 24 61.810 17.483 30.870 1.00 29.46 C ATOM 3020 CE1 TYR D 24 63.893 15.804 30.147 1.00 28.77 C ATOM 3021 CE2 TYR D 24 62.175 16.433 31.702 1.00 29.39 C ATOM 3022 CZ TYR D 24 63.217 15.593 31.331 1.00 28.77 C ATOM 3023 OH TYR D 24 63.559 14.538 32.141 1.00 27.74 O ATOM 3024 N CYS D 25 65.051 19.966 29.972 1.00 32.20 N ATOM 3025 CA CYS D 25 66.467 19.642 30.133 1.00 32.62 C ATOM 3026 C CYS D 25 66.643 18.290 30.822 1.00 33.02 C ATOM 3027 O CYS D 25 66.117 18.059 31.915 1.00 32.11 O ATOM 3028 CB CYS D 25 67.187 20.723 30.946 1.00 32.95 C ATOM 3029 SG CYS D 25 69.001 20.532 30.972 1.00 31.97 S ATOM 3030 N LYS D 26 67.382 17.400 30.169 1.00 34.05 N ATOM 3031 CA LYS D 26 67.637 16.076 30.710 1.00 35.40 C ATOM 3032 C LYS D 26 68.281 16.180 32.089 1.00 36.05 C ATOM 3033 O LYS D 26 68.062 15.331 32.955 1.00 36.30 O ATOM 3034 CB LYS D 26 68.559 15.281 29.785 1.00 35.59 C ATOM 3035 CG LYS D 26 68.716 13.828 30.221 1.00 36.96 C ATOM 3036 CD LYS D 26 69.634 13.048 29.297 1.00 37.22 C ATOM 3037 CE LYS D 26 69.752 11.603 29.752 1.00 38.52 C ATOM 3038 NZ LYS D 26 70.750 10.852 28.930 1.00 39.15 N ATOM 3039 N ASN D 27 69.074 17.228 32.291 1.00 36.41 N ATOM 3040 CA ASN D 27 69.750 17.436 33.568 1.00 36.38 C ATOM 3041 C ASN D 27 68.740 17.901 34.617 1.00 36.08 C ATOM 3042 O ASN D 27 68.336 19.066 34.615 1.00 35.53 O ATOM 3043 CB ASN D 27 70.852 18.491 33.408 1.00 36.79 C ATOM 3044 CG ASN D 27 71.929 18.379 34.482 1.00 37.99 C ATOM 3045 OD1 ASN D 27 72.675 19.333 34.746 1.00 37.72 O ATOM 3046 ND2 ASN D 27 72.024 17.207 35.096 1.00 37.35 N ATOM 3047 N GLY D 28 68.326 16.989 35.500 1.00 35.93 N ATOM 3048 CA GLY D 28 67.368 17.340 36.539 1.00 35.08 C ATOM 3049 C GLY D 28 65.898 17.394 36.123 1.00 35.49 C ATOM 3050 O GLY D 28 65.009 17.399 36.971 1.00 34.34 O ATOM 3051 N GLY D 29 65.630 17.443 34.825 1.00 35.76 N ATOM 3052 CA GLY D 29 64.252 17.489 34.373 1.00 36.75 C ATOM 3053 C GLY D 29 63.562 18.835 34.551 1.00 37.21 C ATOM 3054 O GLY D 29 62.400 18.880 34.942 1.00 37.24 O ATOM 3055 N PHE D 30 64.269 19.928 34.276 1.00 37.20 N ATOM 3056 CA PHE D 30 63.694 21.270 34.391 1.00 37.97 C ATOM 3057 C PHE D 30 63.298 21.800 33.010 1.00 38.10 C ATOM 3058 O PHE D 30 63.945 21.496 32.009 1.00 38.11 O ATOM 3059 CB PHE D 30 64.695 22.287 34.963 1.00 37.64 C ATOM 3060 CG PHE D 30 65.278 21.923 36.296 1.00 37.90 C ATOM 3061 CD1 PHE D 30 66.540 21.334 36.381 1.00 37.94 C ATOM 3062 CD2 PHE D 30 64.603 22.239 37.474 1.00 38.44 C ATOM 3063 CE1 PHE D 30 67.126 21.074 37.626 1.00 37.98 C ATOM 3064 CE2 PHE D 30 65.175 21.983 38.720 1.00 37.36 C ATOM 3065 CZ PHE D 30 66.440 21.401 38.795 1.00 38.16 C ATOM 3066 N PHE D 31 62.246 22.609 32.968 1.00 37.80 N ATOM 3067 CA PHE D 31 61.799 23.226 31.726 1.00 37.80 C ATOM 3068 C PHE D 31 62.462 24.603 31.677 1.00 38.08 C ATOM 3069 O PHE D 31 62.414 25.343 32.661 1.00 37.41 O ATOM 3070 CB PHE D 31 60.276 23.415 31.723 1.00 37.75 C ATOM 3071 CG PHE D 31 59.493 22.134 31.584 1.00 37.85 C ATOM 3072 CD1 PHE D 31 59.590 21.369 30.431 1.00 37.09 C ATOM 3073 CD2 PHE D 31 58.645 21.707 32.601 1.00 38.01 C ATOM 3074 CE1 PHE D 31 58.854 20.196 30.285 1.00 37.44 C ATOM 3075 CE2 PHE D 31 57.901 20.528 32.465 1.00 38.66 C ATOM 3076 CZ PHE D 31 58.007 19.774 31.301 1.00 38.10 C ATOM 3077 N LEU D 32 63.085 24.942 30.550 1.00 38.06 N ATOM 3078 CA LEU D 32 63.733 26.244 30.416 1.00 38.41 C ATOM 3079 C LEU D 32 62.678 27.326 30.623 1.00 39.14 C ATOM 3080 O LEU D 32 61.622 27.295 29.991 1.00 39.29 O ATOM 3081 CB LEU D 32 64.357 26.399 29.029 1.00 37.69 C ATOM 3082 CG LEU D 32 65.257 27.630 28.835 1.00 37.38 C ATOM 3083 CD1 LEU D 32 66.368 27.640 29.887 1.00 36.99 C ATOM 3084 CD2 LEU D 32 65.856 27.600 27.445 1.00 36.24 C ATOM 3085 N ARG D 33 62.965 28.281 31.501 1.00 39.62 N ATOM 3086 CA ARG D 33 62.019 29.355 31.799 1.00 40.13 C ATOM 3087 C ARG D 33 62.569 30.759 31.540 1.00 40.47 C ATOM 3088 O ARG D 33 63.702 31.069 31.908 1.00 40.15 O ATOM 3089 CB ARG D 33 61.564 29.247 33.261 1.00 39.82 C ATOM 3090 CG ARG D 33 60.565 30.316 33.681 1.00 40.22 C ATOM 3091 CD ARG D 33 59.896 29.988 35.013 1.00 39.80 C ATOM 3092 NE ARG D 33 60.834 29.991 36.131 1.00 40.49 N ATOM 3093 CZ ARG D 33 60.468 29.978 37.413 1.00 41.41 C ATOM 3094 NH1 ARG D 33 59.175 29.959 37.732 1.00 41.64 N ATOM 3095 NH2 ARG D 33 61.386 29.991 38.378 1.00 39.88 N ATOM 3096 N ILE D 34 61.758 31.602 30.905 1.00 41.17 N ATOM 3097 CA ILE D 34 62.158 32.976 30.610 1.00 42.90 C ATOM 3098 C ILE D 34 61.194 33.940 31.309 1.00 44.48 C ATOM 3099 O ILE D 34 60.048 34.114 30.885 1.00 44.51 O ATOM 3100 CB ILE D 34 62.159 33.243 29.082 1.00 42.66 C ATOM 3101 CG1 ILE D 34 63.213 32.362 28.399 1.00 42.04 C ATOM 3102 CG2 ILE D 34 62.453 34.701 28.800 1.00 41.35 C ATOM 3103 CD1 ILE D 34 63.256 32.507 26.889 1.00 41.47 C ATOM 3104 N HIS D 35 61.676 34.550 32.389 1.00 46.13 N ATOM 3105 CA HIS D 35 60.890 35.482 33.193 1.00 48.17 C ATOM 3106 C HIS D 35 60.651 36.828 32.514 1.00 49.27 C ATOM 3107 O HIS D 35 61.449 37.273 31.687 1.00 49.41 O ATOM 3108 CB HIS D 35 61.569 35.702 34.553 1.00 47.48 C ATOM 3109 N PRO D 36 59.538 37.498 32.865 1.00 50.83 N ATOM 3110 CA PRO D 36 59.169 38.804 32.300 1.00 51.53 C ATOM 3111 C PRO D 36 60.272 39.859 32.420 1.00 52.04 C ATOM 3112 O PRO D 36 60.417 40.713 31.543 1.00 52.40 O ATOM 3113 CB PRO D 36 57.926 39.186 33.100 1.00 52.02 C ATOM 3114 CG PRO D 36 57.314 37.859 33.428 1.00 51.73 C ATOM 3115 CD PRO D 36 58.517 37.038 33.825 1.00 51.06 C ATOM 3116 N ASP D 37 61.045 39.795 33.502 1.00 52.30 N ATOM 3117 CA ASP D 37 62.124 40.746 33.738 1.00 52.98 C ATOM 3118 C ASP D 37 63.442 40.350 33.082 1.00 52.81 C ATOM 3119 O ASP D 37 64.467 41.003 33.298 1.00 52.83 O ATOM 3120 CB ASP D 37 62.349 40.925 35.240 1.00 54.57 C ATOM 3121 CG ASP D 37 62.536 39.607 35.956 1.00 56.00 C ATOM 3122 OD1 ASP D 37 61.538 38.866 36.088 1.00 57.43 O ATOM 3123 OD2 ASP D 37 63.675 39.307 36.376 1.00 56.89 O ATOM 3124 N GLY D 38 63.427 39.270 32.307 1.00 52.15 N ATOM 3125 CA GLY D 38 64.638 38.849 31.626 1.00 51.24 C ATOM 3126 C GLY D 38 65.546 37.828 32.292 1.00 50.73 C ATOM 3127 O GLY D 38 66.608 37.512 31.749 1.00 50.65 O ATOM 3128 N ARG D 39 65.174 37.308 33.457 1.00 49.97 N ATOM 3129 CA ARG D 39 66.029 36.309 34.093 1.00 49.69 C ATOM 3130 C ARG D 39 65.758 34.932 33.492 1.00 48.51 C ATOM 3131 O ARG D 39 64.637 34.643 33.061 1.00 48.43 O ATOM 3132 CB ARG D 39 65.818 36.274 35.611 1.00 51.28 C ATOM 3133 CG ARG D 39 66.829 37.120 36.384 1.00 54.09 C ATOM 3134 CD ARG D 39 66.597 37.087 37.895 1.00 55.79 C ATOM 3135 NE ARG D 39 65.250 37.530 38.246 1.00 58.04 N ATOM 3136 CZ ARG D 39 64.186 36.733 38.292 1.00 58.99 C ATOM 3137 NH1 ARG D 39 62.997 37.226 38.614 1.00 59.48 N ATOM 3138 NH2 ARG D 39 64.311 35.437 38.038 1.00 60.22 N ATOM 3139 N VAL D 40 66.786 34.091 33.447 1.00 46.54 N ATOM 3140 CA VAL D 40 66.634 32.751 32.890 1.00 45.12 C ATOM 3141 C VAL D 40 67.030 31.647 33.866 1.00 44.62 C ATOM 3142 O VAL D 40 68.118 31.670 34.443 1.00 44.40 O ATOM 3143 CB VAL D 40 67.471 32.571 31.596 1.00 44.81 C ATOM 3144 CG1 VAL D 40 67.383 31.128 31.114 1.00 43.98 C ATOM 3145 CG2 VAL D 40 66.973 33.508 30.510 1.00 44.13 C ATOM 3146 N ASP D 41 66.134 30.680 34.039 1.00 43.92 N ATOM 3147 CA ASP D 41 66.370 29.534 34.916 1.00 43.96 C ATOM 3148 C ASP D 41 65.503 28.355 34.474 1.00 44.09 C ATOM 3149 O ASP D 41 64.914 28.379 33.394 1.00 43.67 O ATOM 3150 CB ASP D 41 66.066 29.881 36.389 1.00 43.15 C ATOM 3151 CG ASP D 41 64.581 30.180 36.653 1.00 43.98 C ATOM 3152 OD1 ASP D 41 64.233 30.406 37.840 1.00 43.89 O ATOM 3153 OD2 ASP D 41 63.765 30.191 35.703 1.00 41.66 O ATOM 3154 N GLY D 42 65.427 27.334 35.321 1.00 44.01 N ATOM 3155 CA GLY D 42 64.630 26.167 35.011 1.00 44.61 C ATOM 3156 C GLY D 42 63.653 25.867 36.130 1.00 45.13 C ATOM 3157 O GLY D 42 63.891 26.232 37.274 1.00 45.40 O ATOM 3158 N VAL D 43 62.553 25.200 35.796 1.00 45.41 N ATOM 3159 CA VAL D 43 61.531 24.852 36.771 1.00 45.73 C ATOM 3160 C VAL D 43 60.873 23.534 36.359 1.00 46.34 C ATOM 3161 O VAL D 43 60.838 23.196 35.174 1.00 46.69 O ATOM 3162 CB VAL D 43 60.469 25.995 36.875 1.00 45.11 C ATOM 3163 CG1 VAL D 43 59.625 26.067 35.609 1.00 43.89 C ATOM 3164 CG2 VAL D 43 59.596 25.789 38.092 1.00 45.21 C ATOM 3165 N ARG D 44 60.359 22.795 37.339 1.00 47.07 N ATOM 3166 CA ARG D 44 59.721 21.504 37.093 1.00 48.22 C ATOM 3167 C ARG D 44 58.216 21.574 36.810 1.00 49.00 C ATOM 3168 O ARG D 44 57.660 20.680 36.169 1.00 49.13 O ATOM 3169 CB ARG D 44 59.947 20.570 38.296 1.00 48.25 C ATOM 3170 CG ARG D 44 61.396 20.125 38.554 1.00 48.15 C ATOM 3171 CD ARG D 44 61.425 19.003 39.600 1.00 47.68 C ATOM 3172 NE ARG D 44 62.689 18.262 39.650 1.00 48.47 N ATOM 3173 CZ ARG D 44 63.846 18.740 40.112 1.00 48.64 C ATOM 3174 NH1 ARG D 44 63.932 19.977 40.579 1.00 49.00 N ATOM 3175 NH2 ARG D 44 64.928 17.972 40.109 1.00 49.22 N ATOM 3176 N GLU D 45 57.557 22.627 37.289 1.00 49.76 N ATOM 3177 CA GLU D 45 56.109 22.773 37.106 1.00 50.30 C ATOM 3178 C GLU D 45 55.680 23.011 35.656 1.00 50.71 C ATOM 3179 O GLU D 45 55.824 24.112 35.121 1.00 50.47 O ATOM 3180 CB GLU D 45 55.577 23.905 37.987 1.00 49.49 C ATOM 3181 N LYS D 46 55.135 21.970 35.036 1.00 51.11 N ATOM 3182 CA LYS D 46 54.685 22.040 33.652 1.00 51.83 C ATOM 3183 C LYS D 46 53.616 23.116 33.430 1.00 52.71 C ATOM 3184 O LYS D 46 53.309 23.470 32.289 1.00 52.71 O ATOM 3185 CB LYS D 46 54.140 20.677 33.219 1.00 50.96 C ATOM 3186 N SER D 47 53.057 23.641 34.517 1.00 53.19 N ATOM 3187 CA SER D 47 52.015 24.657 34.418 1.00 53.48 C ATOM 3188 C SER D 47 52.522 26.092 34.336 1.00 52.94 C ATOM 3189 O SER D 47 51.762 26.996 33.983 1.00 52.87 O ATOM 3190 CB SER D 47 51.048 24.543 35.601 1.00 54.05 C ATOM 3191 OG SER D 47 51.734 24.698 36.833 1.00 56.01 O ATOM 3192 N ASP D 48 53.794 26.310 34.664 1.00 52.50 N ATOM 3193 CA ASP D 48 54.362 27.657 34.621 1.00 51.66 C ATOM 3194 C ASP D 48 54.161 28.310 33.254 1.00 50.90 C ATOM 3195 O ASP D 48 54.530 27.745 32.223 1.00 50.75 O ATOM 3196 CB ASP D 48 55.858 27.629 34.961 1.00 51.83 C ATOM 3197 N PRO D 49 53.567 29.516 33.232 1.00 50.14 N ATOM 3198 CA PRO D 49 53.306 30.263 31.996 1.00 49.15 C ATOM 3199 C PRO D 49 54.550 30.820 31.305 1.00 48.42 C ATOM 3200 O PRO D 49 54.472 31.288 30.167 1.00 48.13 O ATOM 3201 CB PRO D 49 52.373 31.380 32.457 1.00 49.52 C ATOM 3202 CG PRO D 49 52.857 31.657 33.855 1.00 49.18 C ATOM 3203 CD PRO D 49 53.052 30.251 34.406 1.00 50.05 C ATOM 3204 N HIS D 50 55.696 30.773 31.981 1.00 46.75 N ATOM 3205 CA HIS D 50 56.916 31.304 31.383 1.00 45.88 C ATOM 3206 C HIS D 50 57.874 30.272 30.765 1.00 44.34 C ATOM 3207 O HIS D 50 59.045 30.570 30.528 1.00 44.23 O ATOM 3208 CB HIS D 50 57.638 32.185 32.405 1.00 45.79 C ATOM 3209 CG HIS D 50 56.829 33.371 32.833 1.00 47.26 C ATOM 3210 ND1 HIS D 50 56.501 34.395 31.970 1.00 47.30 N ATOM 3211 CD2 HIS D 50 56.213 33.657 34.005 1.00 47.36 C ATOM 3212 CE1 HIS D 50 55.715 35.257 32.589 1.00 47.33 C ATOM 3213 NE2 HIS D 50 55.525 34.833 33.824 1.00 47.72 N ATOM 3214 N ILE D 51 57.370 29.068 30.499 1.00 42.18 N ATOM 3215 CA ILE D 51 58.177 28.016 29.871 1.00 41.06 C ATOM 3216 C ILE D 51 57.698 27.771 28.442 1.00 40.46 C ATOM 3217 O ILE D 51 58.264 26.950 27.721 1.00 40.26 O ATOM 3218 CB ILE D 51 58.097 26.665 30.636 1.00 39.75 C ATOM 3219 CG1 ILE D 51 56.647 26.181 30.697 1.00 38.79 C ATOM 3220 CG2 ILE D 51 58.675 26.818 32.030 1.00 38.97 C ATOM 3221 CD1 ILE D 51 56.457 24.914 31.485 1.00 37.44 C ATOM 3222 N LYS D 52 56.639 28.471 28.043 1.00 39.78 N ATOM 3223 CA LYS D 52 56.103 28.345 26.691 1.00 38.80 C ATOM 3224 C LYS D 52 56.999 29.181 25.783 1.00 37.62 C ATOM 3225 O LYS D 52 57.023 30.399 25.881 1.00 37.88 O ATOM 3226 CB LYS D 52 54.663 28.851 26.649 1.00 39.06 C ATOM 3227 CG LYS D 52 54.076 28.941 25.254 1.00 41.38 C ATOM 3228 CD LYS D 52 52.551 29.006 25.306 1.00 43.38 C ATOM 3229 CE LYS D 52 51.956 29.144 23.910 1.00 44.51 C ATOM 3230 NZ LYS D 52 50.463 29.058 23.940 1.00 45.28 N ATOM 3231 N LEU D 53 57.740 28.516 24.903 1.00 35.77 N ATOM 3232 CA LEU D 53 58.677 29.198 24.023 1.00 34.05 C ATOM 3233 C LEU D 53 58.325 29.103 22.546 1.00 33.69 C ATOM 3234 O LEU D 53 57.587 28.220 22.120 1.00 33.77 O ATOM 3235 CB LEU D 53 60.081 28.628 24.246 1.00 32.10 C ATOM 3236 CG LEU D 53 60.438 28.457 25.722 1.00 32.46 C ATOM 3237 CD1 LEU D 53 61.812 27.799 25.873 1.00 30.90 C ATOM 3238 CD2 LEU D 53 60.396 29.827 26.405 1.00 31.78 C ATOM 3239 N GLN D 54 58.859 30.030 21.763 1.00 32.79 N ATOM 3240 CA GLN D 54 58.614 30.018 20.336 1.00 32.41 C ATOM 3241 C GLN D 54 59.953 30.037 19.593 1.00 32.05 C ATOM 3242 O GLN D 54 60.705 31.018 19.659 1.00 31.21 O ATOM 3243 CB GLN D 54 57.748 31.215 19.920 1.00 31.73 C ATOM 3244 CG GLN D 54 57.428 31.249 18.426 1.00 33.58 C ATOM 3245 CD GLN D 54 56.543 30.082 17.970 1.00 35.55 C ATOM 3246 OE1 GLN D 54 55.339 30.051 18.246 1.00 36.89 O ATOM 3247 NE2 GLN D 54 57.144 29.116 17.272 1.00 35.05 N ATOM 3248 N LEU D 55 60.247 28.940 18.896 1.00 31.92 N ATOM 3249 CA LEU D 55 61.481 28.824 18.121 1.00 31.53 C ATOM 3250 C LEU D 55 61.228 29.362 16.717 1.00 30.93 C ATOM 3251 O LEU D 55 60.121 29.248 16.201 1.00 30.58 O ATOM 3252 CB LEU D 55 61.910 27.355 18.008 1.00 32.24 C ATOM 3253 CG LEU D 55 62.556 26.584 19.164 1.00 32.83 C ATOM 3254 CD1 LEU D 55 64.047 26.722 19.085 1.00 33.91 C ATOM 3255 CD2 LEU D 55 62.029 27.063 20.506 1.00 31.56 C ATOM 3256 N GLN D 56 62.252 29.944 16.106 1.00 30.47 N ATOM 3257 CA GLN D 56 62.141 30.473 14.749 1.00 30.30 C ATOM 3258 C GLN D 56 63.520 30.438 14.088 1.00 30.10 C ATOM 3259 O GLN D 56 64.496 30.946 14.636 1.00 29.40 O ATOM 3260 CB GLN D 56 61.587 31.910 14.768 1.00 31.17 C ATOM 3261 CG GLN D 56 61.602 32.646 13.415 1.00 31.41 C ATOM 3262 CD GLN D 56 60.679 32.024 12.367 1.00 32.89 C ATOM 3263 OE1 GLN D 56 59.470 31.897 12.585 1.00 32.67 O ATOM 3264 NE2 GLN D 56 61.247 31.643 11.221 1.00 31.40 N ATOM 3265 N ALA D 57 63.596 29.822 12.912 1.00 30.59 N ATOM 3266 CA ALA D 57 64.863 29.722 12.191 1.00 31.46 C ATOM 3267 C ALA D 57 65.208 31.047 11.514 1.00 31.50 C ATOM 3268 O ALA D 57 64.337 31.689 10.915 1.00 31.96 O ATOM 3269 CB ALA D 57 64.787 28.608 11.148 1.00 31.14 C ATOM 3270 N GLU D 58 66.472 31.455 11.612 1.00 31.48 N ATOM 3271 CA GLU D 58 66.937 32.708 11.003 1.00 31.93 C ATOM 3272 CG GLU D 58 67.651 32.352 9.704 1.00 31.62 C ATOM 3273 O GLU D 58 67.669 33.118 8.743 1.00 32.03 O ATOM 3274 CB GLU D 58 67.902 33.423 11.950 1.00 31.82 C ATOM 3275 CG GLU D 58 68.104 34.897 11.642 1.00 33.93 C ATOM 3276 CD GLU D 58 66.805 35.697 11.682 1.00 33.77 C ATOM 3277 OE1 GLU D 58 65.925 35.394 12.509 1.00 33.41 O ATOM 3278 OE2 GLU D 58 66.673 36.649 10.891 1.00 36.68 O ATOM 3279 N GLU D 59 68.261 31.174 9.707 1.00 32.39 N ATOM 3280 CA GLU D 59 68.956 30.625 8.552 1.00 33.39 C ATOM 3281 C GLU D 59 69.078 29.123 8.824 1.00 32.60 C ATOM 3282 O GLU D 59 68.781 28.661 9.932 1.00 32.53 O ATOM 3283 CB GLU D 59 70.336 31.275 8.365 1.00 34.87 C ATOM 3284 CG GLU D 59 71.455 30.693 9.205 1.00 38.35 C ATOM 3285 CD GLU D 59 72.766 31.445 9.016 1.00 40.56 C ATOM 3286 OE1 GLU D 59 73.170 31.658 7.852 1.00 42.72 O ATOM 3287 OE2 GLU D 59 73.394 31.823 10.028 1.00 40.49 O ATOM 3288 N ARG D 60 69.503 28.357 7.826 1.00 32.00 N ATOM 3289 CA ARG D 60 69.611 26.910 7.992 1.00 32.66 C ATOM 3290 C ARG D 60 70.320 26.475 9.280 1.00 31.35 C ATOM 3291 O ARG D 60 71.459 26.856 9.527 1.00 31.20 O ATOM 3292 CB ARG D 60 70.306 26.295 6.768 1.00 33.95 C ATOM 3293 CG ARG D 60 70.378 24.778 6.814 1.00 36.32 C ATOM 3294 CD ARG D 60 70.800 24.196 5.477 1.00 38.66 C ATOM 3295 NE ARG D 60 71.248 22.825 5.636 1.00 42.38 N ATOM 3296 CZ ARG D 60 72.497 22.472 5.930 1.00 43.93 C ATOM 3297 NH1 ARG D 60 73.440 23.392 6.083 1.00 44.45 N ATOM 3298 NH2 ARG D 60 72.795 21.192 6.099 1.00 45.88 N ATOM 3299 N GLY D 61 69.628 25.696 10.108 1.00 30.50 N ATOM 3300 CA GLY D 61 70.211 25.213 11.354 1.00 29.35 C ATOM 3301 C GLY D 61 70.450 26.224 12.478 1.00 29.03 C ATOM 3302 O GLY D 61 71.051 25.882 13.491 1.00 28.44 O ATOM 3303 N VAL D 62 69.981 27.459 12.311 1.00 28.42 N ATOM 3304 CA VAL D 62 70.151 28.499 13.319 1.00 27.63 C ATOM 3305 C VAL D 62 68.798 29.040 13.787 1.00 27.82 C ATOM 3306 O VAL D 62 67.971 29.435 12.969 1.00 28.05 O ATOM 3307 CB VAL D 62 70.971 29.674 12.755 1.00 28.71 C ATOM 3308 CG1 VAL D 62 71.055 30.802 13.789 1.00 27.45 C ATOM 3309 CG2 VAL D 62 72.370 29.183 12.349 1.00 29.28 C ATOM 3310 N VAL D 63 68.580 29.082 15.098 1.00 27.12 N ATOM 3311 CA VAL D 63 67.309 29.568 15.627 1.00 26.23 C ATOM 3312 C VAL D 63 67.416 30.634 16.721 1.00 27.27 C ATOM 3313 O VAL D 63 68.472 30.824 17.342 1.00 26.15 O ATOM 3314 CB VAL D 63 66.472 28.413 16.250 1.00 26.29 C ATOM 3315 CG1 VAL D 63 66.320 27.251 15.257 1.00 25.11 C ATOM 3316 CG2 VAL D 63 67.135 27.936 17.552 1.00 25.13 C ATOM 3317 N SER D 64 66.295 31.326 16.933 1.00 27.59 N ATOM 3318 CA SER D 64 66.162 32.314 18.003 1.00 28.77 C ATOM 3319 C SER D 64 65.100 31.675 18.897 1.00 28.82 C ATOM 3320 O SER D 64 64.194 31.001 18.398 1.00 29.07 O ATOM 3321 CB SER D 64 65.663 33.662 17.466 1.00 29.15 C ATOM 3322 OG SER D 64 64.344 33.586 16.972 1.00 30.31 O ATOM 3323 N ILE D 65 65.217 31.850 20.206 1.00 29.32 N ATOM 3324 CA ILE D 65 64.256 31.269 21.140 1.00 30.33 C ATOM 3325 C ILE D 65 63.588 32.396 21.941 1.00 31.89 C ATOM 3326 O ILE D 65 64.252 33.113 22.697 1.00 32.70 O ATOM 3327 CB ILE D 65 64.967 30.280 22.087 1.00 29.23 C ATOM 3328 CG1 ILE D 65 65.685 29.209 21.262 1.00 29.54 C ATOM 3329 CG2 ILE D 65 63.967 29.636 23.018 1.00 29.94 C ATOM 3330 CD1 ILE D 65 66.525 28.236 22.086 1.00 28.65 C ATOM 3331 N LYS D 66 62.277 32.544 21.778 1.00 33.04 N ATOM 3332 CA LYS D 66 61.537 33.617 22.439 1.00 34.75 C ATOM 3333 C LYS D 66 60.500 33.186 23.467 1.00 35.49 C ATOM 3334 O LYS D 66 59.659 32.334 23.195 1.00 35.39 O ATOM 3335 CB LYS D 66 60.859 34.481 21.365 1.00 36.40 C ATOM 3336 CG LYS D 66 59.924 35.589 21.865 1.00 38.42 C ATOM 3337 CD LYS D 66 59.419 36.412 20.674 1.00 41.42 C ATOM 3338 CE LYS D 66 58.472 37.543 21.071 1.00 43.03 C ATOM 3339 NZ LYS D 66 57.094 37.064 21.404 1.00 45.12 N ATOM 3340 N GLY D 67 60.573 33.777 24.658 1.00 36.59 N ATOM 3341 CA GLY D 67 59.603 33.471 25.695 1.00 38.30 C ATOM 3342 C GLY D 67 58.311 34.187 25.329 1.00 39.98 C ATOM 3343 O GLY D 67 58.275 35.415 25.269 1.00 39.06 O ATOM 3344 N VAL D 68 57.251 33.428 25.075 1.00 41.48 N ATOM 3345 CA VAL D 68 55.981 34.027 24.679 1.00 43.26 C ATOM 3346 C VAL D 68 55.437 35.015 25.707 1.00 43.98 C ATOM 3347 O VAL D 68 55.105 36.145 25.356 1.00 44.25 O ATOM 3348 CB VAL D 68 54.903 32.942 24.392 1.00 43.86 C ATOM 3349 CG1 VAL D 68 53.635 33.594 23.829 1.00 43.37 C ATOM 3350 CG2 VAL D 68 55.447 31.920 23.400 1.00 43.79 C ATOM 3351 N SER D 69 55.358 34.599 26.970 1.00 44.50 N ATOM 3352 CA SER D 69 54.843 35.468 28.033 1.00 45.32 C ATOM 3353 C SER D 69 55.714 36.707 28.248 1.00 45.20 C ATOM 3354 O SER D 69 55.242 37.840 28.141 1.00 45.09 O ATOM 3355 CB SER D 69 54.724 34.685 29.348 1.00 44.74 C ATOM 3356 N ALA D 70 56.988 36.477 28.541 1.00 45.20 N ATOM 3357 CA ALA D 70 57.942 37.551 28.772 1.00 44.77 C ATOM 3358 C ALA D 70 58.131 38.448 27.555 1.00 45.28 C ATOM 3359 O ALA D 70 58.580 39.586 27.681 1.00 45.68 O ATOM 3360 CB ALA D 70 59.276 36.957 29.175 1.00 45.09 C ATOM 3361 N ASN D 71 57.790 37.934 26.378 1.00 45.22 N ATOM 3362 CA ASN D 71 57.956 38.679 25.136 1.00 45.09 C ATOM 3363 C ASN D 71 59.421 39.113 24.974 1.00 44.75 C ATOM 3364 O ASN D 71 59.706 40.226 24.510 1.00 44.98 O ATOM 3365 CB ASN D 71 57.032 39.907 25.114 1.00 45.04 C ATOM 3366 CG ASN D 71 56.922 40.529 23.729 1.00 45.44 C ATOM 3367 OD1 ASN D 71 56.594 39.849 22.752 1.00 45.94 O ATOM 3368 ND2 ASN D 71 57.188 41.826 23.638 1.00 45.88 N ATOM 3369 N ARG D 72 60.341 38.226 25.357 1.00 43.91 N ATOM 3370 CA ARG D 72 61.780 38.485 25.262 1.00 43.19 C ATOM 3371 C ARG D 72 62.500 37.329 24.560 1.00 42.45 C ATOM 3372 O ARG D 72 61.974 36.219 24.498 1.00 42.53 O ATOM 3373 CB ARG D 72 62.381 38.669 26.658 1.00 43.38 C ATOM 3374 CG ARG D 72 62.019 39.969 27.372 1.00 44.06 C ATOM 3375 CD ARG D 72 62.333 39.815 28.854 1.00 45.57 C ATOM 3376 NE ARG D 72 62.160 41.029 29.650 1.00 46.11 N ATOM 3377 CZ ARG D 72 63.090 41.967 29.807 1.00 46.62 C ATOM 3378 NH1 ARG D 72 64.271 41.847 29.218 1.00 46.83 N ATOM 3379 NH2 ARG D 72 62.853 43.012 30.586 1.00 47.06 N ATOM 3380 N TYR D 73 63.702 37.601 24.046 1.00 40.48 N ATOM 3381 CA TYR D 73 64.516 36.604 23.347 1.00 39.21 C ATOM 3382 C TYR D 73 65.706 36.118 24.165 1.00 38.88 C ATOM 3383 O TYR D 73 66.448 36.918 24.731 1.00 38.06 O ATOM 3384 CB TYR D 73 65.057 37.162 22.027 1.00 38.39 C ATOM 3385 CG TYR D 73 63.982 37.544 21.043 1.00 38.49 C ATOM 3386 CD1 TYR D 73 63.326 38.774 21.137 1.00 37.45 C ATOM 3387 CD2 TYR D 73 63.599 36.664 20.029 1.00 37.61 C ATOM 3388 CE1 TYR D 73 62.316 39.118 20.243 1.00 37.57 C ATOM 3389 CE2 TYR D 73 62.590 36.996 19.134 1.00 37.51 C ATOM 3390 CZ TYR D 73 61.953 38.223 19.245 1.00 37.70 C ATOM 3391 OH TYR D 73 60.957 38.543 18.354 1.00 37.47 O ATOM 3392 N LEU D 74 65.888 34.802 24.205 1.00 38.24 N ATOM 3393 CA LEU D 74 67.000 34.185 24.926 1.00 38.30 C ATOM 3394 C LEU D 74 68.311 34.681 24.328 1.00 38.42 C ATOM 3395 O LEU D 74 68.423 34.834 23.118 1.00 38.39 O ATOM 3396 CB LEU D 74 66.941 32.657 24.786 1.00 38.60 C ATOM 3397 CG LEU D 74 67.984 31.822 25.537 1.00 38.75 C ATOM 3398 CD1 LEU D 74 67.692 31.874 27.037 1.00 38.70 C ATOM 3399 CD2 LEU D 74 67.946 30.384 25.049 1.00 38.55 C ATOM 3400 N ALA D 75 69.301 34.932 25.174 1.00 39.28 N ATOM 3401 CA ALA D 75 70.592 35.402 24.696 1.00 40.08 C ATOM 3402 C ALA D 75 71.714 34.975 25.628 1.00 40.36 C ATOM 3403 O ALA D 75 71.499 34.754 26.820 1.00 38.94 O ATOM 3404 CB ALA D 75 70.580 36.918 24.567 1.00 40.17 C ATOM 3405 N MET D 76 72.912 34.850 25.069 1.00 41.52 N ATOM 3406 CA MET D 76 74.082 34.487 25.853 1.00 43.06 C ATOM 3407 C MET D 76 75.094 35.620 25.732 1.00 44.08 C ATOM 3408 O MET D 76 75.503 35.984 24.628 1.00 43.36 O ATOM 3409 CB MET D 76 74.705 33.194 25.345 1.00 42.43 C ATOM 3410 CG MET D 76 75.868 32.738 26.195 1.00 42.51 C ATOM 3411 SD MET D 76 76.653 31.282 25.525 1.00 43.26 S ATOM 3412 CE MET D 76 75.417 30.042 25.906 1.00 42.34 C ATOM 3413 N LYS D 77 75.487 36.167 26.877 1.00 45.76 N ATOM 3414 CA LYS D 77 76.437 37.272 26.941 1.00 47.47 C ATOM 3415 C LYS D 77 77.891 36.817 26.796 1.00 48.42 C ATOM 3416 O LYS D 77 78.186 35.619 26.823 1.00 47.92 O ATOM 3417 CB LYS D 77 76.246 38.013 28.266 1.00 48.92 C ATOM 3418 CG LYS D 77 74.901 38.733 28.408 1.00 49.43 C ATOM 3419 CD LYS D 77 75.008 40.158 27.884 1.00 51.25 C ATOM 3420 CE LYS D 77 73.707 40.920 28.072 1.00 52.60 C ATOM 3421 NZ LYS D 77 73.836 42.337 27.620 1.00 53.85 N ATOM 3422 N GLU D 78 78.794 37.785 26.648 1.00 49.49 N ATOM 3423 CA GLU D 78 80.219 37.508 26.488 1.00 50.47 C ATOM 3424 C GLU D 78 80.847 36.716 27.641 1.00 51.20 C ATOM 3425 O GLU D 78 81.797 35.967 27.428 1.00 51.18 O ATOM 3426 CB GLU D 78 80.988 38.819 26.290 1.00 50.83 C ATOM 3427 N ASP D 79 80.325 36.875 28.855 1.00 51.96 N ATOM 3428 CA ASP D 79 80.867 36.156 30.011 1.00 52.63 C ATOM 3429 C ASP D 79 80.228 34.778 30.166 1.00 52.67 C ATOM 3430 O ASP D 79 80.521 34.053 31.116 1.00 53.01 O ATOM 3431 CB ASP D 79 80.646 36.957 31.300 1.00 52.97 C ATOM 3432 CG ASP D 79 79.177 37.145 31.622 1.00 53.36 C ATOM 3433 OD1 ASP D 79 78.861 37.653 32.718 1.00 53.30 O ATOM 3434 OD2 ASP D 79 78.334 36.788 30.772 1.00 53.86 O ATOM 3435 N GLY D 80 79.344 34.427 29.237 1.00 52.19 N ATOM 3436 CA GLY D 80 78.691 33.130 29.298 1.00 51.48 C ATOM 3437 C GLY D 80 77.404 33.082 30.105 1.00 50.93 C ATOM 3438 O GLY D 80 76.886 32.000 30.383 1.00 50.90 O ATOM 3439 N ARG D 81 76.875 34.243 30.480 1.00 50.15 N ATOM 3440 CA ARG D 81 75.640 34.286 31.257 1.00 49.57 C ATOM 3441 C ARG D 81 74.415 34.294 30.344 1.00 49.04 C ATOM 3442 O ARG D 81 74.467 34.799 29.222 1.00 48.59 O ATOM 3443 CB ARG D 81 75.622 35.528 32.161 1.00 49.50 C ATOM 3444 N LEU D 82 73.310 33.732 30.824 1.00 48.27 N ATOM 3445 CA LEU D 82 72.083 33.700 30.031 1.00 47.90 C ATOM 3446 C LEU D 82 71.065 34.728 30.517 1.00 48.39 C ATOM 3447 O LEU D 82 70.910 34.940 31.722 1.00 48.80 O ATOM 3448 CB LEU D 82 71.436 32.309 30.081 1.00 46.28 C ATOM 3449 CG LEU D 82 72.140 31.090 29.482 1.00 45.38 C ATOM 3450 CD1 LEU D 82 71.198 29.896 29.554 1.00 44.72 C ATOM 3451 CD2 LEU D 82 72.525 31.357 28.035 1.00 45.05 C ATOM 3452 N LEU D 83 70.380 35.365 29.572 1.00 48.54 N ATOM 3453 CA LEU D 83 69.351 36.349 29.888 1.00 49.02 C ATOM 3454 C LEU D 83 68.410 36.479 28.690 1.00 49.02 C ATOM 3455 O LEU D 83 68.683 35.925 27.628 1.00 49.46 O ATOM 3456 CB LEU D 83 69.979 37.705 30.225 1.00 49.68 C ATOM 3457 CG LEU D 83 70.659 38.558 29.145 1.00 50.40 C ATOM 3458 CD1 LEU D 83 69.660 39.026 28.091 1.00 49.95 C ATOM 3459 CD2 LEU D 83 71.283 39.773 29.829 1.00 51.61 C ATOM 3460 N ALA D 84 67.304 37.202 28.859 1.00 48.84 N ATOM 3461 CA ALA D 84 66.348 37.391 27.767 1.00 48.88 C ATOM 3462 C ALA D 84 66.184 38.876 27.430 1.00 48.68 C ATOM 3463 O ALA D 84 65.796 39.675 28.280 1.00 49.18 O ATOM 3464 CB ALA D 84 65.001 36.773 28.128 1.00 48.28 C ATOM 3465 N SER D 85 66.468 39.233 26.180 1.00 48.45 N ATOM 3466 CA SER D 85 66.383 40.621 25.745 1.00 48.43 C ATOM 3467 C SER D 85 65.078 41.014 25.071 1.00 48.54 C ATOM 3468 O SER D 85 64.424 40.206 24.403 1.00 48.35 O ATOM 3469 CB SER D 85 67.543 40.961 24.815 1.00 47.61 C ATOM 3470 OG SER D 85 67.471 40.180 23.646 1.00 48.73 O ATOM 3471 N LYS D 86 64.714 42.280 25.252 1.00 48.04 N ATOM 3472 CA LYS D 86 63.493 42.814 24.675 1.00 47.48 C ATOM 3473 C LYS D 86 63.627 42.857 23.160 1.00 47.38 C ATOM 3474 O LYS D 86 62.678 42.541 22.431 1.00 47.31 O ATOM 3475 CB LYS D 86 63.219 44.219 25.216 1.00 47.13 C ATOM 3476 N SER D 87 64.811 43.236 22.689 1.00 46.35 N ATOM 3477 CA SER D 87 65.062 43.316 21.258 1.00 46.37 C ATOM 3478 C SER D 87 66.134 42.307 20.825 1.00 45.65 C ATOM 3479 O SER D 87 67.060 42.003 21.572 1.00 45.52 O ATOM 3480 CB SER D 87 65.494 44.741 20.888 1.00 47.49 C ATOM 3481 N VAL D 88 66.000 41.807 19.606 1.00 45.23 N ATOM 3482 CA VAL D 88 66.919 40.827 19.049 1.00 44.31 C ATOM 3483 C VAL D 88 68.320 41.370 18.741 1.00 44.05 C ATOM 3484 O VAL D 88 68.455 42.397 18.083 1.00 44.55 O ATOM 3485 CB VAL D 88 66.328 40.238 17.753 1.00 44.15 C ATOM 3486 CG1 VAL D 88 67.261 39.174 17.182 1.00 43.40 C ATOM 3487 CG2 VAL D 88 64.943 39.660 18.035 1.00 44.10 C ATOM 3488 N THR D 89 69.353 40.677 19.219 1.00 42.84 N ATOM 3489 CA THR D 89 70.739 41.067 18.952 1.00 42.13 C ATOM 3490 C THR D 89 71.487 39.835 18.460 1.00 41.62 C ATOM 3491 O THR D 89 70.918 38.752 18.403 1.00 41.27 O ATOM 3492 CB THR D 89 71.468 41.580 20.203 1.00 41.82 C ATOM 3493 OG1 THR D 89 71.848 40.468 21.024 1.00 41.87 O ATOM 3494 CG2 THR D 89 70.567 42.513 21.001 1.00 42.55 C ATOM 3495 N ASP D 90 72.761 39.999 18.114 1.00 41.36 N ATOM 3496 CA ASP D 90 73.571 38.889 17.616 1.00 41.12 C ATOM 3497 C ASP D 90 73.844 37.802 18.654 1.00 41.18 C ATOM 3498 O ASP D 90 74.408 36.755 18.332 1.00 42.37 O ATOM 3499 CB ASP D 90 74.907 39.412 17.064 1.00 41.11 C ATOM 3500 CG ASP D 90 75.656 40.326 18.051 1.00 41.39 C ATOM 3501 OD1 ASP D 90 75.268 40.402 19.239 1.00 40.75 O ATOM 3502 OD2 ASP D 90 76.651 40.965 17.631 1.00 39.90 O ATOM 3503 N GLU D 91 73.445 38.045 19.897 1.00 40.48 N ATOM 3504 CA GLU D 91 73.662 37.072 20.965 1.00 40.42 C ATOM 3505 C GLU D 91 72.391 36.250 21.201 1.00 38.92 C ATOM 3506 O GLU D 91 72.300 35.498 22.172 1.00 38.93 O ATOM 3507 CB GLU D 91 74.062 37.788 22.265 1.00 40.64 C ATOM 3508 CG GLU D 91 75.140 38.852 22.089 1.00 41.05 C ATOM 3509 CD GLU D 91 75.549 39.509 23.405 1.00 41.33 C ATOM 3510 OE1 GLU D 91 74.670 40.048 24.112 1.00 40.56 O ATOM 3511 OE2 GLU D 91 76.755 39.488 23.728 1.00 42.06 O ATOM 3512 N CYS D 92 71.419 36.386 20.305 1.00 37.53 N ATOM 3513 CA CYS D 92 70.155 35.662 20.434 1.00 37.33 C ATOM 3514 C CYS D 92 69.965 34.523 19.428 1.00 37.35 C ATOM 3515 O CYS D 92 68.857 33.998 19.289 1.00 37.11 O ATOM 3516 CB CYS D 92 68.978 36.631 20.300 1.00 37.57 C ATOM 3517 SG CYS D 92 68.952 37.991 21.499 1.00 36.54 S ATOM 3518 N PHE D 93 71.040 34.133 18.742 1.00 36.58 N ATOM 3519 CA PHE D 93 70.973 33.075 17.742 1.00 35.75 C ATOM 3520 C PHE D 93 71.817 31.858 18.128 1.00 35.61 C ATOM 3521 O PHE D 93 72.961 31.994 18.560 1.00 35.37 O ATOM 3522 CB PHE D 93 71.393 33.654 16.386 1.00 35.89 C ATOM 3523 CG PHE D 93 70.464 34.732 15.889 1.00 36.43 C ATOM 3524 CD1 PHE D 93 69.186 34.414 15.442 1.00 36.23 C ATOM 3525 CD2 PHE D 93 70.831 36.074 15.950 1.00 36.97 C ATOM 3526 CE1 PHE D 93 68.281 35.411 15.069 1.00 36.80 C ATOM 3527 CE2 PHE D 93 69.936 37.079 15.579 1.00 37.17 C ATOM 3528 CZ PHE D 93 68.652 36.743 15.138 1.00 37.41 C ATOM 3529 N PHE D 94 71.244 30.669 17.956 1.00 33.92 N ATOM 3530 CA PHE D 94 71.906 29.435 18.344 1.00 33.26 C ATOM 3531 C PHE D 94 71.802 28.315 17.300 1.00 33.32 C ATOM 3532 O PHE D 94 70.737 28.117 16.689 1.00 32.41 O ATOM 3533 CB PHE D 94 71.279 28.933 19.649 1.00 33.05 C ATOM 3534 CG PHE D 94 71.288 29.944 20.775 1.00 33.05 C ATOM 3535 CD1 PHE D 94 72.357 29.998 21.675 1.00 32.73 C ATOM 3536 CD2 PHE D 94 70.217 30.824 20.952 1.00 32.88 C ATOM 3537 CE1 PHE D 94 72.359 30.906 22.733 1.00 32.76 C ATOM 3538 CE2 PHE D 94 70.206 31.739 22.006 1.00 32.89 C ATOM 3539 CZ PHE D 94 71.279 31.780 22.901 1.00 33.32 C ATOM 3540 N PHE D 95 72.899 27.582 17.109 1.00 31.85 N ATOM 3541 CA PHE D 95 72.899 26.457 16.179 1.00 32.60 C ATOM 3542 C PHE D 95 72.089 25.339 16.844 1.00 32.30 C ATOM 3543 O PHE D 95 72.397 24.938 17.968 1.00 32.05 O ATOM 3544 CB PHE D 95 74.324 25.934 15.923 1.00 33.10 C ATOM 3545 CG PHE D 95 75.195 26.866 15.119 1.00 32.91 C ATOM 3546 CD1 PHE D 95 76.261 27.535 15.721 1.00 33.04 C ATOM 3547 CD2 PHE D 95 74.968 27.055 13.757 1.00 32.86 C ATOM 3548 CE1 PHE D 95 77.097 28.381 14.971 1.00 33.29 C ATOM 3549 CE2 PHE D 95 75.793 27.898 12.997 1.00 33.32 C ATOM 3550 CZ PHE D 95 76.859 28.561 13.607 1.00 32.86 C ATOM 3551 N GLU D 96 71.048 24.854 16.172 1.00 31.87 N ATOM 3552 CA GLU D 96 70.254 23.766 16.733 1.00 32.18 C ATOM 3553 C GLU D 96 70.703 22.471 16.084 1.00 33.15 C ATOM 3554 O GLU D 96 70.798 22.377 14.858 1.00 32.44 O ATOM 3555 CB GLU D 96 68.756 23.928 16.467 1.00 31.12 C ATOM 3556 CG GLU D 96 67.933 22.775 17.062 1.00 29.98 C ATOM 3557 CD GLU D 96 66.498 22.755 16.562 1.00 30.66 C ATOM 3558 OE1 GLU D 96 66.294 22.331 15.406 1.00 30.70 O ATOM 3559 OE2 GLU D 96 65.584 23.166 17.316 1.00 28.95 O ATOM 3560 N ARG D 97 70.958 21.470 16.915 1.00 34.24 N ATOM 3561 CA ARG D 97 71.398 20.178 16.420 1.00 35.69 C ATOM 3562 C ARG D 97 70.717 19.011 17.133 1.00 34.61 C ATOM 3563 O ARG D 97 70.569 19.013 18.353 1.00 33.67 O ATOM 3564 CB ARG D 97 72.918 20.067 16.577 1.00 37.85 C ATOM 3565 CG ARG D 97 73.515 18.742 16.123 1.00 41.19 C ATOM 3566 CD ARG D 97 75.028 18.753 16.275 1.00 43.69 C ATOM 3567 NE ARG D 97 75.620 17.424 16.122 1.00 45.78 N ATOM 3568 CZ ARG D 97 76.905 17.149 16.339 1.00 47.38 C ATOM 3569 NH1 ARG D 97 77.741 18.113 16.717 1.00 47.78 N ATOM 3570 NH2 ARG D 97 77.357 15.908 16.191 1.00 48.28 N ATOM 3571 N LEU D 98 70.281 18.035 16.350 1.00 34.95 N ATOM 3572 CA LEU D 98 69.654 16.827 16.877 1.00 35.44 C ATOM 3573 C LEU D 98 70.809 15.841 17.032 1.00 36.45 C ATOM 3574 O LEU D 98 71.350 15.369 16.036 1.00 36.70 O ATOM 3575 CB LEU D 98 68.644 16.268 15.880 1.00 34.55 C ATOM 3576 CG LEU D 98 68.079 14.873 16.199 1.00 35.46 C ATOM 3577 CD1 LEU D 98 67.448 14.843 17.582 1.00 32.80 C ATOM 3578 CD2 LEU D 98 67.048 14.506 15.135 1.00 35.91 C ATOM 3579 N GLU D 99 71.208 15.550 18.270 1.00 38.33 N ATOM 3580 CA GLU D 99 72.325 14.628 18.518 1.00 38.88 C ATOM 3581 C GLU D 99 71.920 13.181 18.270 1.00 40.14 C ATOM 3582 O GLU D 99 70.729 12.846 18.213 1.00 39.39 O ATOM 3583 CB GLU D 99 72.847 14.748 19.965 1.00 39.75 C ATOM 3584 CG GLU D 99 73.198 16.162 20.442 1.00 41.74 C ATOM 3585 CD GLU D 99 74.502 16.716 19.866 1.00 43.10 C ATOM 3586 OE1 GLU D 99 74.743 17.936 20.020 1.00 42.78 O ATOM 3587 OE2 GLU D 99 75.287 15.943 19.271 1.00 43.51 O ATOM 3588 N SER D 100 72.928 12.321 18.143 1.00 40.94 N ATOM 3589 CA SER D 100 72.715 10.898 17.900 1.00 40.80 C ATOM 3590 C SER D 100 71.904 10.244 19.011 1.00 39.91 C ATOM 3591 O SER D 100 71.263 9.208 18.803 1.00 40.88 O ATOM 3592 CB SER D 100 74.071 10.190 17.741 1.00 42.60 C ATOM 3593 OG SER D 100 74.947 10.490 18.817 1.00 44.54 O ATOM 3594 N ASN D 101 71.932 10.845 20.195 1.00 38.36 N ATOM 3595 CA ASN D 101 71.177 10.321 21.332 1.00 36.69 C ATOM 3596 C ASN D 101 69.696 10.749 21.276 1.00 35.64 C ATOM 3597 O ASN D 101 68.899 10.398 22.150 1.00 35.66 O ATOM 3598 CB ASN D 101 71.804 10.803 22.651 1.00 38.65 C ATOM 3599 CG ASN D 101 72.075 12.313 22.666 1.00 40.05 C ATOM 3600 CD1 ASN D 101 71.369 13.092 22.022 1.00 41.26 O ATOM 3601 ND2 ASN D 101 73.096 12.726 23.415 1.00 39.62 N ATOM 3602 N ASN D 102 69.349 11.507 20.239 1.00 33.81 N ATOM 3603 CA ASN D 102 68.002 12.019 20.009 1.00 32.56 C ATOM 3604 C ASN D 102 67.522 13.171 20.899 1.00 31.26 C ATOM 3605 O ASN D 102 66.317 13.381 21.053 1.00 29.28 O ATOM 3606 CB ASN D 102 66.970 10.883 20.007 1.00 32.99 C ATOM 3607 CG ASN D 102 66.878 10.190 18.649 1.00 35.04 C ATOM 3608 OD1 ASN D 102 67.072 10.824 17.608 1.00 35.88 O ATOM 3609 ND2 ASN D 102 66.571 8.894 18.654 1.00 35.03 N ATOM 3610 N TYR D 103 68.476 13.907 21.474 1.00 29.52 N ATOM 3611 CA TYR D 103 68.196 15.085 22.292 1.00 27.94 C ATOM 3612 C TYR D 103 68.703 16.265 21.454 1.00 27.63 C ATOM 3613 O TYR D 103 69.495 16.081 20.533 1.00 27.55 O ATOM 3614 CB TYR D 103 68.960 15.030 23.615 1.00 26.70 C ATOM 3615 CG TYR D 103 68.322 14.163 24.679 1.00 26.44 C ATOM 3616 CD1 TYR D 103 67.350 14.677 25.540 1.00 26.62 C ATOM 3617 CD2 TYR D 103 68.686 12.822 24.825 1.00 26.07 C ATOM 3618 CE1 TYR D 103 66.759 13.869 26.525 1.00 26.64 C ATOM 3619 CE2 TYR D 103 68.101 12.015 25.797 1.00 25.54 C ATOM 3620 CZ TYR D 103 67.146 12.537 26.638 1.00 26.07 C ATOM 3621 OH TYR D 103 66.562 11.727 27.578 1.00 26.51 O ATOM 3622 N ASN D 104 68.248 17.472 21.757 1.00 27.05 N ATOM 3623 CA ASN D 104 68.686 18.651 21.008 1.00 27.18 C ATOM 3624 C ASN D 104 69.728 19.441 21.803 1.00 26.18 C ATOM 3625 O ASN D 104 69.762 19.364 23.030 1.00 25.52 O ATOM 3626 CB ASN D 104 67.497 19.581 20.732 1.00 28.01 C ATOM 3627 CG ASN D 104 66.696 19.179 19.503 1.00 29.43 C ATOM 3628 OD1 ASN D 104 66.739 18.037 19.054 1.00 29.97 O ATOM 3629 ND2 ASN D 104 65.949 20.129 18.962 1.00 29.97 N ATOM 3630 N THR D 105 70.583 20.177 21.095 1.00 25.93 N ATOM 3631 CA THR D 105 71.567 21.047 21.745 1.00 26.23 C ATOM 3632 C THR D 105 71.494 22.398 21.050 1.00 26.45 C ATOM 3633 O THR D 105 71.169 22.481 19.858 1.00 25.80 O ATOM 3634 CB THR D 105 73.027 20.518 21.667 1.00 26.04 C ATOM 3635 OG1 THR D 105 73.457 20.456 20.300 1.00 26.82 O ATOM 3636 CG2 THR D 105 73.132 19.158 22.319 1.00 26.71 C ATOM 3637 N TYR D 106 71.792 23.453 21.804 1.00 27.12 N ATOM 3638 CA TYR D 106 71.751 24.815 21.291 1.00 27.86 C ATOM 3639 C TYR D 106 73.087 25.500 21.565 1.00 29.60 C ATOM 3640 O TYR D 106 73.414 25.799 22.714 1.00 29.29 O ATOM 3641 CB TYR D 106 70.590 25.551 21.966 1.00 26.16 C ATOM 3642 CG TYR D 106 69.281 24.950 21.546 1.00 25.64 C ATOM 3643 CD1 TYR D 106 68.707 25.285 20.316 1.00 24.14 C ATOM 3644 CD2 TYR D 106 68.671 23.958 22.314 1.00 23.58 C ATOM 3645 CE1 TYR D 106 67.567 24.636 19.856 1.00 25.46 C ATOM 3646 CE2 TYR D 106 67.533 23.301 21.861 1.00 25.15 C ATOM 3647 CZ TYR D 106 66.988 23.643 20.631 1.00 24.17 C ATOM 3648 OH TYR D 106 65.902 22.965 20.148 1.00 24.91 O ATOM 3649 N ARG D 107 73.845 25.732 20.494 1.00 31.16 N ATOM 3650 CA ARG D 107 75.174 26.336 20.574 1.00 32.67 C ATOM 3651 C ARG D 107 75.199 27.760 20.030 1.00 33.24 C ATOM 3652 O ARG D 107 74.730 28.020 18.924 1.00 33.30 O ATOM 3653 CB ARG D 107 76.158 25.463 19.798 1.00 32.67 C ATOM 3654 CG ARG D 107 77.603 25.889 19.865 1.00 32.58 C ATOM 3655 CD ARG D 107 78.476 24.804 19.241 1.00 31.51 C ATOM 3656 NE ARG D 107 78.094 24.520 17.862 1.00 29.79 N ATOM 3657 CZ ARG D 107 78.500 25.227 16.814 1.00 31.11 C ATOM 3658 NH1 ARG D 107 79.311 26.267 16.989 1.00 31.22 N ATOM 3659 NH2 ARG D 107 78.104 24.899 15.589 1.00 29.39 N ATOM 3660 N SER D 108 75.752 28.676 20.822 1.00 34.39 N ATOM 3661 CA SER D 108 75.843 30.091 20.456 1.00 35.36 C ATOM 3662 C SER D 108 76.526 30.316 19.108 1.00 36.03 C ATOM 3663 O SER D 108 77.611 29.789 18.861 1.00 36.15 O ATOM 3664 CB SER D 108 76.600 30.858 21.551 1.00 35.17 C ATOM 3665 OG SER D 108 76.895 32.186 21.163 1.00 33.39 O ATOM 3666 N ARG D 109 75.889 31.092 18.233 1.00 36.63 N ATOM 3667 CA ARG D 109 76.480 31.373 16.930 1.00 38.27 C ATOM 3668 C ARG D 109 77.601 32.401 17.088 1.00 39.85 C ATOM 3669 O ARG D 109 78.510 32.460 16.264 1.00 40.21 O ATOM 3670 CB ARG D 109 75.426 31.906 15.946 1.00 37.43 C ATOM 3671 CG ARG D 109 75.960 32.088 14.509 1.00 36.51 C ATOM 3672 CD ARG D 109 74.879 32.531 13.518 1.00 35.80 C ATOM 3673 NE ARG D 109 74.373 33.875 13.799 1.00 36.06 N ATOM 3674 CZ ARG D 109 73.471 34.516 13.055 1.00 35.79 C ATOM 3675 NH1 ARG D 109 72.962 33.941 11.977 1.00 35.72 N ATOM 3676 NH2 ARG D 109 73.076 35.740 13.385 1.00 34.84 N ATOM 3677 N LYS D 110 77.535 33.202 18.153 1.00 41.38 N ATOM 3678 CA LYS D 110 78.548 34.224 18.409 1.00 42.34 C ATOM 3679 C LYS D 110 79.756 33.629 19.142 1.00 42.60 C ATOM 3680 O LYS D 110 80.887 33.701 18.654 1.00 42.50 O ATOM 3681 CB LYS D 110 77.950 35.372 19.228 1.00 43.39 C ATOM 3682 CG LYS D 110 78.764 36.671 19.157 1.00 45.14 C ATOM 3683 CD LYS D 110 78.184 37.733 20.089 1.00 46.94 C ATOM 3684 CE LYS D 110 78.868 39.075 19.907 1.00 46.68 C ATOM 3685 NZ LYS D 110 78.587 39.607 18.551 1.00 48.63 N ATOM 3686 N TYR D 111 79.505 33.048 20.313 1.00 42.45 N ATOM 3687 CA TYR D 111 80.536 32.405 21.121 1.00 42.43 C ATOM 3688 C TYR D 111 80.366 30.917 20.802 1.00 41.95 C ATOM 3689 O TYR D 111 79.767 30.157 21.567 1.00 41.52 O ATOM 3690 CB TYR D 111 80.276 32.716 22.604 1.00 42.93 C ATOM 3691 CG TYR D 111 80.008 34.192 22.835 1.00 44.45 C ATOM 3692 CD1 TYR D 111 81.028 35.142 22.685 1.00 44.58 C ATOM 3693 CD2 TYR D 111 78.716 34.656 23.100 1.00 44.75 C ATOM 3694 CE1 TYR D 111 80.763 36.515 22.779 1.00 44.52 C ATOM 3695 CE2 TYR D 111 78.439 36.035 23.198 1.00 44.98 C ATOM 3696 CZ TYR D 111 79.468 36.958 23.031 1.00 44.96 C ATOM 3697 OH TYR D 111 79.198 38.313 23.072 1.00 43.46 O ATOM 3698 N THR D 112 80.900 30.530 19.647 1.00 41.87 N ATOM 3699 CA THR D 112 80.780 29.176 19.106 1.00 42.40 C ATOM 3700 C THR D 112 81.192 27.950 19.913 1.00 42.28 C ATOM 3701 O THR D 112 81.138 26.839 19.395 1.00 42.54 O ATOM 3702 CB THR D 112 81.475 29.082 17.731 1.00 42.16 C ATOM 3703 OG1 THR D 112 82.874 29.351 17.884 1.00 41.13 O ATOM 3704 CG2 THR D 112 80.859 30.088 16.748 1.00 41.44 C ATOM 3705 N SER D 113 81.587 28.118 21.168 1.00 42.10 N ATOM 3706 CA SER D 113 81.975 26.954 21.955 1.00 42.41 C ATOM 3707 C SER D 113 81.080 26.724 23.163 1.00 41.80 C ATOM 3708 O SER D 113 81.165 25.685 23.822 1.00 41.36 O ATOM 3709 CB SER D 113 83.435 27.081 22.409 1.00 42.58 C ATOM 3710 OG SER D 113 84.313 26.966 21.300 1.00 42.66 O ATOM 3711 N TRP D 114 80.213 27.686 23.445 1.00 41.58 N ATOM 3712 CA TRP D 114 79.332 27.576 24.599 1.00 41.47 C ATOM 3713 C TRP D 114 77.904 27.130 24.259 1.00 39.93 C ATOM 3714 O TRP D 114 77.361 27.475 23.206 1.00 39.72 O ATOM 3715 CB TRP D 114 79.332 28.910 25.356 1.00 43.57 C ATOM 3716 CG TRP D 114 80.737 29.376 25.716 1.00 46.05 C ATOM 3717 CD1 TRP D 114 81.863 28.593 25.827 1.00 46.16 C ATOM 3718 CD2 TRP D 114 81.150 30.713 26.040 1.00 46.32 C ATOM 3719 NE1 TRP D 114 82.943 29.363 26.198 1.00 46.71 N ATOM 3720 CE2 TRP D 114 82.536 30.665 26.336 1.00 47.01 C ATOM 3721 CE3 TRP D 114 80.486 31.947 26.110 1.00 47.32 C ATOM 3722 CZ2 TRP D 114 83.265 31.805 26.699 1.00 47.13 C ATOM 3723 CZ3 TRP D 114 81.216 33.085 26.469 1.00 47.34 C ATOM 3724 CH2 TRP D 114 82.589 33.002 26.759 1.00 47.61 C ATOM 3725 N TYR D 115 77.314 26.356 25.168 1.00 38.33 N ATOM 3726 CA TYR D 115 75.960 25.828 25.006 1.00 36.97 C ATOM 3727 C TYR D 115 74.963 26.369 26.025 1.00 36.33 C ATOM 3728 O TYR D 115 75.331 26.736 27.138 1.00 35.87 O ATOM 3729 CB TYR D 115 75.942 24.304 25.164 1.00 36.22 C ATOM 3730 CG TYR D 115 76.677 23.519 24.111 1.00 36.66 C ATOM 3731 CD1 TYR D 115 78.025 23.190 24.268 1.00 36.79 C ATOM 3732 CD2 TYR D 115 76.019 23.076 22.965 1.00 36.10 C ATOM 3733 CE1 TYR D 115 78.701 22.430 23.303 1.00 36.07 C ATOM 3734 CE2 TYR D 115 76.683 22.319 21.998 1.00 36.64 C ATOM 3735 CZ TYR D 115 78.024 22.001 22.174 1.00 36.29 C ATOM 3736 OH TYR D 115 78.680 21.264 21.215 1.00 37.12 O ATOM 3737 N VAL D 116 73.695 26.407 25.635 1.00 35.23 N ATOM 3738 CA VAL D 116 72.642 26.819 26.551 1.00 34.37 C ATOM 3739 C VAL D 116 72.531 25.584 27.446 1.00 34.42 C ATOM 3740 O VAL D 116 72.486 24.459 26.952 1.00 34.27 O ATOM 3741 CB VAL D 116 71.323 27.074 25.793 1.00 34.00 C ATOM 3742 CG1 VAL D 116 70.193 27.308 26.770 1.00 33.39 C ATOM 3743 CG2 VAL D 116 71.488 28.278 24.859 1.00 32.59 C ATOM 3744 N ALA D 117 72.516 25.782 28.758 1.00 34.87 N ATOM 3745 CA ALA D 117 72.467 24.649 29.670 1.00 35.64 C ATOM 3746 C ALA D 117 71.928 25.005 31.042 1.00 36.78 C ATOM 3747 O ALA D 117 71.969 26.163 31.464 1.00 37.35 O ATOM 3748 CB ALA D 117 73.860 24.049 29.816 1.00 34.13 C ATOM 3749 N LEU D 118 71.436 23.989 31.741 1.00 37.10 N ATOM 3750 CA LEU D 118 70.900 24.169 33.077 1.00 38.06 C ATOM 3751 C LEU D 118 71.645 23.263 34.048 1.00 38.81 C ATOM 3752 O LEU D 118 72.098 22.184 33.670 1.00 39.30 O ATOM 3753 CB LEU D 118 69.407 23.837 33.094 1.00 37.70 C ATOM 3754 CG LEU D 118 68.470 24.742 32.287 1.00 37.45 C ATOM 3755 CD1 LEU D 118 67.059 24.204 32.409 1.00 37.34 C ATOM 3756 CD2 LEU D 118 68.536 26.189 32.801 1.00 37.18 C ATOM 3757 N LYS D 119 71.773 23.709 35.294 1.00 40.12 N ATOM 3758 CA LYS D 119 72.457 22.938 36.332 1.00 41.45 C ATOM 3759 C LYS D 119 71.459 22.071 37.089 1.00 41.83 C ATOM 3760 O LYS D 119 70.251 22.332 37.059 1.00 41.78 O ATOM 3761 CB LYS D 119 73.172 23.882 37.311 1.00 41.32 C ATOM 3762 N ARG D 120 71.967 21.044 37.767 1.00 41.92 N ATOM 3763 CA ARG D 120 71.121 20.127 38.531 1.00 42.76 C ATOM 3764 C ARG D 120 70.283 20.873 39.562 1.00 43.01 C ATOM 3765 O ARG D 120 69.272 20.367 40.036 1.00 42.82 O ATOM 3766 CB ARG D 120 71.977 19.066 39.232 1.00 41.45 C ATOM 3767 N THR D 121 70.705 22.087 39.896 1.00 44.40 N ATOM 3768 CA THR D 121 70.002 22.902 40.878 1.00 45.13 C ATOM 3769 C THR D 121 68.783 23.614 40.294 1.00 45.85 C ATOM 3770 O THR D 121 67.838 23.928 41.015 1.00 46.11 O ATOM 3771 CB THR D 121 70.938 23.968 41.492 1.00 45.88 C ATOM 3772 OG1 THR D 121 71.355 24.884 40.474 1.00 46.18 O ATOM 3773 CG2 THR D 121 72.170 23.311 42.107 1.00 45.54 C ATOM 3774 N GLY D 122 68.795 23.861 38.990 1.00 46.02 N ATOM 3775 CA GLY D 122 67.676 24.550 38.380 1.00 46.48 C ATOM 3776 C GLY D 122 68.100 25.922 37.901 1.00 47.04 C ATOM 3777 O GLY D 122 67.324 26.662 37.291 1.00 47.14 O ATOM 3778 N GLN D 123 69.348 26.269 38.191 1.00 47.07 N ATOM 3779 CA GLN D 123 69.901 27.544 37.766 1.00 47.46 C ATOM 3780 C GLN D 123 70.659 27.275 36.471 1.00 47.19 C ATOM 3781 O GLN D 123 71.162 26.169 36.261 1.00 46.75 O ATOM 3782 CB GLN D 123 70.844 28.091 38.841 1.00 48.11 C ATOM 3783 CG GLN D 123 70.171 28.283 40.208 1.00 50.27 C ATOM 3784 CD GLN D 123 68.986 29.255 40.164 1.00 51.25 C ATOM 3785 OE1 GLN D 123 69.148 30.434 39.844 1.00 52.08 O ATOM 3786 NE2 GLN D 123 67.792 28.758 40.488 1.00 52.19 N ATOM 3787 N TYR D 124 70.728 28.266 35.589 1.00 46.86 N ATOM 3788 CA TYR D 124 71.437 28.057 34.334 1.00 46.79 C ATOM 3789 C TYR D 124 72.906 27.787 34.621 1.00 46.37 C ATOM 3790 O TYR D 124 73.376 28.001 35.732 1.00 45.85 O ATOM 3791 CB TYR D 124 71.280 29.267 33.392 1.00 46.13 C ATOM 3792 CG TYR D 124 71.982 30.538 33.819 1.00 46.17 C ATOM 3793 CD1 TYR D 124 73.378 30.606 33.889 1.00 46.43 C ATOM 3794 CD2 TYR D 124 71.255 31.679 34.141 1.00 46.18 C ATOM 3795 CE1 TYR D 124 74.027 31.773 34.271 1.00 45.82 C ATOM 3796 CE2 TYR D 124 71.895 32.855 34.525 1.00 46.61 C ATOM 3797 CZ TYR D 124 73.281 32.893 34.588 1.00 46.75 C ATOM 3798 OH TYR D 124 73.916 34.050 34.968 1.00 46.83 O ATOM 3799 N LYS D 125 73.623 27.309 33.614 1.00 46.56 N ATOM 3800 CA LYS D 125 75.037 27.012 33.753 1.00 46.99 C ATOM 3801 C LYS D 125 75.827 27.925 32.810 1.00 48.06 C ATOM 3802 O LYS D 125 75.468 28.063 31.639 1.00 47.64 O ATOM 3803 CB LYS D 125 75.286 25.536 33.412 1.00 46.02 C ATOM 3804 CG LYS D 125 76.737 25.092 33.511 1.00 44.48 C ATOM 3805 CD LYS D 125 76.882 23.588 33.317 1.00 43.98 C ATOM 3806 CE LYS D 125 78.340 23.164 33.502 1.00 44.57 C ATOM 3807 NZ LYS D 125 78.571 21.693 33.380 1.00 44.60 N ATOM 3808 N LEU D 126 76.885 28.557 33.326 1.00 49.01 N ATOM 3809 CA LEU D 126 77.709 29.456 32.515 1.00 49.83 C ATOM 3810 C LEU D 126 78.138 28.779 31.227 1.00 50.46 C ATOM 3811 O LEU D 126 78.679 27.671 31.249 1.00 50.50 O ATOM 3812 CB LEU D 126 78.961 29.896 33.275 1.00 50.45 C ATOM 3813 CG LEU D 126 78.867 31.113 34.195 1.00 50.81 C ATOM 3814 CD1 LEU D 126 80.256 31.435 34.713 1.00 51.18 C ATOM 3815 CD2 LEU D 126 78.300 32.310 33.440 1.00 51.05 C ATOM 3816 N GLY D 127 77.902 29.451 30.107 1.00 50.73 N ATOM 3817 CA GLY D 127 78.273 28.887 28.825 1.00 51.40 C ATOM 3818 C GLY D 127 79.724 28.447 28.784 1.00 51.76 C ATOM 3819 O GLY D 127 80.065 27.458 28.135 1.00 51.74 O ATOM 3820 N SER D 128 80.581 29.181 29.485 1.00 52.20 N ATOM 3821 CA SER D 128 82.009 28.877 29.517 1.00 52.38 C ATOM 3822 C SER D 128 82.332 27.552 30.204 1.00 52.36 C ATOM 3823 O SER D 128 83.422 27.010 30.032 1.00 52.38 O ATOM 3824 CB SER D 128 82.766 30.015 30.210 1.00 51.84 C ATOM 3825 OG SER D 128 82.245 30.256 31.508 1.00 52.17 O ATOM 3826 N LYS D 129 81.385 27.032 30.978 1.00 52.20 N ATOM 3827 CA LYS D 129 81.603 25.778 31.679 1.00 51.76 C ATOM 3828 C LYS D 129 80.881 24.603 31.022 1.00 51.64 C ATOM 3829 O LYS D 129 80.761 23.531 31.626 1.00 51.64 O ATOM 3830 CB LYS D 129 81.163 25.914 33.141 1.00 51.90 C ATOM 3831 N THR D 130 80.414 24.795 29.788 1.00 50.58 N ATOM 3832 CA THR D 130 79.702 23.732 29.073 1.00 49.71 C ATOM 3833 C THR D 130 80.607 22.981 28.093 1.00 49.74 C ATOM 3834 O THR D 130 81.644 23.495 27.668 1.00 49.14 O ATOM 3835 CB THR D 130 78.464 24.285 28.296 1.00 48.64 C ATOM 3836 OG1 THR D 130 78.893 25.121 27.217 1.00 47.18 O ATOM 3837 CG2 THR D 130 77.579 25.098 29.223 1.00 47.63 C ATOM 3838 N GLY D 131 80.197 21.763 27.748 1.00 49.99 N ATOM 3839 CA GLY D 131 80.957 20.932 26.831 1.00 50.29 C ATOM 3840 C GLY D 131 80.034 19.973 26.106 1.00 50.69 C ATOM 3841 O GLY D 131 78.958 19.665 26.611 1.00 50.84 O ATOM 3842 N PRO D 132 80.436 19.460 24.932 1.00 50.75 N ATOM 3843 CA PRO D 132 79.650 18.532 24.114 1.00 50.96 C ATOM 3844 C PRO D 132 79.156 17.236 24.755 1.00 50.84 C ATOM 3845 O PRO D 132 78.126 16.697 24.342 1.00 51.32 O ATOM 3846 CB PRO D 132 80.564 18.266 22.922 1.00 50.45 C ATOM 3847 CG PRO D 132 81.915 18.352 23.534 1.00 51.47 C ATOM 3848 CD PRO D 132 81.794 19.599 24.383 1.00 50.85 C ATOM 3849 N GLY D 133 79.866 16.729 25.755 1.00 50.62 N ATOM 3850 CA GLY D 133 79.423 15.487 26.368 1.00 50.28 C ATOM 3851 C GLY D 133 78.620 15.632 27.653 1.00 49.91 C ATOM 3852 O GLY D 133 78.214 14.631 28.251 1.00 50.17 O ATOM 3853 N GLN D 134 78.365 16.868 28.072 1.00 48.40 N ATOM 3854 CA GLN D 134 77.634 17.100 29.317 1.00 46.81 C ATOM 3855 C GLN D 134 76.134 16.832 29.238 1.00 45.15 C ATOM 3856 O GLN D 134 75.516 16.930 28.177 1.00 46.04 O ATOM 3857 CB GLN D 134 77.873 18.531 29.811 1.00 46.96 C ATOM 3858 CG GLN D 134 79.338 18.926 29.846 1.00 47.70 C ATOM 3859 CD GLN D 134 79.558 20.326 30.386 1.00 47.89 C ATOM 3860 OE1 GLN D 134 78.691 21.188 30.283 1.00 47.89 O ATOM 3861 NE2 GLN D 134 80.735 20.562 30.948 1.00 48.55 N ATOM 3862 N LYS D 135 75.561 16.497 30.386 1.00 42.43 N ATOM 3863 CA LYS D 135 74.137 16.218 30.512 1.00 40.19 C ATOM 3864 C LYS D 135 73.340 17.526 30.594 1.00 38.53 C ATOM 3865 O LYS D 135 72.152 17.557 30.285 1.00 37.67 O ATOM 3866 CB LYS D 135 73.897 15.394 31.777 1.00 40.03 C ATOM 3867 CG LYS D 135 72.472 14.945 32.004 1.00 41.05 C ATOM 3868 CD LYS D 135 72.397 14.061 33.240 1.00 42.04 C ATOM 3869 CE LYS D 135 71.022 13.439 33.391 1.00 44.23 C ATOM 3870 NZ LYS D 135 70.910 12.597 34.613 1.00 44.81 N ATOM 3871 N ALA D 136 74.015 18.599 30.999 1.00 36.85 N ATOM 3872 CA ALA D 136 73.396 19.914 31.159 1.00 35.15 C ATOM 3873 C ALA D 136 72.975 20.606 29.865 1.00 34.16 C ATOM 3874 O ALA D 136 72.150 21.519 29.895 1.00 34.00 O ATOM 3875 CB ALA D 136 74.333 20.825 31.935 1.00 35.72 C ATOM 3876 N ILE D 137 73.531 20.180 28.733 1.00 32.28 N ATOM 3877 CA ILE D 137 73.203 20.799 27.448 1.00 31.23 C ATOM 3878 C ILE D 137 72.155 20.046 26.610 1.00 29.99 C ATOM 3879 O ILE D 137 71.809 20.487 25.512 1.00 28.99 O ATOM 3880 CB ILE D 137 74.457 20.948 26.562 1.00 31.38 C ATOM 3881 CG1 ILE D 137 74.947 19.568 26.118 1.00 31.67 C ATOM 3882 CG2 ILE D 137 75.565 21.644 27.333 1.00 31.93 C ATOM 3883 CD1 ILE D 137 75.937 19.625 24.952 1.00 31.85 C ATOM 3884 N LEU D 138 71.654 18.925 27.126 1.00 28.53 N ATOM 3885 CA LEU D 138 70.688 18.110 26.390 1.00 28.11 C ATOM 3886 C LEU D 138 69.227 18.469 26.674 1.00 27.53 C ATOM 3887 O LEU D 138 68.759 18.376 27.804 1.00 26.19 O ATOM 3888 CB LEU D 138 70.953 16.626 26.681 1.00 27.39 C ATOM 3889 CG LEU D 138 72.392 16.167 26.347 1.00 27.32 C ATOM 3890 CD1 LEU D 138 72.682 14.832 27.011 1.00 26.61 C ATOM 3891 CD2 LEU D 138 72.600 16.079 24.829 1.00 25.73 C ATOM 3892 N PHE D 139 68.521 18.878 25.622 1.00 27.78 N ATOM 3893 CA PHE D 139 67.125 19.281 25.725 1.00 27.77 C ATOM 3894 C PHE D 139 66.203 18.467 24.832 1.00 28.45 C ATOM 3895 O PHE D 139 66.593 18.021 23.752 1.00 27.88 O ATOM 3896 CB PHE D 139 66.977 20.753 25.336 1.00 27.55 C ATOM 3897 CG PHE D 139 67.586 21.709 26.317 1.00 28.64 C ATOM 3898 CD1 PHE D 139 68.936 22.036 26.249 1.00 28.56 C ATOM 3899 CD2 PHE D 139 66.808 22.275 27.324 1.00 28.87 C ATOM 3900 CE1 PHE D 139 69.504 22.913 27.173 1.00 30.32 C ATOM 3901 CE2 PHE D 139 67.365 23.152 28.255 1.00 29.77 C ATOM 3902 CZ PHE D 139 68.719 23.472 28.179 1.00 29.35 C ATOM 3903 N LEU D 140 64.960 18.314 25.271 1.00 28.29 N ATOM 3904 CA LEU D 140 63.966 17.586 24.501 1.00 28.59 C ATOM 3905 C LEU D 140 62.785 18.526 24.250 1.00 29.50 C ATOM 3906 O LEU D 140 62.099 18.943 25.187 1.00 29.38 O ATOM 3907 CB LEU D 140 63.496 16.359 25.281 1.00 29.24 C ATOM 3908 CG LEU D 140 62.673 15.280 24.567 1.00 31.29 C ATOM 3909 CD1 LEU D 140 63.522 14.623 23.477 1.00 31.65 C ATOM 3910 CD2 LEU D 140 62.212 14.221 25.592 1.00 30.86 C ATOM 3911 N PRO D 141 62.548 18.903 22.985 1.00 30.09 N ATOM 3912 CA PRO D 141 61.418 19.795 22.727 1.00 31.12 C ATOM 3913 C PRO D 141 60.091 19.067 22.980 1.00 32.93 C ATOM 3914 O PRO D 141 59.897 17.931 22.533 1.00 32.97 O ATOM 3915 CB PRO D 141 61.607 20.184 21.260 1.00 30.79 C ATOM 3916 CG PRO D 141 62.294 18.994 20.689 1.00 32.15 C ATOM 3917 CD PRO D 141 63.310 18.658 21.747 1.00 29.91 C ATOM 3918 N MET D 142 59.194 19.718 23.716 1.00 33.86 N ATOM 3919 CA MET D 142 57.892 19.132 24.030 1.00 35.77 C ATOM 3920 C MET D 142 56.747 20.096 23.728 1.00 36.97 C ATOM 3921 O MET D 142 56.921 21.317 23.711 1.00 36.81 O ATOM 3922 CB MET D 142 57.820 18.728 25.511 1.00 35.48 C ATOM 3923 CG MET D 142 58.802 17.641 25.919 1.00 35.60 C ATOM 3924 SD MET D 142 58.757 17.282 27.684 1.00 36.85 S ATOM 3925 CE MET D 142 57.505 15.979 27.723 1.00 35.78 C ATOM 3926 N SER D 143 55.572 19.529 23.499 1.00 38.75 N ATOM 3927 CA SER D 143 54.375 20.304 23.202 1.00 40.93 C ATOM 3928 C SER D 143 54.012 21.269 24.320 1.00 41.71 C ATOM 3929 O SER D 143 54.180 20.966 25.502 1.00 40.96 O ATOM 3930 CB SER D 143 53.194 19.362 22.976 1.00 41.49 C ATOM 3931 OG SER D 143 51.973 20.068 23.054 1.00 43.53 O ATOM 3932 N ALA D 144 53.508 22.435 23.939 1.00 43.61 N ATOM 3933 CA ALA D 144 53.092 23.430 24.915 1.00 46.08 C ATOM 3934 C ALA D 144 51.644 23.151 25.325 1.00 47.46 C ATOM 3935 O ALA D 144 50.915 24.060 25.720 1.00 48.06 O ATOM 3936 CB ALA D 144 53.210 24.815 24.319 1.00 46.29 C ATOM 3937 N LYS D 145 51.239 21.885 25.223 1.00 48.83 N ATOM 3938 CA LYS D 145 49.887 21.465 25.587 1.00 50.09 C ATOM 3939 C LYS D 145 48.841 22.277 24.834 1.00 50.66 C ATOM 3940 O LYS D 145 48.764 22.067 23.603 1.00 51.83 O ATOM 3941 CB LYS D 145 49.679 21.615 27.099 1.00 49.26 C TER 3942 LYS D 145 ATOM 3943 N ASN E 150 63.387 18.498 −44.664 1.00 47.77 N ATOM 3944 CA ASN E 150 63.113 19.128 −43.338 1.00 46.93 C ATOM 3945 C ASN E 150 62.016 18.447 −42.513 1.00 46.19 C ATOM 3946 O ASN E 150 62.081 18.424 −41.284 1.00 46.58 O ATOM 3947 CB ASN E 150 62.737 20.595 −43.521 1.00 46.99 C ATOM 3948 N LYS E 151 61.010 17.896 −43.184 1.00 45.03 N ATOM 3949 CA LYS E 151 59.899 17.209 −42.519 1.00 43.69 C ATOM 3950 C LYS E 151 60.297 15.780 −42.130 1.00 43.11 C ATOM 3951 O LYS E 151 60.737 14.997 −42.972 1.00 42.16 O ATOM 3952 CB LYS E 151 58.666 17.186 −43.434 1.00 42.74 C ATOM 3953 N ARG E 152 60.135 15.427 −40.856 1.00 42.03 N ATOM 3954 CA ARG E 152 60.542 14.090 −40.419 1.00 40.41 C ATOM 3955 C ARG E 152 59.854 13.582 −39.156 1.00 39.14 C ATOM 3956 O ARG E 152 59.402 14.355 −38.305 1.00 38.94 O ATOM 3957 CB ARG E 152 62.056 14.073 −40.194 1.00 40.84 C ATOM 3958 CG ARG E 152 62.522 15.098 −39.163 1.00 41.74 C ATOM 3959 CD ARG E 152 64.039 15.142 −39.044 1.00 41.72 C ATOM 3960 NE ARG E 152 64.597 13.867 −38.601 1.00 41.23 N ATOM 3961 CZ ARG E 152 65.873 13.691 −38.262 1.00 41.68 C ATOM 3962 NH1 ARG E 152 66.722 14.706 −38.319 1.00 41.31 N ATOM 3963 NH2 ARG E 152 66.304 12.507 −37.851 1.00 41.80 N ATOM 3964 N ALA E 153 59.790 12.262 −39.050 1.00 37.40 N ATOM 3965 CA ALA E 153 59.188 11.604 −37.908 1.00 35.59 C ATOM 3966 C ALA E 153 59.976 11.931 −36.633 1.00 34.63 C ATOM 3967 O ALA E 153 61.091 12.444 −36.683 1.00 34.27 O ATOM 3968 CB ALA E 153 59.153 10.086 −38.147 1.00 35.29 C ATOM 3969 N PRO E 154 59.396 11.629 −35.467 1.00 33.84 N ATOM 3970 CA PRO E 154 60.045 11.892 −34.183 1.00 33.06 C ATOM 3971 C PRO E 154 61.294 11.046 −33.977 1.00 33.19 C ATOM 3972 O PRO E 154 61.378 9.921 −34.475 1.00 32.44 O ATOM 3973 CB PRO E 154 58.954 11.553 −33.185 1.00 33.37 C ATOM 3974 CG PRO E 154 58.220 10.453 −33.883 1.00 33.19 C ATOM 3975 CD PRO E 154 58.098 10.962 −35.274 1.00 32.82 C ATOM 3976 N TYR E 155 62.260 11.596 −33.247 1.00 33.51 N ATOM 3977 CA TYR E 155 63.498 10.894 −32.958 1.00 34.94 C ATOM 3978 C TYR E 155 64.120 11.421 −31.662 1.00 34.71 C ATOM 3979 O TYR E 155 63.963 12.592 −31.327 1.00 34.98 O ATOM 3980 CB TYR E 155 64.481 11.049 −34.127 1.00 36.16 C ATOM 3981 CG TYR E 155 64.952 12.469 −34.361 1.00 37.74 C ATOM 3982 CD1 TYR E 155 64.101 13.430 −34.914 1.00 38.83 C ATOM 3983 CD2 TYR E 155 66.246 12.854 −34.017 1.00 38.46 C ATOM 3984 CE1 TYR E 155 64.532 14.740 −35.117 1.00 39.50 C ATOM 3985 CE2 TYR E 155 66.685 14.156 −34.212 1.00 39.37 C ATOM 3986 CZ TYR E 155 65.826 15.093 −34.762 1.00 39.92 C ATOM 3987 OH TYR E 155 66.273 16.380 −34.954 1.00 41.10 O ATOM 3988 N TRP E 156 64.812 10.548 −30.935 1.00 34.75 N ATOM 3989 CA TRP E 156 65.469 10.923 −29.681 1.00 36.24 C ATOM 3990 C TRP E 156 66.687 11.801 −29.972 1.00 37.97 C ATOM 3991 O TRP E 156 67.530 11.419 −30.777 1.00 38.67 O ATOM 3992 CB TRP E 156 65.934 9.663 −28.944 1.00 33.60 C ATOM 3993 CG TRP E 156 64.863 8.670 −28.702 1.00 31.13 C ATOM 3994 CD1 TRP E 156 64.932 7.336 −28.928 1.00 29.72 C ATOM 3995 CD2 TRP E 156 63.554 8.925 −28.168 1.00 30.40 C ATOM 3996 NE1 TRP E 156 63.755 6.732 −28.572 1.00 29.08 N ATOM 3997 CE2 TRP E 156 62.888 7.682 −28.103 1.00 30.19 C ATOM 3998 CE3 TRP E 156 62.881 10.082 −27.737 1.00 29.65 C ATOM 3999 CZ2 TRP E 156 61.575 7.554 −27.625 1.00 29.52 C ATOM 4000 CZ3 TRP E 156 61.574 9.962 −27.261 1.00 29.43 C ATOM 4001 CH2 TRP E 156 60.935 8.703 −27.209 1.00 29.93 C ATOM 4002 N THR E 157 66.782 12.957 −29.314 1.00 40.28 N ATOM 4003 CA THR E 157 67.902 13.875 −29.521 1.00 42.16 C ATOM 4004 C THR E 157 69.039 13.675 −28.533 1.00 43.32 C ATOM 4005 O THR E 157 70.058 14.349 −28.620 1.00 44.81 O ATOM 4006 CB THR E 157 67.461 15.348 −29.435 1.00 42.71 C ATOM 4007 OG1 THR E 157 66.867 15.605 −28.154 1.00 43.09 O ATOM 4008 CG2 THR E 157 66.473 15.672 −30.544 1.00 43.30 C ATOM 4009 N ASN E 158 68.872 12.757 −27.590 1.00 44.89 N ATOM 4010 CA ASN E 158 69.924 12.487 −26.612 1.00 46.03 C ATOM 4011 C ASN E 158 69.718 11.148 −25.926 1.00 45.86 C ATOM 4012 O ASN E 158 69.194 11.090 −24.817 1.00 45.97 O ATOM 4013 CB ASN E 158 69.979 13.589 −25.551 1.00 47.13 C ATOM 4014 CG ASN E 158 71.164 13.429 −24.610 1.00 48.57 C ATOM 4015 OD1 ASN E 158 71.263 12.448 −23.865 1.00 48.99 O ATOM 4016 ND2 ASN E 158 72.074 14.394 −24.644 1.00 48.78 N ATOM 4017 N THR E 159 70.146 10.075 −26.586 1.00 45.97 N ATOM 4018 CA THR E 159 69.996 8.730 −26.040 1.00 46.61 C ATOM 4019 C THR E 159 70.850 8.478 −24.806 1.00 47.15 C ATOM 4020 O THR E 159 70.583 7.542 −24.051 1.00 47.10 O ATOM 4021 CB THR E 159 70.339 7.634 −27.087 1.00 47.22 C ATOM 4022 OG1 THR E 159 71.646 7.868 −27.626 1.00 48.06 O ATOM 4023 CG2 THR E 159 69.318 7.629 −28.221 1.00 47.67 C ATOM 4024 N GLU E 160 71.877 9.303 −24.612 1.00 47.12 N ATOM 4025 CA GLU E 160 72.773 9.159 −23.469 1.00 47.32 C ATOM 4026 C GLU E 160 71.976 9.235 −22.169 1.00 47.16 C ATOM 4027 O GLU E 160 72.101 8.379 −21.299 1.00 47.06 O ATOM 4028 CB GLU E 160 73.837 10.265 −23.494 1.00 47.70 C ATOM 4029 N LYS E 161 71.144 10.265 −22.065 1.00 46.66 N ATOM 4030 CA LYS E 161 70.311 10.491 −20.892 1.00 46.05 C ATOM 4031 C LYS E 161 69.145 9.506 −20.757 1.00 45.11 C ATOM 4032 O LYS E 161 68.353 9.626 −19.822 1.00 45.34 O ATOM 4033 CB LYS E 161 69.756 11.923 −20.926 1.00 46.21 C ATOM 4034 N MET E 162 69.038 8.548 −21.678 1.00 44.22 N ATOM 4035 CA MET E 162 67.946 7.560 −21.659 1.00 43.37 C ATOM 4036 C MET E 162 68.428 6.130 −21.400 1.00 43.15 C ATOM 4037 O MET E 162 67.617 5.214 −21.232 1.00 42.92 O ATOM 4038 CB MET E 162 67.181 7.569 −22.999 1.00 42.59 C ATOM 4039 CG MET E 162 66.441 8.858 −23.359 1.00 42.12 C ATOM 4040 SD MET E 162 65.737 8.805 −25.069 1.00 43.12 S ATOM 4041 CE MET E 162 64.428 7.582 −24.869 1.00 41.06 C ATOM 4042 N GLU E 163 69.742 5.937 −21.367 1.00 42.76 N ATOM 4043 CA GLU E 163 70.316 4.605 −21.163 1.00 42.46 C ATOM 4044 C GLU E 163 69.991 3.951 −19.814 1.00 41.50 C ATOM 4045 O GLU E 163 69.837 2.728 −19.727 1.00 41.96 O ATOM 4046 CB GLU E 163 71.837 4.667 −21.363 1.00 42.74 C ATOM 4047 N LYS E 164 69.898 4.760 −18.765 1.00 39.99 N ATOM 4048 CA LYS E 164 69.585 4.270 −17.422 1.00 38.16 C ATOM 4049 C LYS E 164 68.083 3.937 −17.381 1.00 37.14 C ATOM 4050 O LYS E 164 67.256 4.827 −17.185 1.00 37.33 O ATOM 4051 CB LYS E 164 69.945 5.369 −16.410 1.00 36.48 C ATOM 4052 CG LYS E 164 69.679 5.058 −14.947 1.00 36.37 C ATOM 4053 CD LYS E 164 70.119 6.229 −14.072 1.00 37.37 C ATOM 4054 CE LYS E 164 69.633 6.106 −12.638 1.00 38.14 C ATOM 4055 NZ LYS E 164 69.990 7.292 −11.803 1.00 38.47 N ATOM 4056 N ARG E 165 67.739 2.664 −17.580 1.00 36.23 N ATOM 4057 CA ARG E 165 66.335 2.235 −17.596 1.00 35.70 C ATOM 4058 C ARG E 165 65.707 2.067 −16.224 1.00 34.16 C ATOM 4059 O ARG E 165 64.562 2.469 −16.011 1.00 32.97 O ATOM 4060 CB ARG E 165 66.172 0.936 −18.392 1.00 36.74 C ATOM 4061 CG ARG E 165 66.260 1.141 −19.899 1.00 39.91 C ATOM 4062 CD ARG E 165 66.310 −0.183 −20.631 1.00 41.98 C ATOM 4063 NE ARG E 165 66.734 −0.020 −22.017 1.00 44.67 N ATOM 4064 CZ ARG E 165 65.920 0.2482 −3.035 1.00 46.24 C ATOM 4065 NH1 ARG E 165 64.607 0.3822 −2.840 1.00 46.06 N ATOM 4066 NH2 ARG E 165 66.428 0.3922 −4.253 1.00 46.74 N ATOM 4067 N LEU E 166 66.456 1.466 −15.305 1.00 33.11 N ATOM 4068 CA LEU E 166 65.995 1.251 −13.938 1.00 32.45 C ATOM 4069 C LEU E 166 66.407 2.422 −13.053 1.00 32.78 C ATOM 4070 O LEU E 166 67.600 2.701 −12.911 1.00 32.57 O ATOM 4071 CB LEU E 166 66.603 −0.034 −13.363 1.00 30.72 C ATOM 4072 CG LEU E 166 66.452 −0.238 −11.842 1.00 31.40 C ATOM 4073 CD1 LEU E 166 64.982 −0.336 −11.443 1.00 29.68 C ATOM 4074 CD2 LEU E 166 67.179 −1.497 −11.430 1.00 31.08 C ATOM 4075 N HIS E 167 65.421 3.102 −12.472 1.00 32.56 N ATOM 4076 CA HIS E 167 65.657 4.223 −11.563 1.00 32.60 C ATOM 4077 C HIS E 167 65.250 3.782 −10.170 1.00 32.67 C ATOM 4078 O HIS E 167 64.053 3.731 −9.863 1.00 32.64 O ATOM 4079 CB HIS E 167 64.799 5.438 −11.927 1.00 33.90 C ATOM 4080 CG HIS E 167 65.393 6.322 −12.975 1.00 35.97 C ATOM 4081 ND1 HIS E 167 65.717 5.871 −14.237 1.00 37.14 N ATOM 4082 CD2 HIS E 167 65.711 7.638 −12.950 1.00 35.95 C ATOM 4083 CE1 HIS E 167 66.212 6.872 −14.944 1.00 36.75 C ATOM 4084 NE2 HIS E 167 66.217 7.954 −14.185 1.00 36.35 N ATOM 4085 N ALA E 168 66.234 3.456 −9.337 1.00 31.87 N ATOM 4086 CA ALA E 168 65.982 3.044 −7.960 1.00 31.90 C ATOM 4087 C ALA E 168 66.360 4.250 −7.119 1.00 31.80 C ATOM 4088 O ALA E 168 67.505 4.698 −7.162 1.00 31.50 O ATOM 4089 CB ALA E 168 66.863 1.855 −7.586 1.00 32.12 C ATOM 4090 N VAL E 169 65.413 4.770 −6.351 1.00 31.54 N ATOM 4091 CA VAL E 169 65.676 5.942 −5.531 1.00 32.05 C ATOM 4092 C VAL E 169 65.116 5.822 −4.122 1.00 31.84 C ATOM 4093 O VAL E 169 64.165 5.085 −3.876 1.00 31.58 O ATOM 4094 CB VAL E 169 65.058 7.209 −6.158 1.00 33.04 C ATOM 4095 CG1 VAL E 169 65.520 7.359 −7.606 1.00 33.81 C ATOM 4096 CG2 VAL E 169 63.536 7.135 −6.077 1.00 32.98 C ATOM 4097 N PRO E 170 65.705 6.564 −3.177 1.00 31.48 N ATOM 4098 CA PRO E 170 65.226 6.517 −1.796 1.00 31.72 C ATOM 4099 C PRO E 170 63.924 7.295 −1.658 1.00 32.29 C ATOM 4100 O PRO E 170 63.715 8.310 −2.334 1.00 31.99 O ATOM 4101 CB PRO E 170 66.380 7.135 −1.015 1.00 31.55 C ATOM 4102 CG PRO E 170 66.954 8.136 −2.001 1.00 31.18 C ATOM 4103 CD PRO E 170 66.904 7.408 −3.314 1.00 30.68 C ATOM 4104 N ALA E 171 63.038 6.804 −0.795 1.00 33.07 N ATOM 4105 CA ALA E 171 61.751 7.455 −0.557 1.00 33.03 C ATOM 4106 C ALA E 171 61.931 8.925 −0.162 1.00 33.54 C ATOM 4107 O ALA E 171 62.927 9.295 0.474 1.00 32.77 O ATOM 4108 CB ALA E 171 60.988 6.718 0.534 1.00 32.87 C ATOM 4109 N ALA E 172 60.964 9.754 −0.560 1.00 33.21 N ATOM 4110 CA ALA E 172 60.947 11.185 −0.266 1.00 33.03 C ATOM 4111 C ALA E 172 61.740 12.058 −1.238 1.00 33.63 C ATOM 4112 O ALA E 172 61.736 13.287 −1.124 1.00 34.46 O ATOM 4113 CB ALA E 172 61.400 11.443 1.187 1.00 34.01 C ATOM 4114 N ASN E 173 62.415 11.435 −2.196 1.00 33.56 N ATOM 4115 CA ASN E 173 63.166 12.197 −3.190 1.00 32.94 C ATOM 4116 C ASN E 173 62.284 12.535 −4.384 1.00 31.99 C ATOM 4117 O ASN E 173 61.169 12.036 −4.508 1.00 31.57 O ATOM 4118 CB ASN E 173 64.391 11.405 −3.662 1.00 33.95 C ATOM 4119 CG ASN E 173 65.628 11.723 −2.845 1.00 35.18 C ATOM 4120 OD1 ASN E 173 65.561 11.861 −1.625 1.00 34.81 O ATOM 4121 ND2 ASN E 173 66.766 11.840 −3.518 1.00 36.97 N ATOM 4122 N THR E 174 62.789 13.401 −5.249 1.00 31.28 N ATOM 4123 CA THR E 174 62.086 13.781 −6.462 1.00 30.65 C ATOM 4124 C THR E 174 62.686 12.961 −7.598 1.00 30.83 C ATOM 4125 O THR E 174 63.902 12.760 −7.639 1.00 31.45 O ATOM 4126 CB THR E 174 62.282 15.275 −6.779 1.00 29.35 C ATOM 4127 OG1 THR E 174 61.465 16.058 −5.904 1.00 30.67 O ATOM 4128 CG2 THR E 174 61.914 15.568 −8.217 1.00 29.28 C ATOM 4129 N VAL E 175 61.845 12.473 −8.507 1.00 30.88 N ATOM 4130 CA VAL E 175 62.348 11.712 −9.638 1.00 30.80 C ATOM 4131 C VAL E 175 61.974 12.419 −10.937 1.00 30.86 C ATOM 4132 O VAL E 175 60.902 13.025 −11.054 1.00 31.51 O ATOM 4133 CB VAL E 175 61.821 10.248 −9.627 1.00 31.74 C ATOM 4134 CG1 VAL E 175 60.319 10.233 −9.781 1.00 32.32 C ATOM 4135 CG2 VAL E 175 62.495 9.445 −10.738 1.00 31.70 C ATOM 4136 N LYS E 176 62.878 12.374 −11.905 1.00 30.11 N ATOM 4137 CA LYS E 176 62.633 13.014 −13.186 1.00 30.97 C ATOM 4138 C LYS E 176 63.008 12.107 −14.357 1.00 30.93 C ATOM 4139 O LYS E 176 64.146 11.636 −14.454 1.00 30.54 O ATOM 4140 CB LYS A 176 63.421 14.331 −13.269 1.00 32.52 C ATOM 4141 CG LYS A 176 63.251 15.108 −14.578 1.00 34.91 C ATOM 4142 CD LYS A 176 63.964 16.489 −14.539 1.00 36.19 C ATOM 4143 CE LYS A 176 63.966 17.158 −15.924 1.00 38.06 C ATOM 4144 NZ LYS E 176 64.564 18.542 −15.996 1.00 38.65 N ATOM 4145 N PHE E 177 62.043 11.847 −15.233 1.00 30.34 N ATOM 4146 CA PHE E 177 62.293 11.022 −16.405 1.00 29.82 C ATOM 4147 C PHE E 177 62.299 11.931 −17.615 1.00 29.71 C ATOM 4148 O PHE E 177 61.473 12.834 −17.713 1.00 30.29 O ATOM 4149 CB PHE E 177 61.207 9.965 −16.557 1.00 29.12 C ATOM 4150 CG PHE E 177 61.217 8.934 −15.469 1.00 29.66 C ATOM 4151 CD1 PHE E 177 62.347 8.152 −15.249 1.00 29.65 C ATOM 4152 CD2 PHE E 177 60.095 8.725 −14.680 1.00 29.44 C ATOM 4153 CE1 PHE E 177 62.359 7.179 −14.266 1.00 29.37 C ATOM 4154 CE2 PHE E 177 60.095 7.752 −13.690 1.00 30.37 C ATOM 4155 CZ PHE E 177 61.235 6.973 −13.484 1.00 29.78 C ATOM 4156 N ARG E 178 63.232 11.700 −18.531 1.00 29.90 N ATOM 4157 CA ARG E 178 63.325 12.518 −19.737 1.00 30.18 C ATOM 4158 C ARG E 178 63.414 11.697 −21.025 1.00 30.49 C ATOM 4159 O ARG E 178 63.956 10.585 −21.040 1.00 28.47 O ATOM 4160 CB ARG E 178 64.544 13.443 −19.659 1.00 31.50 C ATOM 4161 CG ARG E 178 64.607 14.318 −18.410 1.00 35.87 C ATOM 4162 CD ARG E 178 65.695 15.381 −18.567 1.00 37.95 C ATOM 4163 NE ARG E 178 65.438 16.174 −19.766 1.00 41.27 N ATOM 4164 CZ ARG E 178 66.350 16.890 −20.415 1.00 42.38 C ATOM 4165 NH1 ARG E 178 67.609 16.929 −19.983 1.00 43.71 N ATOM 4166 NH2 ARG E 178 66.007 17.545 −21.519 1.00 42.32 N ATOM 4167 N CYS E 179 62.870 12.263 −22.102 1.00 30.09 N ATOM 4168 CA CYS E 179 62.900 11.645 −23.415 1.00 31.40 C ATOM 4169 C CYS E 179 63.079 12.753 −24.455 1.00 31.54 C ATOM 4170 O CYS E 179 62.190 13.026 −25.260 1.00 30.99 O ATOM 4171 CB CYS E 179 61.608 10.857 −23.646 1.00 32.04 C ATOM 4172 SG CYS E 179 61.472 9.459 −22.503 1.00 33.20 S ATOM 4173 N PRO E 180 64.253 13.412 −24.436 1.00 32.00 N ATOM 4174 CA PRO E 180 64.578 14.504 −25.365 1.00 32.32 C ATOM 4175 C PRO E 180 64.274 14.080 −26.789 1.00 32.64 C ATOM 4176 O PRO E 180 64.824 13.092 −27.272 1.00 32.30 O ATOM 4177 CB PRO E 180 66.076 14.713 −25.137 1.00 31.72 C ATOM 4178 CG PRO E 180 66.238 14.376 −23.684 1.00 32.39 C ATOM 4179 CD PRO E 180 65.394 13.113 −23.550 1.00 31.38 C ATOM 4180 N ALA E 181 63.405 14.821 −27.466 1.00 33.54 N ATOM 4181 CA ALA E 181 63.037 14.459 −28.823 1.00 34.81 C ATOM 4182 C ALA E 181 63.051 15.604 −29.836 1.00 36.17 C ATOM 4183 O ALA E 181 62.969 16.777 −29.476 1.00 35.97 O ATOM 4184 CB ALA E 181 61.662 13.803 −28.806 1.00 33.94 C ATOM 4185 N GLY E 182 63.149 15.228 −31.109 1.00 37.42 N ATOM 4186 CA GLY E 182 63.141 16.184 −32.203 1.00 38.05 C ATOM 4187 C GLY E 182 62.107 15.728 −33.215 1.00 38.82 C ATOM 4188 O GLY E 182 61.548 14.634 −33.076 1.00 38.84 O ATOM 4189 N GLY E 183 61.850 16.548 −34.232 1.00 39.61 N ATOM 4190 CA GLY E 183 60.873 16.194 −35.248 1.00 39.37 C ATOM 4191 C GLY E 183 60.209 17.403 −35.886 1.00 40.34 C ATOM 4192 O GLY E 183 60.126 18.472 −35.276 1.00 39.97 O ATOM 4193 N ASN E 184 59.735 17.239 −37.118 1.00 40.45 N ATOM 4194 CA ASN E 184 59.068 18.322 −37.835 1.00 41.60 C ATOM 4195 C ASN E 184 57.875 17.793 −38.627 1.00 41.71 C ATOM 4196 O ASN E 184 58.038 17.046 −39.586 1.00 42.15 O ATOM 4197 CB ASN E 184 60.054 19.020 −38.781 1.00 41.57 C ATOM 4198 N PRO E 185 56.657 18.206 −38.258 1.00 42.39 N ATOM 4199 CA PRO E 185 56.348 19.132 −37.163 1.00 42.99 C ATOM 4200 C PRO E 185 56.699 18.635 −35.758 1.00 44.39 C ATOM 4201 O PRO E 185 56.941 17.441 −35.541 1.00 44.92 O ATOM 4202 CB PRO E 185 54.850 19.384 −37.343 1.00 42.48 C ATOM 4203 CG PRO E 185 54.355 18.108 −37.914 1.00 42.87 C ATOM 4204 CD PRO E 185 55.424 17.771 −38.938 1.00 42.74 C ATOM 4205 N MET E 186 56.733 19.572 −34.810 1.00 44.67 N ATOM 4206 CA MET E 186 57.044 19.276 −33.412 1.00 44.59 C ATOM 4207 C MET E 186 56.137 18.167 −32.883 1.00 43.62 C ATOM 4208 O MET E 186 54.917 18.304 −32.854 1.00 43.45 O ATOM 4209 CB MET E 186 56.861 20.533 −32.551 1.00 46.17 C ATOM 4210 CG MET E 186 57.269 20.364 −31.089 1.00 47.14 C ATOM 4211 SD MET E 186 59.028 19.948 −30.944 1.00 50.88 S ATOM 4212 CE MET E 186 59.755 21.534 −30.489 1.00 49.96 C ATOM 4213 N PRO E 187 56.731 17.052 −32.444 1.00 42.84 N ATOM 4214 CA PRO E 187 55.937 15.936 −31.925 1.00 42.11 C ATOM 4215 C PRO E 187 55.327 16.199 −30.551 1.00 41.39 C ATOM 4216 O PRO E 187 55.850 16.997 −29.771 1.00 40.66 O ATOM 4217 CB PRO E 187 56.945 14.789 −31.897 1.00 42.56 C ATOM 4218 CG PRO E 187 58.229 15.478 −31.584 1.00 42.73 C ATOM 4219 CD PRO E 187 58.172 16.736 −32.434 1.00 42.58 C ATOM 4220 N THR E 188 54.213 15.533 −30.261 1.00 40.80 N ATOM 4221 CA THR E 188 53.570 15.694 −28.967 1.00 40.77 C ATOM 4222 C THR E 188 54.119 14.622 −28.039 1.00 40.73 C ATOM 4223 O THR E 188 54.756 13.660 −28.476 1.00 40.10 O ATOM 4224 CB THR E 188 52.042 15.522 −29.027 1.00 40.84 C ATOM 4225 OG1 THR E 188 51.728 14.136 −29.201 1.00 41.02 O ATOM 4226 CG2 THR E 188 51.453 16.330 −30.169 1.00 40.27 C ATOM 4227 N MET E 189 53.867 14.791 −26.751 1.00 40.54 N ATOM 4228 CA MET E 189 54.345 13.841 −25.764 1.00 41.01 C ATOM 4229 C MET E 189 53.263 13.438 −24.781 1.00 39.45 C ATOM 4230 O MET E 189 52.493 14.278 −24.318 1.00 38.97 O ATOM 4231 CB MET E 189 55.523 14.432 −24.982 1.00 42.49 C ATOM 4232 CG MET E 189 55.951 13.576 −23.791 1.00 45.02 C ATOM 4233 SD MET E 189 57.378 14.250 −22.910 1.00 48.98 S ATOM 4234 CE MET E 189 58.674 13.084 −23.501 1.00 48.53 C ATOM 4235 N ARG E 190 53.222 12.146 −24.466 1.00 37.91 N ATOM 4236 CA ARG E 190 52.264 11.603 −23.509 1.00 36.69 C ATOM 4237 C ARG E 190 53.002 10.599 −22.625 1.00 34.83 C ATOM 4238 O ARG E 190 53.896 9.891 −23.103 1.00 33.14 O ATOM 4239 CB ARG E 190 51.122 10.875 −24.220 1.00 38.19 C ATOM 4240 CG ARG E 190 50.527 11.607 −25.410 1.00 41.65 C ATOM 4241 CD ARG E 190 49.163 11.021 −25.794 1.00 43.46 C ATOM 4242 NE ARG E 190 49.161 9.560 −25.891 1.00 44.29 N ATOM 4243 CZ ARG E 190 49.719 8.866 −26.878 1.00 45.19 C ATOM 4244 NH1 ARG E 190 50.338 9.495 −27.873 1.00 46.13 N ATOM 4245 NH2 ARG E 190 49.653 7.540 −26.874 1.00 44.60 N ATOM 4246 N TRP E 191 52.639 10.539 −21.343 1.00 31.83 N ATOM 4247 CA TRP E 191 53.269 9.586 −20.431 1.00 31.00 C ATOM 4248 C TRP E 191 52.268 8.540 −19.908 1.00 30.76 C ATOM 4249 O TRP E 191 51.138 8.867 −19.536 1.00 30.52 O ATOM 4250 CB TRP E 191 53.937 10.301 −19.246 1.00 29.62 C ATOM 4251 CG TRP E 191 55.187 11.072 −19.603 1.00 28.95 C ATOM 4252 CD1 TRP E 191 55.259 12.337 −20.128 1.00 29.00 C ATOM 4253 CD2 TRP E 191 56.540 10.612 −19.487 1.00 28.32 C ATOM 4254 NE1 TRP E 191 56.572 12.688 −20.344 1.00 28.22 N ATOM 4255 CE2 TRP E 191 57.378 11.649 −19.960 1.00 28.76 C ATOM 4256 CE3 TRP E 191 57.125 9.423 −19.030 1.00 29.22 C ATOM 4257 CZ2 TRP E 191 58.775 11.533 −19.985 1.00 29.04 C ATOM 4258 CZ3 TRP E 191 58.520 9.306 −19.060 1.00 30.17 C ATOM 4259 CH2 TRP E 191 59.326 10.359 −19.534 1.00 29.04 C ATOM 4260 N LEU E 192 52.687 7.280 −19.905 1.00 29.28 N ATOM 4261 CA LEU E 192 51.840 6.197 −19.421 1.00 29.58 C ATOM 4262 C LEU E 192 52.428 5.583 −18.143 1.00 29.57 C ATOM 4263 O LEU E 192 53.645 5.571 −17.958 1.00 30.74 O ATOM 4264 CB LEU E 192 51.721 5.084 −20.477 1.00 28.80 C ATOM 4265 CG LEU E 192 51.382 5.339 −21.958 1.00 30.27 C ATOM 4266 CD1 LEU E 192 51.448 4.015 −22.708 1.00 31.01 C ATOM 4267 CD2 LEU E 192 49.998 5.950 −22.115 1.00 29.80 C ATOM 4268 N LYS E 193 51.559 5.097 −17.260 1.00 28.96 N ATOM 4269 CA LYS E 193 51.986 4.412 −16.051 1.00 28.34 C ATOM 4270 C LYS E 193 51.466 2.983 −16.225 1.00 29.18 C ATOM 4271 O LYS E 193 50.257 2.763 −16.362 1.00 27.91 O ATOM 4272 CB LYS E 193 51.371 5.023 −14.794 1.00 27.85 C ATOM 4273 CG LYS E 193 51.762 4.267 −13.506 1.00 28.13 C ATOM 4274 CD LYS E 193 51.139 4.882 −12.254 1.00 29.87 C ATOM 4275 CE LYS E 193 51.541 4.112 −10.999 1.00 30.30 C ATOM 4276 NZ LYS E 193 50.798 4.559 −9.789 1.00 28.18 N ATOM 4277 N ASN E 194 52.376 2.013 −16.230 1.00 28.65 N ATOM 4278 CA ASN E 194 51.990 0.620 −16.417 1.00 29.49 C ATOM 4279 C ASN E 194 51.132 0.450 −17.682 1.00 30.66 C ATOM 4280 O ASN E 194 50.069 −0.168 −17.642 1.00 30.92 O ATOM 4281 CB ASN E 194 51.215 0.099 −15.195 1.00 27.12 C ATOM 4282 CG ASN E 194 52.064 0.051 −13.934 1.00 27.31 C ATOM 4283 OD1 ASN E 194 53.271 −0.233 −13.987 1.00 25.63 O ATOM 4284 ND2 ASN E 194 51.433 0.310 −12.783 1.00 24.35 N ATOM 4285 N GLY E 195 51.595 1.022 −18.792 1.00 31.66 N ATOM 4286 CA GLY E 195 50.886 0.919 −20.060 1.00 32.64 C ATOM 4287 C GLY E 195 49.528 1.601 −20.206 1.00 33.77 C ATOM 4288 O GLY E 195 48.838 1.357 −21.191 1.00 33.63 O ATOM 4289 N LYS E 196 49.137 2.440 −19.247 1.00 34.77 N ATOM 4290 CA LYS E 196 47.845 3.132 −19.314 1.00 36.07 C ATOM 4291 C LYS E 196 48.029 4.615 −19.042 1.00 35.87 C ATOM 4292 O LYS E 196 49.003 5.011 −18.405 1.00 35.40 O ATOM 4293 CB LYS E 196 46.871 2.599 −18.258 1.00 37.29 C ATOM 4294 CG LYS E 196 47.072 1.156 −17.820 1.00 40.01 C ATOM 4295 CD LYS E 196 46.543 1.000 −16.393 1.00 42.51 C ATOM 4296 CE LYS E 196 47.036 −0.269 −15.718 1.00 43.43 C ATOM 4297 NZ LYS E 196 46.738 −0.231 −14.254 1.00 44.06 N ATOM 4298 N GLU E 197 47.082 5.429 −19.504 1.00 36.09 N ATOM 4299 CA GLU E 197 47.142 6.867 −19.275 1.00 35.90 C ATOM 4300 C GLU E 197 47.445 7.136 −17.802 1.00 34.76 C ATOM 4301 O GLU E 197 46.858 6.521 −16.915 1.00 34.16 O ATOM 4302 CB GLU E 197 45.815 7.533 −19.672 1.00 37.72 C ATOM 4303 CG GLU E 197 45.694 9.008 −19.247 1.00 39.18 C ATOM 4304 CD GLU E 197 44.430 9.698 −19.778 1.00 41.13 C ATOM 4305 OE1 GLU E 197 43.397 9.016 −19.985 1.00 40.19 O ATOM 4306 OE2 GLU E 197 44.470 10.933 −19.969 1.00 40.93 O ATOM 4307 N PHE E 198 48.384 8.046 −17.564 1.00 34.33 N ATOM 4308 CA PHE E 198 48.805 8.427 −16.223 1.00 33.43 C ATOM 4309 C PHE E 198 48.051 9.719 −15.917 1.00 34.28 C ATOM 4310 O PHE E 198 48.245 10.725 −16.596 1.00 33.79 O ATOM 4311 CB PHE E 198 50.321 8.669 −16.229 1.00 31.88 C ATOM 4312 CG PHE E 198 50.939 8.873 −14.861 1.00 29.49 C ATOM 4313 CD1 PHE E 198 52.201 9.455 −14.750 1.00 28.38 C ATOM 4314 CD2 PHE E 198 50.293 8.461 −13.702 1.00 28.64 C ATOM 4315 CE1 PHE E 198 52.816 9.625 −13.494 1.00 27.94 C ATOM 4316 CE2 PHE E 198 50.901 8.625 −12.442 1.00 29.18 C ATOM 4317 CZ PHE E 198 52.166 9.209 −12.345 1.00 26.63 C ATOM 4318 N LYS E 199 47.190 9.680 −14.903 1.00 35.47 N ATOM 4319 CA LYS E 199 46.383 10.841 −14.515 1.00 36.46 C ATOM 4320 C LYS E 199 46.855 11.457 −13.209 1.00 36.29 C ATOM 4321 O LYS E 199 47.434 10.772 −12.368 1.00 35.86 O ATOM 4322 CB LYS E 199 44.920 10.436 −14.345 1.00 37.45 C ATOM 4323 CG LYS E 199 44.182 10.086 −15.625 1.00 39.26 C ATOM 4324 CD LYS E 199 42.923 9.300 −15.288 1.00 40.34 C ATOM 4325 CE LYS E 199 41.879 9.432 −16.383 1.00 42.06 C ATOM 4326 NZ LYS E 199 42.480 9.246 −17.726 1.00 42.43 N ATOM 4327 N GLN E 200 46.572 12.746 −13.035 1.00 35.97 N ATOM 4328 CA GLN E 200 46.957 13.464 −11.830 1.00 36.14 C ATOM 4329 C GLN E 200 46.466 12.783 −10.555 1.00 36.13 C ATOM 4330 O GLN E 200 47.177 12.746 −9.558 1.00 36.15 O ATOM 4331 CB GLN E 200 46.428 14.905 −11.881 1.00 35.07 C ATOM 4332 CG GLN E 200 47.097 15.794 −12.922 1.00 32.75 C ATOM 4333 CD GLN E 200 48.565 16.049 −12.629 1.00 31.75 C ATOM 4334 OE1 GLN E 200 48.980 16.095 −11.472 1.00 31.98 O ATOM 4335 NE2 GLN E 200 49.352 16.238 −13.677 1.00 31.84 N ATOM 4336 N GLU E 201 45.260 12.228 −10.590 1.00 36.20 N ATOM 4337 CA GLU E 201 44.697 11.579 −9.410 1.00 36.53 C ATOM 4338 C GLU E 201 45.307 10.212 −9.105 1.00 35.82 C ATOM 4339 O GLU E 201 44.946 9.582 −8.113 1.00 34.99 O ATOM 4340 CB GLU E 201 43.183 11.421 −9.569 1.00 37.47 C ATOM 4341 CG GLU E 201 42.799 10.440 −10.651 1.00 40.87 C ATOM 4342 CD GLU E 201 42.124 11.104 −11.834 1.00 43.50 C ATOM 4343 OE1 GLU E 201 42.719 12.037 −12.439 1.00 43.56 O ATOM 4344 OE2 GLU E 201 40.990 10.681 −12.154 1.00 44.02 O ATOM 4345 N HIS E 202 46.216 9.746 −9.957 1.00 35.29 N ATOM 4346 CA HIS E 202 46.847 8.444 −9.740 1.00 34.98 C ATOM 4347 C HIS E 202 47.852 8.397 −8.572 1.00 34.41 C ATOM 4348 O HIS E 202 48.291 7.313 −8.187 1.00 35.13 O ATOM 4349 CB HIS E 202 47.514 7.940 −11.029 1.00 34.01 C ATOM 4350 CG HIS E 202 46.547 7.437 −12.059 1.00 35.20 C ATOM 4351 ND1 HIS E 202 45.353 6.825 −11.729 1.00 35.20 N ATOM 4352 CD2 HIS E 202 46.611 7.424 −13.413 1.00 34.39 C ATOM 4353 CE1 HIS E 202 44.725 6.462 −12.833 1.00 33.57 C ATOM 4354 NE2 HIS E 202 45.468 6.813 −13.869 1.00 34.45 N ATOM 4355 N ARG E 203 48.216 9.556 −8.018 1.00 33.22 N ATOM 4356 CA ARG E 203 49.130 9.613 −6.867 1.00 32.51 C ATOM 4357 C ARG E 203 48.912 10.907 −6.080 1.00 32.39 C ATOM 4358 O ARG E 203 48.459 11.906 −6.635 1.00 31.51 O ATOM 4359 CB ARG E 203 50.605 9.523 −7.309 1.00 30.32 C ATOM 4360 CG ARG E 203 51.174 10.814 −7.895 1.00 29.22 C ATOM 4361 CD ARG E 203 52.563 10.591 −8.502 1.00 29.55 C ATOM 4362 NE ARG E 203 53.557 10.178 −7.508 1.00 28.00 N ATOM 4363 CZ ARG E 203 54.259 11.013 −6.749 1.00 26.43 C ATOM 4364 NH1 ARG E 203 54.093 12.323 −6.859 1.00 25.80 N ATOM 4365 NH2 ARG E 203 55.117 10.536 −5.860 1.00 27.50 N ATOM 4366 N ILE E 204 49.215 10.880 −4.787 1.00 32.99 N ATOM 4367 CA ILE E 204 49.061 12.069 −3.964 1.00 34.24 C ATOM 4368 C ILE E 204 49.946 13.162 −4.559 1.00 34.70 C ATOM 4369 O ILE E 204 51.125 12.928 −4.851 1.00 34.35 O ATOM 4370 CB ILE E 204 49.496 11.810 −2.503 1.00 35.02 C ATOM 4371 CG1 ILE E 204 48.705 10.633 −1.918 1.00 35.18 C ATOM 4372 CG2 ILE E 204 49.296 13.083 −1.664 1.00 36.10 C ATOM 4373 CD1 ILE E 204 47.206 10.812 −1.957 1.00 34.74 C ATOM 4374 N GLY E 205 49.364 14.341 −4.769 1.00 34.34 N ATOM 4375 CA GLY E 205 50.115 15.454 −5.327 1.00 34.71 C ATOM 4376 C GLY E 205 50.338 15.406 −6.832 1.00 34.80 C ATOM 4377 O GLY E 205 50.963 16.308 −7.397 1.00 35.12 O ATOM 4378 N GLY E 206 49.840 14.362 −7.490 1.00 33.63 N ATOM 4379 CA GLY E 206 50.007 14.255 −8.932 1.00 33.94 C ATOM 4380 C GLY E 206 51.436 14.357 −9.462 1.00 33.65 C ATOM 4381 O GLY E 206 52.390 13.927 −8.815 1.00 32.95 O ATOM 4382 N TYR E 207 51.586 14.924 −10.651 1.00 33.53 N ATOM 4383 CA TYR E 207 52.904 15.080 −11.239 1.00 34.03 C ATOM 4384 C TYR E 207 52.992 16.344 −12.079 1.00 34.49 C ATOM 4385 O TYR E 207 51.989 17.036 −12.283 1.00 34.71 O ATOM 4386 CB TYR E 207 53.257 13.860 −12.105 1.00 34.68 C ATOM 4387 CG TYR E 207 52.320 13.631 −13.271 1.00 34.71 C ATOM 4388 CD1 TYR E 207 51.186 12.827 −13.133 1.00 34.16 C ATOM 4389 CD2 TYR E 207 52.557 14.237 −14.508 1.00 34.98 C ATOM 4390 CE1 TYR E 207 50.304 12.630 −14.201 1.00 35.89 C ATOM 4391 CE2 TYR E 207 51.673 14.049 −15.592 1.00 35.73 C ATOM 4392 CZ TYR E 207 50.551 13.248 −15.424 1.00 35.64 C ATOM 4393 OH TYR E 207 49.660 13.090 −16.458 1.00 36.29 O ATOM 4394 N LYS E 208 54.196 16.637 −12.566 1.00 34.28 N ATOM 4395 CA LYS E 208 54.440 17.814 −13.391 1.00 35.05 C ATOM 4396 C LYS E 208 55.157 17.431 −14.677 1.00 37.11 C ATOM 4397 O LYS E 208 55.993 16.526 −14.690 1.00 36.91 O ATOM 4398 CB LYS E 208 55.298 18.837 −12.635 1.00 34.30 C ATOM 4399 CG LYS E 208 54.680 19.377 −11.362 1.00 33.60 C ATOM 4400 CD LYS E 208 55.696 20.177 −10.562 1.00 32.63 C ATOM 4401 CE LYS E 208 55.100 20.639 −9.241 1.00 32.80 C ATOM 4402 NZ LYS E 208 56.080 21.379 −8.404 1.00 32.69 N ATOM 4403 N VAL E 209 54.824 18.119 −15.761 1.00 38.97 N ATOM 4404 CA VAL E 209 55.449 17.860 −17.047 1.00 41.04 C ATOM 4405 C VAL E 209 55.932 19.162 −17.671 1.00 42.95 C ATOM 4406 O VAL E 209 55.197 20.151 −17.727 1.00 44.04 O ATOM 4407 CB VAL E 209 54.476 17.152 −18.026 1.00 40.56 C ATOM 4408 CG1 VAL E 209 55.001 17.246 −19.444 1.00 41.33 C ATOM 4409 CG2 VAL E 209 54.320 15.689 −17.637 1.00 39.57 C ATOM 4410 N ARG E 210 57.182 19.158 −18.118 1.00 44.27 N ATOM 4411 CA ARG E 210 57.776 20.323 −18.760 1.00 45.71 C ATOM 4412 C ARG E 210 58.059 19.952 −20.219 1.00 46.45 C ATOM 4413 O ARG E 210 59.105 19.382 −20.533 1.00 46.98 O ATOM 4414 CB ARG E 210 59.073 20.718 −18.047 1.00 45.37 C ATOM 4415 N ASN E 211 57.114 20.266 −21.103 1.00 47.44 N ATOM 4416 CA ASN E 211 57.246 19.959 −22.526 1.00 47.92 C ATOM 4417 C ASN E 211 58.580 20.424 −23.107 1.00 47.84 C ATOM 4418 O ASN E 211 59.194 19.721 −23.911 1.00 47.98 O ATOM 4419 CB ASN E 211 56.093 20.588 −23.313 1.00 47.89 C ATOM 4420 N GLN E 212 59.028 21.605 −22.693 1.00 47.52 N ATOM 4421 CA GLN E 212 60.295 22.159 −23.175 1.00 47.00 C ATOM 4422 C GLN E 212 61.479 21.228 −22.886 1.00 46.08 C ATOM 4423 O GLN E 212 62.469 21.233 −23.618 1.00 46.55 O ATOM 4424 CB GLN E 212 60.552 23.534 −22.540 1.00 46.95 C ATOM 4425 N HIS E 213 61.380 20.429 −21.826 1.00 44.00 N ATOM 4426 CA HIS E 213 62.457 19.503 −21.477 1.00 42.28 C ATOM 4427 C HIS E 213 62.090 18.030 −21.713 1.00 40.55 C ATOM 4428 O HIS E 213 62.875 17.141 −21.391 1.00 39.90 O ATOM 4429 CB HIS E 213 62.862 19.694 −20.010 1.00 42.11 C ATOM 4430 N TRP E 214 60.907 17.783 −22.277 1.00 38.70 N ATOM 4431 CA TRP E 214 60.435 16.417 −22.541 1.00 36.92 C ATOM 4432 C TRP E 214 60.559 15.583 −21.270 1.00 35.61 C ATOM 4433 O TRP E 214 61.058 14.456 −21.298 1.00 34.98 O ATOM 4434 CB TRP E 214 61.273 15.768 −23.653 1.00 36.91 C ATOM 4435 CG TRP E 214 61.368 16.612 −24.879 1.00 37.66 C ATOM 4436 CD1 TRP E 214 62.336 17.538 −25.172 1.00 37.83 C ATOM 4437 CD2 TRP E 214 60.411 16.683 −25.940 1.00 37.72 C ATOM 4438 NE1 TRP E 214 62.032 18.184 −26.347 1.00 37.30 N ATOM 4439 CE2 TRP E 214 60.856 17.679 −26.839 1.00 37.75 C ATOM 4440 CE3 TRP E 214 59.215 16.003 −26.219 1.00 37.31 C ATOM 4441 CZ2 TRP E 214 60.149 18.012 −27.997 1.00 37.75 C ATOM 4442 CZ3 TRP E 214 58.513 16.333 −27.370 1.00 37.71 C ATOM 4443 CH2 TRP E 214 58.982 17.329 −28.245 1.00 37.98 C ATOM 4444 N SER E 215 60.090 16.125 −20.154 1.00 33.93 N ATOM 4445 CA SER E 215 60.230 15.427 −18.885 1.00 32.72 C ATOM 4446 C SER E 215 58.961 15.219 −18.060 1.00 31.96 C ATOM 4447 O SER E 215 57.983 15.968 −18.180 1.00 31.78 O ATOM 4448 CB SER E 215 61.244 16.180 −18.034 1.00 32.88 C ATOM 4449 OG SER E 215 60.780 17.503 −17.814 1.00 32.58 O ATOM 4450 N LEU E 216 59.020 14.200 −17.206 1.00 30.06 N ATOM 4451 CA LEU E 216 57.942 13.847 −16.281 1.00 29.24 C ATOM 4452 C LEU E 216 58.569 13.946 −14.896 1.00 28.06 C ATOM 4453 O LEU E 216 59.607 13.333 −14.643 1.00 27.98 O ATOM 4454 CB LEU E 216 57.464 12.408 −16.511 1.00 28.20 C ATOM 4455 CG LEU E 216 56.584 11.871 −15.375 1.00 28.64 C ATOM 4456 CD1 LEU E 216 55.273 12.639 −15.364 1.00 28.75 C ATOM 4457 CD2 LEU E 216 56.321 10.378 −15.553 1.00 28.80 C ATOM 4458 N ILE E 217 57.940 14.700 −14.004 1.00 27.85 N ATOM 4459 CA ILE E 217 58.445 14.903 −12.648 1.00 27.94 C ATOM 4460 C ILE E 217 57.496 14.452 −11.543 1.00 28.38 C ATOM 4461 O ILE E 217 56.320 14.838 −11.532 1.00 27.95 O ATOM 4462 CB ILE E 217 58.758 16.394 −12.426 1.00 28.53 C ATOM 4463 CG1 ILE E 217 59.912 16.804 −13.343 1.00 29.98 C ATOM 4464 CG2 ILE E 217 59.082 16.671 −10.946 1.00 27.96 C ATOM 4465 CD1 ILE E 217 60.168 18.306 −13.386 1.00 31.27 C ATOM 4466 N MET E 218 58.011 13.638 −10.621 1.00 27.96 N ATOM 4467 CA MET E 218 57.233 13.159 −9.480 1.00 29.17 C ATOM 4468 C MET E 218 58.005 13.504 −8.198 1.00 29.88 C ATOM 4469 O MET E 218 59.137 13.059 −7.993 1.00 30.35 O ATOM 4470 CB MET E 218 56.993 11.645 −9.580 1.00 29.88 C ATOM 4471 CG MET E 218 56.119 11.234 −10.779 1.00 30.14 C ATOM 4472 SD MET E 218 55.773 9.449 −10.866 1.00 31.91 S ATOM 4473 CE MET E 218 57.255 8.866 −11.591 1.00 31.93 C ATOM 4474 N GLU E 219 57.388 14.315 −7.347 1.00 29.54 N ATOM 4475 CA GLU E 219 58.007 14.744 −6.097 1.00 29.59 C ATOM 4476 C GLU E 219 57.629 13.851 −4.917 1.00 29.81 C ATOM 4477 O GLU E 219 56.560 13.242 −4.915 1.00 29.98 O ATOM 4478 CB GLU E 219 57.610 16.200 −5.829 1.00 29.31 C ATOM 4479 CG GLU E 219 58.021 17.135 −6.972 1.00 29.10 C ATOM 4480 CD GLU E 219 57.169 18.384 −7.044 1.00 29.99 C ATOM 4481 OE1 GLU E 219 55.943 18.253 −6.868 1.00 28.69 O ATOM 4482 OE2 GLU E 219 57.717 19.490 −7.286 1.00 31.38 O ATOM 4483 N SER E 220 58.528 13.764 −3.935 1.00 29.65 N ATOM 4484 CA SER E 220 58.333 12.967 −2.723 1.00 30.35 C ATOM 4485 C SER E 220 57.809 11.560 −2.985 1.00 30.26 C ATOM 4486 O SER E 220 56.751 11.182 −2.480 1.00 29.71 O ATOM 4487 CB SER E 220 57.376 13.689 −1.764 1.00 31.53 C ATOM 4488 OG SER E 220 57.815 15.014 −1.511 1.00 32.75 O ATOM 4489 N VAL E 221 58.559 10.775 −3.750 1.00 29.92 N ATOM 4490 CA VAL E 221 58.142 9.416 −4.090 1.00 29.80 C ATOM 4491 C VAL E 221 57.992 8.497 −2.869 1.00 30.61 C ATOM 4492 O VAL E 221 58.656 8.680 −1.838 1.00 30.25 O ATOM 4493 CB VAL E 221 59.125 8.776 −5.120 1.00 30.18 C ATOM 4494 CG1 VAL E 221 59.311 9.715 −6.310 1.00 29.28 C ATOM 4495 CG2 VAL E 221 60.476 8.496 −4.475 1.00 29.72 C ATOM 4496 N VAL E 222 57.092 7.524 −2.994 1.00 30.94 N ATOM 4497 CA VAL E 222 56.813 6.550 −1.945 1.00 31.89 C ATOM 4498 C VAL E 222 56.772 5.170 −2.597 1.00 33.21 C ATOM 4499 O VAL E 222 56.720 5.058 −3.823 1.00 33.31 O ATOM 4500 CB VAL E 222 55.434 6.823 −1.235 1.00 32.49 C ATOM 4501 CG1 VAL E 222 55.467 8.160 −0.495 1.00 33.19 C ATOM 4502 CG2 VAL E 222 54.295 6.816 −2.257 1.00 31.82 C ATOM 4503 N PRO E 223 56.811 4.100 −1.784 1.00 34.13 N ATOM 4504 CA PRO E 223 56.779 2.725 −2.292 1.00 33.89 C ATOM 4505 C PRO E 223 55.724 2.452 −3.360 1.00 33.67 C ATOM 4506 O PRO E 223 55.995 1.758 −4.335 1.00 33.72 O ATOM 4507 CB PRO E 223 56.548 1.903 −1.023 1.00 34.43 C ATOM 4508 CG PRO E 223 57.372 2.657 −0.022 1.00 34.86 C ATOM 4509 CD PRO E 223 56.978 4.105 −0.319 1.00 34.62 C ATOM 4510 N SER E 224 54.528 3.006 −3.185 1.00 32.74 N ATOM 4511 CA SER E 224 53.448 2.789 −4.138 1.00 31.97 C ATOM 4512 C SER E 224 53.709 3.334 −5.549 1.00 31.69 C ATOM 4513 O SER E 224 53.001 2.977 −6.489 1.00 31.29 O ATOM 4514 CB SER E 224 52.144 3.381 −3.590 1.00 32.09 C ATOM 4515 OG SER E 224 52.261 4.783 −3.398 1.00 32.79 O ATOM 4516 N ASP E 225 54.712 4.198 −5.704 1.00 31.22 N ATOM 4517 CA ASP E 225 55.037 4.758 −7.023 1.00 30.43 C ATOM 4518 C ASP E 225 55.774 3.757 −7.928 1.00 30.38 C ATOM 4519 O ASP E 225 55.958 4.002 −9.125 1.00 29.76 O ATOM 4520 CB ASP E 225 55.901 6.018 −6.885 1.00 29.19 C ATOM 4521 CG ASP E 225 55.128 7.221 −6.357 1.00 28.97 C ATOM 4522 OD1 ASP E 225 53.977 7.464 −6.809 1.00 25.87 O ATOM 4523 OD2 ASP E 225 55.694 7.940 −5.505 1.00 26.42 O ATOM 4524 N LYS E 226 56.206 2.639 −7.350 1.00 30.23 N ATOM 4525 CA LYS E 226 56.913 1.615 −8.113 1.00 30.24 C ATOM 4526 C LYS E 226 56.081 1.193 −9.323 1.00 29.94 C ATOM 4527 O LYS E 226 54.871 1.019 −9.206 1.00 29.84 O ATOM 4528 CB LYS E 226 57.202 0.399 −7.223 1.00 29.99 C ATOM 4529 CG LYS E 226 57.794 −0.806 −7.964 1.00 30.78 C ATOM 4530 CD LYS E 226 58.129 −1.933 −6.992 1.00 30.41 C ATOM 4531 CE LYS E 226 58.826 −3.099 −7.694 1.00 33.17 C ATOM 4532 NZ LYS E 226 59.329 −4.124 −6.720 1.00 32.61 N ATOM 4533 N GLY E 227 56.737 1.038 −10.477 1.00 29.05 N ATOM 4534 CA GLY E 227 56.046 0.638 −11.693 1.00 28.94 C ATOM 4535 C GLY E 227 56.776 1.071 −12.957 1.00 29.12 C ATOM 4536 O GLY E 227 57.935 1.490 −12.903 1.00 28.36 O ATOM 4537 N ASN E 228 56.109 0.956 −14.100 1.00 28.95 N ATOM 4538 CA ASN E 228 56.701 1.351 −15.374 1.00 29.57 C ATOM 4539 C ASN E 228 56.124 2.673 −15.864 1.00 28.26 C ATOM 4540 O ASN E 228 54.918 2.903 −15.768 1.00 28.23 O ATOM 4541 CB ASN E 228 56.455 0.294 −16.458 1.00 32.45 C ATOM 4542 CG ASN E 228 57.048 −1.054 −16.106 1.00 35.12 C ATOM 4543 OD1 ASN E 228 58.112 −1.139 −15.503 1.00 36.41 O ATOM 4544 ND2 ASN E 228 56.365 −2.116 −16.498 1.00 37.00 N ATOM 4545 N TYR E 229 56.995 3.532 −16.387 1.00 26.32 N ATOM 4546 CA TYR E 229 56.591 4.827 −16.921 1.00 25.19 C ATOM 4547 C TYR E 229 57.097 4.935 −18.350 1.00 25.34 C ATOM 4548 O TYR E 229 58.306 4.882 −18.616 1.00 24.46 O ATOM 4549 CB TYR E 229 57.132 5.964 −16.053 1.00 23.37 C ATOM 4550 CG TYR E 229 56.572 5.928 −14.650 1.00 24.79 C ATOM 4551 CD1 TYR E 229 57.101 5.068 −13.691 1.00 24.70 C ATOM 4552 CD2 TYR E 229 55.447 6.689 −14.306 1.00 24.93 C ATOM 4553 CE1 TYR E 229 56.521 4.954 −12.432 1.00 26.06 C ATOM 4554 CE2 TYR E 229 54.865 6.586 −13.059 1.00 23.86 C ATOM 4555 CZ TYR E 229 55.396 5.714 −12.126 1.00 26.06 C ATOM 4556 OH TYR E 229 54.769 5.550 −10.912 1.00 25.94 O ATOM 4557 N THR E 230 56.150 5.085 −19.271 1.00 25.17 N ATOM 4558 CA THR E 230 56.454 5.151 −20.694 1.00 24.43 C ATOM 4559 C THR E 230 56.142 6.485 −21.349 1.00 24.97 C ATOM 4560 O THR E 230 55.070 7.064 −21.156 1.00 24.36 O ATOM 4561 CB THR E 230 55.666 4.071 −21.457 1.00 24.48 C ATOM 4562 OG1 THR E 230 55.930 2.795 −20.863 1.00 24.81 O ATOM 4563 CG2 THR E 230 56.057 4.055 −22.931 1.00 22.29 C ATOM 4564 N CYS E 231 57.086 6.963 −22.144 1.00 26.19 N ATOM 4565 CA CYS E 231 56.899 8.212 −22.862 1.00 27.54 C ATOM 4566 C CYS E 231 56.607 7.858 −24.317 1.00 27.22 C ATOM 4567 O CYS E 231 57.333 7.065 −24.916 1.00 26.23 O ATOM 4568 CB CYS E 231 58.168 9.062 −22.783 1.00 27.82 C ATOM 4569 SG CYS E 231 59.585 8.263 −23.576 1.00 31.09 S ATOM 4570 N VAL E 232 55.533 8.427 −24.860 1.00 28.00 N ATOM 4571 CA VAL E 232 55.136 8.214 −26.249 1.00 29.12 C ATOM 4572 C VAL E 232 55.235 9.563 −26.970 1.00 29.74 C ATOM 4573 O VAL E 232 54.641 10.541 −26.546 1.00 31.15 O ATOM 4574 CB VAL E 232 53.693 7.700 −26.340 1.00 29.29 C ATOM 4575 CG1 VAL E 232 53.306 7.485 −27.798 1.00 28.53 C ATOM 4576 CG2 VAL E 232 53.557 6.407 −25.549 1.00 29.10 C ATOM 4577 N VAL E 233 56.001 9.607 −28.051 1.00 30.49 N ATOM 4578 CA VAL E 233 56.202 10.833 −28.807 1.00 31.77 C ATOM 4579 C VAL E 233 55.755 10.626 −30.254 1.00 32.47 C ATOM 4580 O VAL E 233 56.157 9.651 −30.903 1.00 32.76 O ATOM 4581 CB VAL E 233 57.694 11.243 −28.779 1.00 31.18 C ATOM 4582 CG1 VAL E 233 57.866 12.612 −29.379 1.00 33.05 C ATOM 4583 CG2 VAL E 233 58.199 11.250 −27.352 1.00 32.93 C ATOM 4584 N GLU E 234 54.951 11.551 −30.773 1.00 32.15 N ATOM 4585 CA GLU E 234 54.444 11.390 −32.129 1.00 33.60 C ATOM 4586 C GLU E 234 54.082 12.639 −32.948 1.00 33.59 C ATOM 4587 O GLU E 234 53.832 13.713 −32.405 1.00 33.70 O ATOM 4588 CB GLU E 234 53.210 10.480 −32.068 1.00 33.20 C ATOM 4589 N ASN E 235 54.068 12.460 −34.267 1.00 34.11 N ATOM 4590 CA ASN E 235 53.657 13.483 −35.233 1.00 34.29 C ATOM 4591 C ASN E 235 53.084 12.694 −36.411 1.00 35.08 C ATOM 4592 O ASN E 235 52.958 11.470 −36.314 1.00 34.59 O ATOM 4593 CB ASN E 235 54.810 14.414 −35.664 1.00 33.28 C ATOM 4594 CG ASN E 235 55.900 13.708 −36.447 1.00 33.88 C ATOM 4595 OD1 ASN E 235 55.730 12.583 −36.910 1.00 33.30 O ATOM 4596 ND2 ASN E 235 57.036 14.385 −36.609 1.00 34.18 N ATOM 4597 N GLU E 236 52.738 13.358 −37.512 1.00 36.42 N ATOM 4598 CA GLU E 236 52.138 12.629 −38.636 1.00 38.00 C ATOM 4599 C GLU E 236 53.011 11.594 −39.343 1.00 37.78 C ATOM 4600 O GLU E 236 52.486 10.739 −40.053 1.00 37.97 O ATOM 4601 CB GLU E 236 51.531 13.595 −39.664 1.00 40.24 C ATOM 4602 CG GLU E 236 52.492 14.582 −40.284 1.00 43.86 C ATOM 4603 CD GLU E 236 51.790 15.531 −41.242 1.00 46.25 C ATOM 4604 OE1 GLU E 236 51.225 15.059 −42.255 1.00 47.28 O ATOM 4605 OE2 GLU E 236 51.803 16.750 −40.976 1.00 47.49 O ATOM 4606 N TYR E 237 54.323 11.640 −39.121 1.00 37.33 N ATOM 4607 CA TYR E 237 55.242 10.708 −39.766 1.00 37.35 C ATOM 4608 C TYR E 237 55.754 9.569 −38.867 1.00 35.98 C ATOM 4609 O TYR E 237 56.577 8.758 −39.290 1.00 35.90 O ATOM 4610 CB TYR E 237 56.415 11.508 −40.346 1.00 38.92 C ATOM 4611 CG TYR E 237 55.957 12.649 −41.233 1.00 41.25 C ATOM 4612 CD1 TYR E 237 56.460 13.943 −41.059 1.00 43.19 C ATOM 4613 CD2 TYR E 237 55.004 12.444 −42.226 1.00 42.47 C ATOM 4614 CE1 TYR E 237 56.018 15.008 −41.855 1.00 44.62 C ATOM 4615 CE2 TYR E 237 54.554 13.495 −43.026 1.00 44.57 C ATOM 4616 CZ TYR E 237 55.062 14.777 −42.835 1.00 45.49 C ATOM 4617 OH TYR E 237 54.598 15.822 −43.609 1.00 46.29 O ATOM 4618 N GLY E 238 55.275 9.497 −37.632 1.00 34.97 N ATOM 4619 CA GLY E 238 55.731 8.417 −36.777 1.00 33.97 C ATOM 4620 C GLY E 238 55.405 8.507 −35.303 1.00 33.08 C ATOM 4621 O GLY E 238 54.983 9.548 −34.803 1.00 32.50 O ATOM 4622 N SER E 239 55.617 7.390 −34.612 1.00 32.34 N ATOM 4623 CA SER E 239 55.369 7.282 −33.181 1.00 31.81 C ATOM 4624 C SER E 239 56.404 6.351 −32.543 1.00 30.71 C ATOM 4625 O SER E 239 56.567 5.211 −32.980 1.00 30.65 O ATOM 4626 CB SER E 239 53.954 6.739 −32.942 1.00 30.90 C ATOM 4627 OG SER E 239 53.628 6.735 −31.563 1.00 33.07 O ATOM 4628 N ILE E 240 57.091 6.834 −31.510 1.00 29.56 N ATOM 4629 CA ILE E 240 58.112 6.042 −30.827 1.00 28.65 C ATOM 4630 C ILE E 240 57.935 6.162 −29.318 1.00 28.96 C ATOM 4631 O ILE E 240 57.382 7.152 −28.830 1.00 30.00 O ATOM 4632 CB ILE E 240 59.528 6.514 −31.210 1.00 28.14 C ATOM 4633 CG1 ILE E 240 59.726 7.960 −30.758 1.00 28.72 C ATOM 4634 CG2 ILE E 240 59.712 6.435 −32.729 1.00 26.24 C ATOM 4635 CD1 ILE E 240 61.132 8.520 −31.032 1.00 29.86 C ATOM 4636 N ASN E 241 58.405 5.157 −28.582 1.00 27.76 N ATOM 4637 CA ASN E 241 58.284 5.147 −27.136 1.00 26.27 C ATOM 4638 C ASN E 241 59.499 4.531 −26.439 1.00 26.41 C ATOM 4639 O ASN E 241 60.301 3.815 −27.058 1.00 25.18 O ATOM 4640 CB ASN E 241 57.018 4.384 −26.711 1.00 25.29 C ATOM 4641 CG ASN E 241 56.946 2.983 −27.311 1.00 27.08 C ATOM 4642 OD1 ASN E 241 56.345 2.769 −28.374 1.00 29.98 O ATOM 4643 ND2 ASN E 241 57.578 2.032 −26.652 1.00 26.55 N ATOM 4644 N HIS E 242 59.610 4.819 −25.145 1.00 26.04 N ATOM 4645 CA HIS E 242 60.693 4.317 −24.309 1.00 27.09 C ATOM 4646 C HIS E 242 60.130 4.097 −22.913 1.00 26.68 C ATOM 4647 O HIS E 242 59.274 4.865 −22.464 1.00 26.32 O ATOM 4648 CB HIS E 242 61.833 5.325 −24.233 1.00 28.10 C ATOM 4649 CG HIS E 242 62.957 4.888 −23.352 1.00 29.54 C ATOM 4650 ND1 HIS E 242 63.851 3.904 −23.716 1.00 30.25 N ATOM 4651 CD2 HIS E 242 63.341 5.309 −22.124 1.00 31.00 C ATOM 4652 CE1 HIS E 242 64.742 3.744 −22.754 1.00 32.05 C ATOM 4653 NE2 HIS E 242 64.455 4.585 −21.778 1.00 32.16 N ATOM 4654 N THR E 243 60.617 3.068 −22.225 1.00 26.12 N ATOM 4655 CA THR E 243 60.112 2.759 −20.893 1.00 26.90 C ATOM 4656 C THR E 243 61.134 2.756 −19.770 1.00 27.39 C ATOM 4657 O THR E 243 62.219 2.202 −19.908 1.00 27.23 O ATOM 4658 CB THR E 243 59.377 1.381 −20.871 1.00 26.77 C ATOM 4659 OG1 THR E 243 58.225 1.439 −21.716 1.00 25.38 O ATOM 4660 CG2 THR E 243 58.917 1.032 −19.449 1.00 26.06 C ATOM 4661 N TYR E 244 60.757 3.390 −18.662 1.00 27.91 N ATOM 4662 CA TYR E 244 61.581 3.460 −17.465 1.00 29.32 C ATOM 4663 C TYR E 244 60.898 2.640 −16.370 1.00 30.85 C ATOM 4664 O TYR E 244 59.677 2.506 −16.354 1.00 30.71 O ATOM 4665 CB TYR E 244 61.723 4.899 −16.960 1.00 27.74 C ATOM 4666 CG TYR E 244 62.566 5.802 −17.828 1.00 27.95 C ATOM 4667 CD1 TYR E 244 61.987 6.840 −18.564 1.00 26.62 C ATOM 4668 CD2 TYR E 244 63.951 5.640 −17.888 1.00 26.74 C ATOM 4669 CE1 TYR E 244 62.769 7.696 −19.334 1.00 27.44 C ATOM 4670 CE2 TYR E 244 64.739 6.481 −18.651 1.00 27.77 C ATOM 4671 CZ TYR E 244 64.147 7.511 −19.371 1.00 28.12 C ATOM 4672 OH TYR E 244 64.943 8.350 −20.107 1.00 27.83 O ATOM 4673 N HIS E 245 61.693 2.088 −15.464 1.00 31.97 N ATOM 4674 CA HIS E 245 61.161 1.322 −14.349 1.00 33.12 C ATOM 4675 C HIS E 245 61.552 2.073 −13.083 1.00 33.00 C ATOM 4676 O HIS E 245 62.706 2.472 −12.929 1.00 32.70 O ATOM 4677 CB HIS E 245 61.760 −0.085 −14.341 1.00 34.97 C ATOM 4678 CG HIS E 245 61.552 −0.826 −15.629 1.00 37.68 C ATOM 4679 ND1 HIS E 245 60.342 −1.378 −15.982 1.00 38.21 N ATOM 4680 CD2 HIS E 245 62.396 −1.081 −16.657 1.00 39.69 C ATOM 4681 CE1 HIS E 245 60.444 −1.941 −17.175 1.00 38.71 C ATOM 4682 NE2 HIS E 245 61.684 −1.772 −17.607 1.00 39.57 N ATOM 4683 N LEU E 246 60.594 2.292 −12.190 1.00 32.23 N ATOM 4684 CA LEU E 246 60.886 3.001 −10.951 1.00 32.14 C ATOM 4685 C LEU E 246 60.742 2.103 −9.728 1.00 33.28 C ATOM 4686 O LEU E 246 59.802 1.309 −9.628 1.00 34.04 O ATOM 4687 CB LEU E 246 59.974 4.228 −10.794 1.00 29.30 C ATOM 4688 CG LEU E 246 60.035 4.965 −9.443 1.00 28.46 C ATOM 4689 CD1 LEU E 246 61.416 5.654 −9.272 1.00 27.02 C ATOM 4690 CD2 LEU E 246 58.903 6.010 −9.365 1.00 24.91 C ATOM 4691 N ASP E 247 61.690 2.224 −8.804 1.00 34.64 N ATOM 4692 CA ASP E 247 61.653 1.454 −7.564 1.00 36.26 C ATOM 4693 C ASP E 247 62.022 2.415 −6.441 1.00 36.40 C ATOM 4694 O ASP E 247 62.929 3.242 −6.597 1.00 36.83 O ATOM 4695 CB ASP E 247 62.637 0.269 −7.619 1.00 37.20 C ATOM 4696 CG ASP E 247 62.243 −0.872 −6.670 1.00 39.20 C ATOM 4697 OD1 ASP E 247 62.687 −2.025 −6.884 1.00 40.40 O ATOM 4698 OD2 ASP E 247 61.494 −0.621 −5.703 1.00 39.88 O ATOM 4699 N VAL E 248 61.309 2.327 −5.322 1.00 36.45 N ATOM 4700 CA VAL E 248 61.563 3.204 −4.194 1.00 36.17 C ATOM 4701 C VAL E 248 61.964 2.413 −2.959 1.00 36.51 C ATOM 4702 O VAL E 248 61.353 1.391 −2.637 1.00 37.11 O ATOM 4703 CB VAL E 248 60.328 4.060 −3.891 1.00 36.50 C ATOM 4704 CG1 VAL E 248 60.629 5.054 −2.775 1.00 35.40 C ATOM 4705 CG2 VAL E 248 59.904 4.785 −5.156 1.00 36.50 C ATOM 4706 N VAL E 249 63.000 2.897 −2.279 1.00 35.72 N ATOM 4707 CA VAL E 249 63.534 2.253 −1.085 1.00 35.92 C ATOM 4708 C VAL E 249 63.487 3.191 0.121 1.00 36.10 C ATOM 4709 O VAL E 249 64.017 4.301 0.080 1.00 35.27 O ATOM 4710 CB VAL E 249 65.019 1.824 −1.313 1.00 35.97 C ATOM 4711 CG1 VAL E 249 65.575 1.161 −0.060 1.00 35.72 C ATOM 4712 CG2 VAL E 249 65.118 0.890 −2.500 1.00 35.65 C ATOM 4713 N GLU E 250 62.866 2.739 1.199 1.00 36.41 N ATOM 4714 CA GLU E 250 62.776 3.555 2.402 1.00 37.64 C ATOM 4715 C GLU E 250 64.031 3.372 3.246 1.00 36.43 C ATOM 4716 O GLU E 250 64.413 2.252 3.553 1.00 36.31 O ATOM 4717 CB GLU E 250 61.523 3.156 3.189 1.00 39.76 C ATOM 4718 CG GLU E 250 60.238 3.451 2.429 1.00 43.74 C ATOM 4719 CD GLU E 250 58.994 2.886 3.103 1.00 46.43 C ATOM 4720 OE1 GLU E 250 58.842 1.644 3.131 1.00 47.52 O ATOM 4721 OE2 GLU E 250 58.173 3.691 3.602 1.00 47.61 O ATOM 4722 N ARG E 251 64.673 4.479 3.605 1.00 35.83 N ATOM 4723 CA ARG E 251 65.887 4.452 4.410 1.00 34.82 C ATOM 4724 C ARG E 251 65.534 4.841 5.837 1.00 35.98 C ATOM 4725 O ARG E 251 64.655 5.659 6.048 1.00 36.11 O ATOM 4726 CB ARG E 251 66.912 5.434 3.848 1.00 32.96 C ATOM 4727 CG ARG E 251 67.309 5.148 2.405 1.00 30.43 C ATOM 4728 CD ARG E 251 67.624 3.661 2.208 1.00 28.89 C ATOM 4729 NE ARG E 251 68.650 3.166 3.125 1.00 25.79 N ATOM 4730 CZ ARG E 251 69.962 3.342 2.973 1.00 24.83 C ATOM 4731 NH1 ARG E 251 70.448 4.011 1.934 1.00 24.17 N ATOM 4732 NH2 ARG E 251 70.798 2.812 3.854 1.00 25.42 N ATOM 4733 N SER E 252 66.208 4.261 6.821 1.00 35.82 N ATOM 4734 CA SER E 252 65.943 4.546 8.227 1.00 36.14 C ATOM 4735 C SER E 252 67.213 5.007 8.944 1.00 36.13 C ATOM 4736 O SER E 252 68.037 4.196 9.349 1.00 35.73 O ATOM 4737 CB SER E 252 65.379 3.291 8.901 1.00 36.34 C ATOM 4738 OG SER E 252 65.345 3.445 10.308 1.00 39.29 O ATOM 4739 N PRO E 253 67.384 6.319 9.112 1.00 36.78 N ATOM 4740 CA PRO E 253 68.579 6.842 9.782 1.00 37.06 C ATOM 4741 C PRO E 253 68.593 6.740 11.310 1.00 37.49 C ATOM 4742 O PRO E 253 68.899 7.715 11.992 1.00 38.41 O ATOM 4743 CB PRO E 253 68.644 8.285 9.289 1.00 37.46 C ATOM 4744 CG PRO E 253 67.196 8.649 9.163 1.00 37.04 C ATOM 4745 CD PRO E 253 66.576 7.413 8.535 1.00 36.82 C ATOM 4746 N HIS E 254 68.263 5.572 11.849 1.00 37.59 N ATOM 4747 CA HIS E 254 68.281 5.390 13.299 1.00 37.95 C ATOM 4748 C HIS E 254 69.383 4.430 13.742 1.00 36.67 C ATOM 4749 O HIS E 254 69.880 3.632 12.956 1.00 35.85 O ATOM 4750 CB HIS E 254 66.943 4.851 13.814 1.00 40.15 C ATOM 4751 CG HIS E 254 65.788 5.774 13.584 1.00 43.58 C ATOM 4752 ND1 HIS E 254 65.029 5.746 12.431 1.00 45.48 N ATOM 4753 CD2 HIS E 254 65.270 6.761 14.352 1.00 44.54 C ATOM 4754 CE1 HIS E 254 64.092 6.675 12.500 1.00 45.14 C ATOM 4755 NE2 HIS E 254 64.216 7.305 13.656 1.00 46.03 N ATOM 4756 N ARG E 255 69.773 4.526 15.004 1.00 35.96 N ATOM 4757 CA ARG E 255 70.767 3.615 15.534 1.00 35.50 C ATOM 4758 C ARG E 255 70.008 2.282 15.656 1.00 34.66 C ATOM 4759 O ARG E 255 68.777 2.262 15.560 1.00 34.53 O ATOM 4760 CB ARG E 255 71.261 4.102 16.897 1.00 37.29 C ATOM 4761 CG ARG E 255 70.222 4.051 17.999 1.00 39.20 C ATOM 4762 CD ARG E 255 70.851 4.379 19.349 1.00 41.59 C ATOM 4763 NE ARG E 255 69.966 4.025 20.454 1.00 44.03 N ATOM 4764 CZ ARG E 255 68.825 4.649 20.734 1.00 45.95 C ATOM 4765 NH1 ARG E 255 68.425 5.675 19.992 1.00 47.53 N ATOM 4766 NH2 ARG E 255 68.070 4.236 21.745 1.00 46.53 N ATOM 4767 N PRO E 256 70.716 1.162 15.855 1.00 33.03 N ATOM 4768 CA PRO E 256 70.046 −0.141 15.974 1.00 32.21 C ATOM 4769 C PRO E 256 68.968 −0.207 17.055 1.00 31.23 C ATOM 4770 O PRO E 256 69.136 0.340 18.136 1.00 31.38 O ATOM 4771 CB PRO E 256 71.198 −1.101 16.271 1.00 31.81 C ATOM 4772 CG PRO E 256 72.384 −0.432 15.589 1.00 32.06 C ATOM 4773 CD PRO E 256 72.177 1.016 15.984 1.00 33.61 C ATOM 4774 N ILE E 257 67.865 −0.882 16.749 1.00 30.78 N ATOM 4775 CA ILE E 257 66.775 −1.047 17.705 1.00 31.56 C ATOM 4776 C ILE E 257 66.654 −2.528 18.123 1.00 31.18 C ATOM 4777 O ILE E 257 66.677 −3.417 17.276 1.00 30.43 O ATOM 4778 CB ILE E 257 65.449 −0.540 17.092 1.00 33.43 C ATOM 4779 CG1 ILE E 257 65.520 0.985 16.923 1.00 34.39 C ATOM 4780 CG2 ILE E 257 64.281 −0.937 17.967 1.00 33.57 C ATOM 4781 CD1 ILE E 257 64.240 1.624 16.450 1.00 36.23 C ATOM 4782 N LEU E 258 66.566 −2.785 19.429 1.00 30.38 N ATOM 4783 CA LEU E 258 66.448 −4.154 19.930 1.00 30.95 C ATOM 4784 C LEU E 258 65.035 −4.436 20.434 1.00 31.23 C ATOM 4785 O LEU E 258 64.336 −3.525 20.884 1.00 30.88 O ATOM 4786 CB LEU E 258 67.429 −4.409 21.081 1.00 29.89 C ATOM 4787 CG LEU E 258 68.918 −4.041 20.966 1.00 32.11 C ATOM 4788 CD1 LEU E 258 69.709 −4.974 21.852 1.00 29.79 C ATOM 4789 CD2 LEU E 258 69.422 −4.144 19.535 1.00 31.84 C ATOM 4790 N GLN E 259 64.625 −5.696 20.367 1.00 31.39 N ATOM 4791 CA GLN E 259 63.303 −6.084 20.839 1.00 32.44 C ATOM 4792 C GLN E 259 63.272 −6.063 22.372 1.00 32.23 C ATOM 4793 O GLN E 259 64.172 −6.598 23.035 1.00 31.48 O ATOM 4794 CB GLN E 259 62.947 −7.485 20.339 1.00 33.89 C ATOM 4795 CG GLN E 259 61.577 −7.972 20.778 1.00 36.67 C ATOM 4796 CD GLN E 259 61.402 −9.462 20.547 1.00 38.34 C ATOM 4797 OE1 GLN E 259 61.645 −9.961 19.451 1.00 39.45 O ATOM 4798 NE2 GLN E 259 60.980 −10.178 21.580 1.00 39.08 N ATOM 4799 N ALA E 260 62.238 −5.443 22.931 1.00 31.78 N ATOM 4800 CA ALA E 260 62.103 −5.366 24.386 1.00 32.73 C ATOM 4801 C ALA E 260 61.931 −6.757 24.992 1.00 32.75 C ATOM 4802 O ALA E 260 61.249 −7.600 24.427 1.00 33.21 O ATOM 4803 CB ALA E 260 60.905 −4.475 24.765 1.00 32.81 C ATOM 4804 N GLY E 261 62.565 −6.991 26.137 1.00 32.60 N ATOM 4805 CA GLY E 261 62.457 −8.282 26.792 1.00 33.01 C ATOM 4806 C GLY E 261 63.577 −9.258 26.473 1.00 33.86 C ATOM 4807 O GLY E 261 63.711 −10.282 27.139 1.00 33.46 O ATOM 4808 N LEU E 262 64.380 −8.952 25.456 1.00 34.46 N ATOM 4809 CA LEU E 262 65.478 −9.836 25.060 1.00 34.63 C ATOM 4810 C LEU E 262 66.821 −9.128 25.125 1.00 35.41 C ATOM 4811 O LEU E 262 66.963 −7.999 24.668 1.00 35.68 O ATOM 4812 CB LEU E 262 65.253 −10.367 23.647 1.00 34.06 C ATOM 4813 CG LEU E 262 64.042 −11.289 23.456 1.00 35.07 C ATOM 4814 CD1 LEU E 262 63.957 −11.728 21.988 1.00 32.19 C ATOM 4815 CD2 LEU E 262 64.177 −12.513 24.369 1.00 33.00 C ATOM 4816 N PRO E 263 67.835 −9.794 25.690 1.00 36.61 N ATOM 4817 CA PRO E 263 67.751 −11.144 26.256 1.00 36.99 C ATOM 4818 C PRO E 263 66.947 −11.202 27.552 1.00 37.76 C ATOM 4819 O PRO E 263 66.684 −10.180 28.181 1.00 37.69 O ATOM 4820 CB PRO E 263 69.216 −11.505 26.464 1.00 37.44 C ATOM 4821 CG PRO E 263 69.809 −10.185 26.849 1.00 36.22 C ATOM 4822 CD PRO E 263 69.197 −9.254 25.830 1.00 36.32 C ATOM 4823 N ALA E 264 66.561 −12.406 27.949 1.00 39.07 N ATOM 4824 CA ALA E 264 65.789 −12.588 29.173 1.00 40.24 C ATOM 4825 C ALA E 264 66.647 −13.176 30.284 1.00 40.74 C ATOM 4826 O ALA E 264 67.602 −13.911 30.024 1.00 40.98 O ATOM 4827 CB ALA E 264 64.586 −13.497 28.905 1.00 40.12 C ATOM 4828 N ASN E 265 66.308 −12.833 31.523 1.00 42.19 N ATOM 4829 CA ASN E 265 67.027 −13.352 32.680 1.00 43.62 C ATOM 4830 C ASN E 265 66.936 −14.880 32.650 1.00 44.58 C ATOM 4831 O ASN E 265 65.966 −15.445 32.124 1.00 44.42 O ATOM 4832 CB ASN E 265 66.399 −12.817 33.969 1.00 44.05 C ATOM 4833 CG ASN E 265 67.055 −11.536 34.456 1.00 45.16 C ATOM 4834 OD1 ASN E 265 67.185 −10.557 33.718 1.00 44.14 O ATOM 4835 ND2 ASN E 265 67.471 −11.540 35.716 1.00 46.55 N ATOM 4836 N ALA E 266 67.947 −15.545 33.198 1.00 45.09 N ATOM 4837 CA ALA E 266 67.955 −17.004 33.230 1.00 46.13 C ATOM 4838 C ALA E 266 68.539 −17.506 34.545 1.00 46.86 C ATOM 4839 O ALA E 266 69.381 −16.842 35.162 1.00 46.71 O ATOM 4840 CB ALA E 266 68.750 −17.556 32.046 1.00 45.45 C ATOM 4841 N SER E 267 68.077 −18.679 34.971 1.00 47.77 N ATOM 4842 CA SER E 267 68.538 −19.290 36.212 1.00 48.84 C ATOM 4843 C SER E 267 68.774 −20.781 35.989 1.00 49.84 C ATOM 4844 O SER E 267 68.054 −21.425 35.214 1.00 50.77 O ATOM 4845 CB SER E 267 67.502 −19.090 37.323 1.00 48.70 C ATOM 4846 N ASP E 273 72.922 −25.916 31.411 1.00 52.50 N ATOM 4847 CA ASP E 273 73.121 −25.160 30.177 1.00 52.79 C ATOM 4848 C ASP E 273 72.109 −24.024 30.024 1.00 52.36 C ATOM 4849 O ASP E 273 70.968 −24.115 30.493 1.00 52.76 O ATOM 4850 CB ASP E 273 73.069 −26.097 28.964 1.00 53.36 C ATOM 4851 CG ASP E 273 74.391 −26.816 28.729 1.00 53.74 C ATOM 4852 OD1 ASP E 273 75.031 −27.208 29.723 1.00 54.01 O ATOM 4853 OD2 ASP E 273 74.786 −26.998 27.557 1.00 53.01 O ATOM 4854 N VAL E 274 72.535 −22.949 29.367 1.00 51.31 N ATOM 4855 CA VAL E 274 71.671 −21.785 29.182 1.00 50.20 C ATOM 4856 C VAL E 274 71.954 −21.011 27.891 1.00 49.58 C ATOM 4857 O VAL E 274 72.997 −21.178 27.255 1.00 49.28 O ATOM 4858 CB VAL E 274 71.830 −20.800 30.366 1.00 49.84 C ATOM 4859 CG1 VAL E 274 73.191 −20.125 30.298 1.00 49.41 C ATOM 4860 CG2 VAL E 274 70.720 −19.770 30.349 1.00 50.22 C ATOM 4861 N GLU E 275 71.010 −20.159 27.509 1.00 48.78 N ATOM 4862 CA GLU E 275 71.183 −19.335 26.329 1.00 47.91 C ATOM 4863 C GLU E 275 70.564 −17.960 26.526 1.00 46.62 C ATOM 4864 O GLU E 275 69.689 −17.765 27.368 1.00 46.91 O ATOM 4865 CB GLU E 275 70.570 −19.993 25.099 1.00 48.23 C ATOM 4866 CG GLU E 275 69.073 −20.101 25.150 1.00 49.42 C ATOM 4867 CD GLU E 275 68.487 −20.457 23.802 1.00 50.68 C ATOM 4868 OE1 GLU E 275 69.158 −21.191 23.039 1.00 51.67 O ATOM 4869 OE2 GLU E 275 67.356 −20.011 23.510 1.00 51.40 O ATOM 4870 N PHE E 276 71.051 −17.005 25.746 1.00 44.96 N ATOM 4871 CA PHE E 276 70.557 −15.642 25.781 1.00 43.18 C ATOM 4872 C PHE E 276 70.298 −15.259 24.342 1.00 42.01 C ATOM 4873 O PHE E 276 71.174 −15.394 23.488 1.00 41.08 O ATOM 4874 CB PHE E 276 71.595 −14.715 26.398 1.00 44.88 C ATOM 4875 CG PHE E 276 71.764 −14.901 27.878 1.00 46.37 C ATOM 4876 CD1 PHE E 276 70.721 −14.605 28.749 1.00 46.80 C ATOM 4877 CD2 PHE E 276 72.977 −15.350 28.402 1.00 46.66 C ATOM 4878 CE1 PHE E 276 70.883 −14.749 30.129 1.00 48.86 C ATOM 4879 CE2 PHE E 276 73.154 −15.499 29.775 1.00 48.80 C ATOM 4880 CZ PHE E 276 72.104 −15.198 30.648 1.00 48.50 C ATOM 4881 N VAL E 277 69.084 −14.799 24.072 1.00 40.85 N ATOM 4882 CA VAL E 277 68.710 −14.420 22.722 1.00 40.07 C ATOM 4883 C VAL E 277 68.559 −12.922 22.573 1.00 39.63 C ATOM 4884 O VAL E 277 68.187 −12.216 23.512 1.00 40.44 O ATOM 4885 CB VAL E 277 67.393 −15.087 22.303 1.00 39.97 C ATOM 4886 CG1 VAL E 277 67.072 −14.742 20.862 1.00 39.49 C ATOM 4887 CG2 VAL E 277 67.503 −16.591 22.484 1.00 40.06 C ATOM 4888 N CYS E 278 68.850 −12.438 21.376 1.00 38.95 N ATOM 4889 CA CYS E 278 68.744 −11.023 21.092 1.00 38.48 C ATOM 4890 C CYS E 278 68.168 −10.848 19.694 1.00 37.35 C ATOM 4891 O CYS E 278 68.469 −11.642 18.809 1.00 37.61 O ATOM 4892 CB CYS E 278 70.122 −10.375 21.170 1.00 39.85 C ATOM 4893 SG CYS E 278 70.048 −8.589 21.045 1.00 44.17 S ATOM 4894 N LYS E 279 67.334 −9.825 19.506 1.00 35.62 N ATOM 4895 CA LYS E 279 66.729 −9.538 18.198 1.00 34.29 C ATOM 4896 C LYS E 279 66.988 −8.093 17.770 1.00 33.03 C ATOM 4897 O LYS E 279 66.437 −7.149 18.356 1.00 31.92 O ATOM 4898 CB LYS E 279 65.214 −9.788 18.220 1.00 34.84 C ATOM 4899 CG LYS E 279 64.798 −11.190 17.806 1.00 37.35 C ATOM 4900 CD LYS E 279 65.191 −11.495 16.349 1.00 37.45 C ATOM 4901 CE LYS E 279 64.485 −10.561 15.370 1.00 38.22 C ATOM 4902 NZ LYS E 279 64.821 −10.836 13.944 1.00 36.90 N ATOM 4903 N VAL E 280 67.799 −7.933 16.727 1.00 31.70 N ATOM 4904 CA VAL E 280 68.179 −6.614 16.223 1.00 30.63 C ATOM 4905 C VAL E 280 67.595 −6.185 14.877 1.00 30.67 C ATOM 4906 O VAL E 280 67.388 −7.000 13.972 1.00 30.96 O ATOM 4907 CB VAL E 280 69.721 −6.510 16.128 1.00 31.01 C ATOM 4908 CG1 VAL E 280 70.128 −5.143 15.601 1.00 30.63 C ATOM 4909 CG2 VAL E 280 70.344 −6.785 17.501 1.00 30.60 C ATOM 4910 N TYR E 281 67.340 −4.883 14.758 1.00 30.41 N ATOM 4911 CA TYR E 281 66.812 −4.277 13.534 1.00 30.43 C ATOM 4912 C TYR E 281 67.654 −3.033 13.214 1.00 29.51 C ATOM 4913 O TYR E 281 67.939 −2.232 14.101 1.00 30.49 O ATOM 4914 CB TYR E 281 65.341 −3.885 13.726 1.00 30.72 C ATOM 4915 N SER E 282 68.059 −2.881 11.959 1.00 28.51 N ATOM 4916 CA SER E 282 68.873 −1.743 11.541 1.00 28.49 C ATOM 4917 C SER E 282 68.981 −1.649 10.016 1.00 28.34 C ATOM 4918 O SER E 282 68.990 −2.670 9.335 1.00 28.39 O ATOM 4919 CB SER E 282 70.276 −1.872 12.144 1.00 28.98 C ATOM 4920 OG SER E 282 71.129 −0.841 11.680 1.00 27.93 O ATOM 4921 N ASP E 283 69.053 −0.425 9.489 1.00 28.16 N ATOM 4922 CA ASP E 283 69.186 −0.203 8.043 1.00 27.48 C ATOM 4923 C ASP E 283 70.686 −0.255 7.763 1.00 27.69 C ATOM 4924 O ASP E 283 71.153 −1.114 7.020 1.00 27.69 O ATOM 4925 CB ASP E 283 68.635 1.173 7.652 1.00 27.30 C ATOM 4926 CG ASP E 283 68.615 1.398 6.138 1.00 26.87 C ATOM 4927 OD1 ASP E 283 69.363 0.720 5.396 1.00 26.10 O ATOM 4928 OD2 ASP E 283 67.847 2.276 5.689 1.00 26.11 O ATOM 4929 N ALA E 284 71.432 0.671 8.363 1.00 26.91 N ATOM 4930 CA ALA E 284 72.885 0.684 8.230 1.00 27.55 C ATOM 4931 C ALA E 284 73.342 −0.636 8.860 1.00 27.06 C ATOM 4932 O ALA E 284 72.814 −1.034 9.903 1.00 26.87 O ATOM 4933 CB ALA E 284 73.485 1.859 9.011 1.00 26.70 C ATOM 4934 N GLN E 285 74.303 −1.320 8.241 1.00 26.18 N ATOM 4935 CA GLN E 285 74.783 −2.598 8.807 1.00 26.17 C ATOM 4936 C GLN E 285 75.162 −2.456 10.277 1.00 25.13 C ATOM 4937 O GLN E 285 75.998 −1.627 10.636 1.00 25.37 O ATOM 4938 CB GLN E 285 76.004 −3.168 8.062 1.00 26.14 C ATOM 4939 CG GLN E 285 75.734 −3.808 6.714 1.00 27.73 C ATOM 4940 CD GLN E 285 74.706 −4.913 6.765 1.00 27.55 C ATOM 4941 OE1 GLN E 285 73.663 −4.815 6.136 1.00 29.93 O ATOM 4942 NE2 GLN E 285 74.992 −5.973 7.516 1.00 29.65 N ATOM 4943 N PRO E 286 74.543 −3.274 11.141 1.00 24.69 N ATOM 4944 CA PRO E 286 74.825 −3.245 12.580 1.00 25.25 C ATOM 4945 C PRO E 286 75.918 −4.237 12.992 1.00 25.84 C ATOM 4946 O PRO E 286 76.096 −5.270 12.359 1.00 27.46 O ATOM 4947 CB PRO E 286 73.467 −3.605 13.181 1.00 24.49 C ATOM 4948 CG PRO E 286 72.960 −4.655 12.225 1.00 23.95 C ATOM 4949 CD PRO E 286 73.349 −4.085 10.851 1.00 24.51 C ATOM 4950 N HIS E 287 76.654 −3.911 14.052 1.00 26.68 N ATOM 4951 CA HIS E 287 77.702 −4.786 14.571 1.00 27.28 C ATOM 4952 C HIS E 287 77.250 −5.261 15.950 1.00 27.80 C ATOM 4953 O HIS E 287 77.062 −4.458 16.868 1.00 27.59 O ATOM 4954 CB HIS E 287 79.044 −4.055 14.680 1.00 27.34 C ATOM 4955 CG HIS E 287 80.167 −4.937 15.139 1.00 28.97 C ATOM 4956 ND1 HIS E 287 80.689 −4.880 16.416 1.00 29.15 N ATOM 4957 CD2 HIS E 287 80.832 −5.935 14.506 1.00 28.29 C ATOM 4958 CE1 HIS E 287 81.625 −5.803 16.551 1.00 29.45 C ATOM 4959 NE2 HIS E 287 81.731 −6.459 15.406 1.00 29.06 N ATOM 4960 N ILE E 288 77.061 −6.570 16.081 1.00 28.01 N ATOM 4961 CA ILE E 288 76.584 −7.159 17.323 1.00 29.20 C ATOM 4962 C ILE E 288 77.650 −7.931 18.104 1.00 30.30 C ATOM 4963 O ILE E 288 78.469 −8.645 17.521 1.00 31.71 O ATOM 4964 CB ILE E 288 75.385 −8.087 17.018 1.00 27.76 C ATOM 4965 CG1 ILE E 288 74.285 −7.278 16.316 1.00 28.76 C ATOM 4966 CG2 ILE E 288 74.850 −8.717 18.290 1.00 27.88 C ATOM 4967 CD1 ILE E 288 73.227 −8.141 15.623 1.00 25.74 C ATOM 4968 N GLN E 289 77.641 −7.771 19.426 1.00 31.39 N ATOM 4969 CA GLN E 289 78.580 −8.475 20.292 1.00 33.14 C ATOM 4970 C GLN E 289 77.924 −8.769 21.633 1.00 33.52 C ATOM 4971 O GLN E 289 76.961 −8.102 22.018 1.00 34.50 O ATOM 4972 CB GLN E 289 79.861 −7.650 20.495 1.00 34.53 C ATOM 4973 CG GLN E 289 79.655 −6.240 21.025 1.00 35.38 C ATOM 4974 CD GLN E 289 80.970 −5.538 21.279 1.00 37.44 C ATOM 4975 OE1 GLN E 289 81.851 −6.087 21.938 1.00 39.19 O ATOM 4976 NE2 GLN E 289 81.113 −4.319 20.765 1.00 37.44 N ATOM 4977 N TRP E 290 78.425 −9.789 22.323 1.00 33.78 N ATOM 4978 CA TRP E 290 77.902 −10.171 23.628 1.00 34.30 C ATOM 4979 C TRP E 290 78.965 −9.867 24.670 1.00 35.91 C ATOM 4980 O TRP E 290 80.131 −10.253 24.515 1.00 36.39 O ATOM 4981 CB TRP E 290 77.537 −11.663 23.669 1.00 32.84 C ATOM 4982 CG TRP E 290 76.254 −12.011 22.953 1.00 31.62 C ATOM 4983 CD1 TRP E 290 76.120 −12.430 21.659 1.00 32.53 C ATOM 4984 CD2 TRP E 290 74.931 −11.985 23.503 1.00 30.60 C ATOM 4985 NE1 TRP E 290 74.796 −12.673 21.369 1.00 30.76 N ATOM 4986 CE2 TRP E 290 74.045 −12.406 22.484 1.00 31.02 C ATOM 4987 CE3 TRP E 290 74.406 −11.644 24.757 1.00 30.73 C ATOM 4988 CZ2 TRP E 290 72.661 −12.497 22.680 1.00 30.30 C ATOM 4989 CZ3 TRP E 290 73.029 −11.736 24.955 1.00 30.32 C ATOM 4990 CH2 TRP E 290 72.173 −12.159 23.918 1.00 31.09 C ATOM 4991 N ILE E 291 78.561 −9.176 25.731 1.00 37.47 N ATOM 4992 CA ILE E 291 79.487 −8.787 26.785 1.00 39.92 C ATOM 4993 C ILE E 291 79.075 −9.239 28.185 1.00 41.83 C ATOM 4994 O ILE E 291 77.892 −9.260 28.529 1.00 41.92 O ATOM 4995 CB ILE E 291 79.658 −7.263 26.808 1.00 39.84 C ATOM 4996 CG1 ILE E 291 80.151 −6.777 25.442 1.00 39.98 C ATOM 4997 CG2 ILE E 291 80.619 −6.867 27.912 1.00 39.95 C ATOM 4998 CD1 ILE E 291 80.132 −5.274 25.295 1.00 40.10 C ATOM 4999 N LYS E 292 80.073 −9.601 28.988 1.00 43.20 N ATOM 5000 CA LYS E 292 79.856 −10.022 30.366 1.00 44.66 C ATOM 5001 C LYS E 292 80.471 −8.948 31.251 1.00 45.75 C ATOM 5002 O LYS E 292 81.609 −8.523 31.028 1.00 45.37 O ATOM 5003 CB LYS E 292 80.536 −11.362 30.649 1.00 44.86 C ATOM 5004 N HIS E 293 79.714 −8.506 32.250 1.00 47.10 N ATOM 5005 CA HIS E 293 80.183 −7.476 33.167 1.00 48.94 C ATOM 5006 C HIS E 293 81.057 −8.107 34.242 1.00 50.05 C ATOM 5007 O HIS E 293 80.555 −8.806 35.125 1.00 50.26 O ATOM 5008 CB HIS E 293 78.988 −6.768 33.816 1.00 48.54 C ATOM 5009 N VAL E 294 82.363 −7.861 34.155 1.00 51.57 N ATOM 5010 CA VAL E 294 83.319 −8.401 35.115 1.00 53.36 C ATOM 5011 C VAL E 294 83.961 −7.281 35.930 1.00 54.68 C ATOM 5012 O VAL E 294 84.546 −7.524 36.986 1.00 56.28 O ATOM 5013 CB VAL E 294 84.436 −9.201 34.407 1.00 53.01 C ATOM 5014 N PRO E 307 83.804 0.595 34.001 1.00 60.83 N ATOM 5015 CA PRO E 307 83.190 −0.739 34.037 1.00 60.46 C ATOM 5016 C PRO E 307 84.063 −1.813 33.386 1.00 59.98 C ATOM 5017 O PRO E 307 84.386 −1.725 32.199 1.00 60.20 O ATOM 5018 CB PRO E 307 81.880 −0.530 33.280 1.00 60.75 C ATOM 5019 CG PRO E 307 82.275 0.476 32.231 1.00 60.65 C ATOM 5020 CD PRO E 307 83.107 1.468 33.037 1.00 61.05 C ATOM 5021 N TYR E 308 84.441 −2.822 34.166 1.00 58.80 N ATOM 5022 CA TYR E 308 85.266 −3.917 33.655 1.00 57.71 C ATOM 5023 C TYR E 308 84.411 −4.844 32.796 1.00 56.51 C ATOM 5024 O TYR E 308 83.524 −5.533 33.301 1.00 57.08 O ATOM 5025 CB TYR E 308 85.887 −4.707 34.815 1.00 57.74 C ATOM 5026 N LEU E 309 84.689 −4.865 31.497 1.00 55.13 N ATOM 5027 CA LEU E 309 83.926 −5.690 30.570 1.00 53.60 C ATOM 5028 C LEU E 309 84.771 −6.784 29.916 1.00 52.13 C ATOM 5029 O LEU E 309 85.991 −6.664 29.813 1.00 52.33 O ATOM 5030 CB LEU E 309 83.313 −4.788 29.496 1.00 53.76 C ATOM 5031 CG LEU E 309 82.632 −3.528 30.042 1.00 54.69 C ATOM 5032 CD1 LEU E 309 82.231 −2.615 28.886 1.00 55.37 C ATOM 5033 CD2 LEU E 309 81.426 −3.910 30.889 1.00 54.17 C ATOM 5034 N LYS E 310 84.111 −7.852 29.483 1.00 49.92 N ATOM 5035 CA LYS E 310 84.784 −8.963 28.812 1.00 47.92 C ATOM 5036 C LYS E 310 83.957 −9.383 27.596 1.00 46.18 C ATOM 5037 O LYS E 310 82.791 −9.760 27.733 1.00 45.41 O ATOM 5038 CB LYS E 310 84.934 −10.151 29.766 1.00 47.80 C ATOM 5039 N VAL E 311 84.561 −9.321 26.412 1.00 44.53 N ATOM 5040 CA VAL E 311 83.864 −9.690 25.178 1.00 42.94 C ATOM 5041 C VAL E 311 83.812 −11.197 24.979 1.00 42.70 C ATOM 5042 O VAL E 311 84.837 −11.841 24.753 1.00 43.13 O ATOM 5043 CB VAL E 311 84.539 −9.071 23.934 1.00 42.45 C ATOM 5044 CG1 VAL E 311 83.833 −9.550 22.661 1.00 40.98 C ATOM 5045 CG2 VAL E 311 84.511 −7.557 24.029 1.00 41.52 C ATOM 5046 N LEU E 312 82.609 −11.753 25.041 1.00 41.79 N ATOM 5047 CA LEU E 312 82.418 −13.188 24.869 1.00 40.92 C ATOM 5048 C LEU E 312 82.405 −13.596 23.405 1.00 40.03 C ATOM 5049 O LEU E 312 82.932 −14.643 23.040 1.00 40.10 O ATOM 5050 CB LEU E 312 81.102 −13.625 25.519 1.00 42.05 C ATOM 5051 CG LEU E 312 80.890 −13.141 26.956 1.00 43.75 C ATOM 5052 CD1 LEU E 312 79.784 −13.962 27.606 1.00 42.68 C ATOM 5053 CD2 LEU E 312 82.187 −13.289 27.748 1.00 44.25 C ATOM 5054 N LYS E 313 81.771 −12.785 22.569 1.00 38.60 N ATOM 5055 CA LYS E 313 81.715 −13.069 21.146 1.00 37.54 C ATOM 5056 C LYS E 313 81.341 −11.805 20.395 1.00 36.63 C ATOM 5057 O LYS E 313 80.612 −10.952 20.910 1.00 36.09 O ATOM 5058 CB LYS E 313 80.741 −14.216 20.832 1.00 38.37 C ATOM 5059 CG LYS E 313 79.283 −13.881 20.927 1.00 40.25 C ATOM 5060 CD LYS E 313 78.434 −15.110 20.642 1.00 41.30 C ATOM 5061 CE LYS E 313 78.667 −15.657 19.245 1.00 42.13 C ATOM 5062 NZ LYS E 313 77.712 −16.764 18.931 1.00 43.04 N ATOM 5063 N ALA E 314 81.871 −11.679 19.181 1.00 34.76 N ATOM 5064 CA ALA E 314 81.633 −10.501 18.362 1.00 33.57 C ATOM 5065 C ALA E 314 81.531 −10.845 16.883 1.00 33.42 C ATOM 5066 O ALA E 314 82.287 −11.684 16.371 1.00 33.25 O ATOM 5067 CB ALA E 314 82.744 −9.494 18.588 1.00 33.65 C ATOM 5068 N ALA E 315 80.595 −10.185 16.201 1.00 32.14 N ATOM 5069 CA ALA E 315 80.353 −10.398 14.780 1.00 31.01 C ATOM 5070 C ALA E 315 81.549 −10.035 13.903 1.00 30.72 C ATOM 5071 O ALA E 315 82.361 −9.177 14.257 1.00 30.48 O ATOM 5072 CB ALA E 315 79.121 −9.607 14.335 1.00 30.66 C ATOM 5073 N GLY E 316 81.631 −10.694 12.751 1.00 30.24 N ATOM 5074 CA GLY E 316 82.708 −10.456 11.816 1.00 31.94 C ATOM 5075 C GLY E 316 82.770 −11.540 10.755 1.00 33.59 C ATOM 5076 O GLY E 316 81.899 −12.405 10.683 1.00 32.55 O ATOM 5077 N VAL E 317 83.802 −11.479 9.925 1.00 35.48 N ATOM 5078 CA VAL E 317 84.013 −12.449 8.860 1.00 38.38 C ATOM 5079 C VAL E 317 84.061 −13.890 9.384 1.00 39.34 C ATOM 5080 O VAL E 317 83.570 −14.810 8.732 1.00 39.08 O ATOM 5081 CB VAL E 317 85.339 −12.140 8.121 1.00 39.18 C ATOM 5082 CG1 VAL E 317 85.814 −13.363 7.350 1.00 41.23 C ATOM 5083 CG2 VAL E 317 85.133 −10.970 7.157 1.00 39.65 C ATOM 5084 N ASN E 318 84.649 −14.073 10.563 1.00 41.02 N ATOM 5085 CA ASN E 318 84.772 −15.397 11.165 1.00 42.81 C ATOM 5086 C ASN E 318 83.640 −15.765 12.112 1.00 43.44 C ATOM 5087 O ASN E 318 83.595 −16.879 12.635 1.00 43.81 O ATOM 5088 CB ASN E 318 86.113 −15.511 11.885 1.00 43.79 C ATOM 5089 CG ASN E 318 87.251 −15.783 10.928 1.00 44.65 C ATOM 5090 OD1 ASN E 318 88.377 −15.342 11.140 1.00 46.43 O ATOM 5091 ND2 ASN E 318 86.961 −16.526 9.863 1.00 45.45 N ATOM 5092 N THR E 319 82.728 −14.825 12.336 1.00 43.23 N ATOM 5093 CA THR E 319 81.585 −15.058 13.207 1.00 42.64 C ATOM 5094 C THR E 319 80.401 −14.304 12.607 1.00 42.30 C ATOM 5095 O THR E 319 80.025 −13.224 13.070 1.00 41.73 O ATOM 5096 CB THR E 319 81.845 −14.542 14.629 1.00 42.95 C ATOM 5097 OG1 THR E 319 83.161 −14.923 15.053 1.00 43.57 O ATOM 5098 CG2 THR E 319 80.829 −15.132 15.583 1.00 42.54 C ATOM 5099 N THR E 320 79.841 −14.898 11.561 1.00 41.32 N ATOM 5100 CA THR E 320 78.713 −14.381 10.791 1.00 41.14 C ATOM 5101 C THR E 320 77.460 −13.982 11.580 1.00 40.79 C ATOM 5102 O THR E 320 77.228 −14.481 12.679 1.00 40.11 O ATOM 5103 CB THR E 320 78.327 −15.445 9.717 1.00 40.88 C ATOM 5104 OG1 THR E 320 79.269 −15.385 8.642 1.00 41.69 O ATOM 5105 CG2 THR E 320 76.926 −15.235 9.186 1.00 41.14 C ATOM 5106 N ASP E 321 76.652 −13.091 10.995 1.00 40.17 N ATOM 5107 CA ASP E 321 75.402 −12.634 11.608 1.00 40.26 C ATOM 5108 C ASP E 321 74.370 −13.760 11.740 1.00 40.48 C ATOM 5109 O ASP E 321 73.453 −13.671 12.551 1.00 40.99 O ATOM 5110 CB ASP E 321 74.761 −11.492 10.785 1.00 40.57 C ATOM 5111 CG ASP E 321 75.508 −10.164 10.911 1.00 40.77 C ATOM 5112 CD1 ASP E 321 76.166 −9.942 11.943 1.00 41.36 O ATOM 5113 OD2 ASP E 321 75.421 −9.334 9.980 1.00 40.77 O ATOM 5114 N LYS E 322 74.513 −14.812 10.941 1.00 40.71 N ATOM 5115 CA LYS E 322 73.561 −15.922 10.970 1.00 40.47 C ATOM 5116 C LYS E 322 73.340 −16.497 12.366 1.00 40.34 C ATOM 5117 O LYS E 322 72.213 −16.817 12.739 1.00 40.39 O ATOM 5118 CB LYS E 322 74.014 −17.038 10.024 1.00 40.54 C ATOM 5119 N GLU E 323 74.410 −16.605 13.146 1.00 39.99 N ATOM 5120 CA GLU E 323 74.304 −17.172 14.486 1.00 40.42 C ATOM 5121 C GLU E 323 74.793 −16.255 15.616 1.00 40.12 C ATOM 5122 O GLU E 323 74.975 −16.705 16.752 1.00 40.19 O ATOM 5123 CB GLU E 323 75.079 −18.497 14.539 1.00 41.39 C ATOM 5124 N ILE E 324 74.980 −14.974 15.315 1.00 39.32 N ATOM 5125 CA ILE E 324 75.472 −14.016 16.304 1.00 38.63 C ATOM 5126 C ILE E 324 74.426 −13.586 17.349 1.00 37.71 C ATOM 5127 O ILE E 324 74.780 −13.190 18.455 1.00 36.93 O ATOM 5128 CB ILE E 324 76.038 −12.750 15.577 1.00 39.58 C ATOM 5129 CG1 ILE E 324 77.275 −12.216 16.305 1.00 40.68 C ATOM 5130 CG2 ILE E 324 74.959 −11.683 15.445 1.00 38.88 C ATOM 5131 CD1 ILE E 324 77.023 −11.669 17.672 1.00 42.53 C ATOM 5132 N GLU E 325 73.144 −13.681 17.010 1.00 37.22 N ATOM 5133 CA GLU E 325 72.085 −13.264 17.932 1.00 38.65 C ATOM 5134 C GLU E 325 71.729 −14.213 19.085 1.00 39.26 C ATOM 5135 O GLU E 325 70.838 −13.921 19.883 1.00 38.60 O ATOM 5136 CB GLU E 325 70.816 −12.907 17.138 1.00 38.87 C ATOM 5137 CG GLU E 325 70.909 −11.561 16.393 1.00 40.03 C ATOM 5138 CD GLU E 325 69.746 −11.319 15.432 1.00 41.78 C ATOM 5139 OE1 GLU E 325 69.663 −12.037 14.413 1.00 42.23 O ATOM 5140 OE2 GLU E 325 68.913 −10.415 15.693 1.00 42.02 O ATOM 5141 N VAL E 326 72.414 −15.347 19.182 1.00 40.15 N ATOM 5142 CA VAL E 326 72.149 −16.281 20.270 1.00 41.03 C ATOM 5143 C VAL E 326 73.467 −16.648 20.937 1.00 41.51 C ATOM 5144 O VAL E 326 74.438 −16.974 20.264 1.00 41.62 O ATOM 5145 CB VAL E 326 71.456 −17.559 19.763 1.00 41.93 C ATOM 5146 CG1 VAL E 326 71.125 −18.469 20.942 1.00 42.60 C ATOM 5147 CG2 VAL E 326 70.193 −17.195 19.007 1.00 41.45 C ATOM 5148 N LEU E 327 73.502 −16.565 22.261 1.00 42.31 N ATOM 5149 CA LEU E 327 74.705 −16.881 23.024 1.00 43.48 C ATOM 5150 C LEU E 327 74.463 −18.120 23.880 1.00 44.60 C ATOM 5151 O LEU E 327 73.572 −18.122 24.732 1.00 44.30 O ATOM 5152 CB LEU E 327 75.064 −15.709 23.936 1.00 43.12 C ATOM 5153 CG LEU E 327 76.273 −15.926 24.848 1.00 43.38 C ATOM 5154 CD1 LEU E 327 77.547 −15.913 24.007 1.00 43.75 C ATOM 5155 CD2 LEU E 327 76.331 −14.839 25.913 1.00 42.65 C ATOM 5156 N TYR E 328 75.264 −19.161 23.662 1.00 45.83 N ATOM 5157 CA TYR E 328 75.130 −20.409 24.409 1.00 47.51 C ATOM 5158 C TYR E 328 76.203 −20.539 25.480 1.00 48.60 C ATOM 5159 O TYR E 328 77.367 −20.219 25.239 1.00 49.02 O ATOM 5160 CB TYR E 328 75.230 −21.604 23.465 1.00 48.05 C ATOM 5161 CG TYR E 328 74.175 −21.633 22.389 1.00 49.56 C ATOM 5162 CD1 TYR E 328 74.428 −21.111 21.118 1.00 50.39 C ATOM 5163 CD2 TYR E 328 72.916 −22.174 22.641 1.00 50.10 C ATOM 5164 CE1 TYR E 328 73.451 −21.132 20.121 1.00 50.75 C ATOM 5165 CE2 TYR E 328 71.930 −22.199 21.654 1.00 50.95 C ATOM 5166 CZ TYR E 328 72.205 −21.679 20.397 1.00 51.33 C ATOM 5167 OH TYR E 328 71.234 −21.720 19.416 1.00 52.19 O ATOM 5168 N ILE E 329 75.808 −21.025 26.653 1.00 50.10 N ATOM 5169 CA ILE E 329 76.719 −21.217 27.784 1.00 51.70 C ATOM 5170 C ILE E 329 76.424 −22.593 28.398 1.00 53.13 C ATOM 5171 O ILE E 329 75.392 −22.759 29.053 1.00 53.28 O ATOM 5172 CB ILE E 329 76.466 −20.124 28.857 1.00 51.99 C ATOM 5173 CG1 ILE E 329 76.483 −18.739 28.201 1.00 52.28 C ATOM 5174 CG2 ILE E 329 77.518 −20.203 29.953 1.00 52.51 C ATOM 5175 CD1 ILE E 329 76.166 −17.593 29.145 1.00 52.93 C ATOM 5176 N ARG E 330 77.320 −23.566 28.198 1.00 54.31 N ATOM 5177 CA ARG E 330 77.128 −24.929 28.713 1.00 54.98 C ATOM 5178 C ARG E 330 77.949 −25.259 29.959 1.00 55.26 C ATOM 5179 O ARG E 330 79.005 −24.666 30.184 1.00 55.44 O ATOM 5180 CB ARG E 330 77.465 −25.940 27.612 1.00 54.90 C ATOM 5181 N ASN E 331 77.461 −26.212 30.755 1.00 55.70 N ATOM 5182 CA ASN E 331 78.154 −26.636 31.970 1.00 56.20 C ATOM 5183 C ASN E 331 78.593 −25.414 32.768 1.00 56.64 C ATOM 5184 O ASN E 331 79.781 −25.231 33.039 1.00 56.90 O ATOM 5185 CB ASN E 331 79.383 −27.480 31.603 1.00 55.73 C ATOM 5186 N VAL E 332 77.627 −24.583 33.147 1.00 57.11 N ATOM 5187 CA VAL E 332 77.916 −23.357 33.884 1.00 57.24 C ATOM 5188 C VAL E 332 78.510 −23.565 35.271 1.00 57.22 C ATOM 5189 O VAL E 332 78.233 −24.556 35.940 1.00 57.43 O ATOM 5190 CB VAL E 332 76.647 −22.487 34.031 1.00 57.41 C ATOM 5191 N THR E 333 79.334 −22.612 35.688 1.00 57.10 N ATOM 5192 CA THR E 333 79.963 −22.634 37.001 1.00 57.30 C ATOM 5193 C THR E 333 79.383 −21.436 37.746 1.00 57.39 C ATOM 5194 O THR E 333 78.661 −20.632 37.155 1.00 57.78 O ATOM 5195 CB THR E 333 81.493 −22.459 36.901 1.00 57.30 C ATOM 5196 N PHE E 334 79.684 −21.309 39.033 1.00 57.05 N ATOM 5197 CA PHE E 334 79.170 −20.175 39.796 1.00 56.67 C ATOM 5198 C PHE E 334 79.828 −18.894 39.280 1.00 55.98 C ATOM 5199 O PHE E 334 79.302 −17.794 39.455 1.00 55.93 O ATOM 5200 CB PHE E 334 79.456 −20.357 41.292 1.00 57.08 C ATOM 5201 N GLU E 335 80.977 −19.052 38.633 1.00 54.82 N ATOM 5202 CA GLU E 335 81.707 −17.917 38.087 1.00 54.10 C ATOM 5203 C GLU E 335 80.959 −17.274 36.911 1.00 53.27 C ATOM 5204 O GLU E 335 81.119 −16.082 36.642 1.00 52.91 O ATOM 5205 CB GLU E 335 83.102 −18.368 37.634 1.00 54.01 C ATOM 5206 N ASP E 336 80.140 −18.060 36.217 1.00 52.36 N ATOM 5207 CA ASP E 336 79.394 −17.540 35.074 1.00 51.65 C ATOM 5208 C ASP E 336 78.263 −16.596 35.459 1.00 50.65 C ATOM 5209 O ASP E 336 77.808 −15.814 34.632 1.00 50.46 O ATOM 5210 CB ASP E 336 78.829 −18.678 34.221 1.00 51.50 C ATOM 5211 CG ASP E 336 79.914 −19.483 33.546 1.00 51.96 C ATOM 5212 OD1 ASP E 336 80.862 −18.865 33.010 1.00 50.96 O ATOM 5213 OD2 ASP E 336 79.817 −20.728 33.549 1.00 51.31 O ATOM 5214 N ALA E 337 77.808 −16.671 36.704 1.00 49.76 N ATOM 5215 CA ALA E 337 76.731 −15.803 37.167 1.00 49.26 C ATOM 5216 C ALA E 337 77.085 −14.351 36.894 1.00 49.07 C ATOM 5217 O ALA E 337 78.259 −13.976 36.914 1.00 49.31 O ATOM 5218 CB ALA E 337 76.496 −16.005 38.658 1.00 49.40 C ATOM 5219 N GLY E 338 76.072 −13.529 36.636 1.00 48.46 N ATOM 5220 CA GLY E 338 76.341 −12.127 36.366 1.00 47.35 C ATOM 5221 C GLY E 338 75.481 −11.508 35.280 1.00 46.17 C ATOM 5222 O GLY E 338 74.546 −12.134 34.772 1.00 45.24 O ATOM 5223 N GLU E 339 75.818 −10.270 34.924 1.00 44.77 N ATOM 5224 CA GLU E 339 75.089 −9.513 33.916 1.00 44.35 C ATOM 5225 C GLU E 339 75.652 −9.701 32.496 1.00 42.94 C ATOM 5226 O GLU E 339 76.840 −9.459 32.249 1.00 41.99 O ATOM 5227 CB GLU E 339 75.121 −8.028 34.296 1.00 44.65 C ATOM 5228 CG GLU E 339 74.100 −7.163 33.591 1.00 46.70 C ATOM 5229 CD GLU E 339 74.220 −5.708 33.992 1.00 47.49 C ATOM 5230 OE1 GLU E 339 74.666 −5.448 35.127 1.00 48.94 O ATOM 5231 OE2 GLU E 339 73.862 −4.823 33.186 1.00 48.65 O ATOM 5232 N TYR E 340 74.790 −10.145 31.579 1.00 41.66 N ATOM 5233 CA TYR E 340 75.160 −10.339 30.172 1.00 40.54 C ATOM 5234 C TYR E 340 74.485 −9.267 29.314 1.00 39.53 C ATOM 5235 O TYR E 340 73.307 −8.955 29.504 1.00 39.67 O ATOM 5236 CB TYR E 340 74.754 −11.736 29.687 1.00 40.75 C ATOM 5237 CG TYR E 340 75.595 −12.833 30.302 1.00 43.00 C ATOM 5238 CD1 TYR E 340 75.423 −13.199 31.637 1.00 43.39 C ATOM 5239 CD2 TYR E 340 76.624 −13.446 29.576 1.00 42.97 C ATOM 5240 CE1 TYR E 340 76.260 −14.144 32.246 1.00 43.85 C ATOM 5241 CE2 TYR E 340 77.465 −14.391 30.172 1.00 44.16 C ATOM 5242 CZ TYR E 340 77.279 −14.732 31.513 1.00 44.42 C ATOM 5243 OH TYR E 340 78.124 −15.631 32.126 1.00 43.97 O ATOM 5244 N THR E 341 75.225 −8.718 28.356 1.00 37.76 N ATOM 5245 CA THR E 341 74.692 −7.661 27.514 1.00 36.11 C ATOM 5246 C THR E 341 74.844 −7.882 26.013 1.00 35.29 C ATOM 5247 O THR E 341 75.913 −8.245 25.535 1.00 35.15 O ATOM 5248 CB THR E 341 75.384 −6.311 27.837 1.00 35.87 C ATOM 5249 OG1 THR E 341 75.114 −5.936 29.192 1.00 36.17 O ATOM 5250 CG2 THR E 341 74.901 −5.219 26.902 1.00 35.45 C ATOM 5251 N CYS E 342 73.765 −7.667 25.273 1.00 34.30 N ATOM 5252 CA CYS E 342 73.838 −7.755 23.820 1.00 33.50 C ATOM 5253 C CYS E 342 73.962 −6.303 23.397 1.00 32.08 C ATOM 5254 O CYS E 342 73.088 −5.491 23.685 1.00 31.94 O ATOM 5255 CB CYS E 342 72.577 −8.347 23.201 1.00 33.31 C ATOM 5256 SG CYS E 342 72.527 −8.113 21.399 1.00 35.61 S ATOM 5257 N LEU E 343 75.056 −5.977 22.724 1.00 31.56 N ATOM 5258 CA LEU E 343 75.292 −4.610 22.278 1.00 30.17 C ATOM 5259 C LEU E 343 75.366 −4.522 20.758 1.00 29.58 C ATOM 5260 O LEU E 343 76.132 −5.245 20.121 1.00 29.15 O ATOM 5261 CB LEU E 343 76.581 −4.080 22.913 1.00 29.36 C ATOM 5262 CG LEU E 343 76.957 −2.619 22.680 1.00 28.90 C ATOM 5263 CD1 LEU E 343 77.509 −2.017 23.964 1.00 29.70 C ATOM 5264 CD2 LEU E 343 77.972 −2.529 21.551 1.00 29.96 C ATOM 5265 N ALA E 344 74.552 −3.633 20.189 1.00 28.85 N ATOM 5266 CA ALA E 344 74.505 −3.430 18.751 1.00 28.63 C ATOM 5267 C ALA E 344 74.810 −1.983 18.371 1.00 28.87 C ATOM 5268 O ALA E 344 74.230 −1.039 18.915 1.00 29.04 O ATOM 5269 CB ALA E 344 73.138 −3.837 18.206 1.00 28.59 C ATOM 5270 N GLY E 345 75.725 −1.806 17.425 1.00 28.49 N ATOM 5271 CA GLY E 345 76.060 −0.465 16.998 1.00 27.62 C ATOM 5272 C GLY E 345 76.246 −0.322 15.499 1.00 27.14 C ATOM 5273 O GLY E 345 76.625 −1.281 14.821 1.00 25.46 O ATOM 5274 N ASN E 346 75.922 0.869 14.986 1.00 26.69 N ATOM 5275 CA ASN E 346 76.132 1.217 13.579 1.00 27.69 C ATOM 5276 C ASN E 346 76.744 2.621 13.563 1.00 28.33 C ATOM 5277 O ASN E 346 77.004 3.190 14.623 1.00 27.30 O ATOM 5278 CB ASN E 346 74.836 1.164 12.736 1.00 27.21 C ATOM 5279 CG ASN E 346 73.761 2.145 13.206 1.00 27.40 C ATOM 5280 OD1 ASN E 346 74.058 3.212 13.742 1.00 26.31 O ATOM 5281 ND2 ASN E 346 72.497 1.787 12.974 1.00 24.84 N ATOM 5282 N SER E 347 76.985 3.178 12.378 1.00 31.00 N ATOM 5283 CA SER E 347 77.602 4.505 12.281 1.00 33.49 C ATOM 5284 C SER E 347 76.856 5.605 13.024 1.00 34.58 C ATOM 5285 O SER E 347 77.469 6.572 13.463 1.00 34.82 O ATOM 5286 CB SER E 347 77.772 4.942 10.816 1.00 35.65 C ATOM 5287 OG SER E 347 76.530 5.254 10.203 1.00 38.30 O ATOM 5288 N ILE E 348 75.541 5.466 13.168 1.00 34.99 N ATOM 5289 CA ILE E 348 74.751 6.483 13.864 1.00 35.50 C ATOM 5290 C ILE E 348 74.840 6.414 15.387 1.00 35.19 C ATOM 5291 O ILE E 348 74.938 7.444 16.048 1.00 36.08 O ATOM 5292 CB ILE E 348 73.265 6.399 13.462 1.00 36.91 C ATOM 5293 CG1 ILE E 348 73.135 6.618 11.955 1.00 37.03 C ATOM 5294 CG2 ILE E 348 72.451 7.433 14.235 1.00 37.40 C ATOM 5295 CD1 ILE E 348 71.779 6.275 11.412 1.00 39.10 C ATOM 5296 N GLY E 349 74.800 5.209 15.945 1.00 34.48 N ATOM 5297 CA GLY E 349 74.871 5.074 17.388 1.00 33.86 C ATOM 5298 C GLY E 349 74.870 3.648 17.923 1.00 33.75 C ATOM 5299 O GLY E 349 74.922 2.681 17.165 1.00 33.05 O ATOM 5300 N ILE E 350 74.789 3.532 19.247 1.00 33.83 N ATOM 5301 CA ILE E 350 74.804 2.248 19.935 1.00 33.98 C ATOM 5302 C ILE E 350 73.567 1.992 20.808 1.00 34.07 C ATOM 5303 O ILE E 350 73.010 2.912 21.408 1.00 34.17 O ATOM 5304 CB ILE E 350 76.056 2.133 20.838 1.00 33.87 C ATOM 5305 CG1 ILE E 350 77.320 2.329 20.004 1.00 34.32 C ATOM 5306 CG2 ILE E 350 76.088 0.779 21.531 1.00 35.06 C ATOM 5307 CD1 ILE E 350 78.577 2.477 20.839 1.00 35.18 C ATOM 5308 N SER E 351 73.153 0.729 20.864 1.00 33.25 N ATOM 5309 CA SER E 351 72.019 0.296 21.682 1.00 33.20 C ATOM 5310 C SER E 351 72.410 −1.014 22.363 1.00 32.62 C ATOM 5311 O SER E 351 73.214 −1.775 21.821 1.00 32.18 O ATOM 5312 CB SER E 351 70.778 0.064 20.817 1.00 34.11 C ATOM 5313 OG SER E 351 70.292 1.276 20.274 1.00 37.01 O ATOM 5314 N PHE E 352 71.858 −1.275 23.544 1.00 32.40 N ATOM 5315 CA PHE E 352 72.163 −2.513 24.260 1.00 33.36 C ATOM 5316 C PHE E 352 71.119 −2.886 25.311 1.00 33.02 C ATOM 5317 O PHE E 352 70.558 −2.018 25.977 1.00 33.29 O ATOM 5318 CB PHE E 352 73.558 −2.413 24.913 1.00 34.47 C ATOM 5319 CG PHE E 352 73.690 −1.297 25.921 1.00 36.24 C ATOM 5320 CD1 PHE E 352 73.218 −1.450 27.225 1.00 37.18 C ATOM 5321 CD2 PHE E 352 74.281 −0.091 25.564 1.00 36.74 C ATOM 5322 CE1 PHE E 352 73.335 −0.413 28.160 1.00 38.09 C ATOM 5323 CE2 PHE E 352 74.403 0.948 26.484 1.00 38.13 C ATOM 5324 CZ PHE E 352 73.929 0.788 27.785 1.00 38.23 C ATOM 5325 N HIS E 353 70.856 −4.182 25.443 1.00 33.31 N ATOM 5326 CA HIS E 353 69.904 −4.687 26.438 1.00 34.40 C ATOM 5327 C HIS E 353 70.655 −5.730 27.274 1.00 35.40 C ATOM 5328 O HIS E 353 71.478 −6.484 26.741 1.00 35.06 O ATOM 5329 CB HIS E 353 68.670 −5.332 25.777 1.00 33.36 C ATOM 5330 CG HIS E 353 67.700 −4.351 25.187 1.00 33.71 C ATOM 5331 ND1 HIS E 353 66.500 −4.735 24.622 1.00 33.31 N ATOM 5332 CD2 HIS E 353 67.745 −2.999 25.075 1.00 32.51 C ATOM 5333 CE1 HIS E 353 65.851 −3.668 24.192 1.00 31.00 C ATOM 5334 NE2 HIS E 353 66.586 −2.603 24.455 1.00 31.60 N ATOM 5335 N SER E 354 70.374 −5.766 28.576 1.00 36.20 N ATOM 5336 CA SER E 354 71.045 −6.698 29.479 1.00 37.46 C ATOM 5337 C SER E 354 70.112 −7.646 30.221 1.00 38.17 C ATOM 5338 O SER E 354 68.928 −7.364 30.425 1.00 37.52 O ATOM 5339 CB SER E 354 71.873 −5.928 30.507 1.00 37.67 C ATOM 5340 OG SER E 354 72.763 −5.031 29.869 1.00 40.40 O ATOM 5341 N ALA E 355 70.670 −8.779 30.631 1.00 39.18 N ATOM 5342 CA ALA E 355 69.919 −9.779 31.375 1.00 40.68 C ATOM 5343 C ALA E 355 70.850 −10.349 32.437 1.00 41.59 C ATOM 5344 O ALA E 355 72.072 −10.179 32.359 1.00 42.09 O ATOM 5345 CB ALA E 355 69.428 −10.886 30.438 1.00 40.51 C ATOM 5346 N TRP E 356 70.273 −11.023 33.425 1.00 42.87 N ATOM 5347 CA TRP E 356 71.055 −11.597 34.508 1.00 44.67 C ATOM 5348 C TRP E 356 71.021 −13.119 34.519 1.00 44.89 C ATOM 5349 O TRP E 356 69.995 −13.734 34.237 1.00 44.45 O ATOM 5350 CB TRP E 356 70.542 −11.068 35.856 1.00 46.66 C ATOM 5351 CG TRP E 356 71.644 −10.589 36.745 1.00 48.84 C ATOM 5352 CD1 TRP E 356 72.536 −11.360 37.436 1.00 49.57 C ATOM 5353 CD2 TRP E 356 72.051 −9.229 36.940 1.00 49.66 C ATOM 5354 NE1 TRP E 356 73.483 −10.563 38.041 1.00 50.48 N ATOM 5355 CE2 TRP E 356 73.209 −9.251 37.752 1.00 50.21 C ATOM 5356 CE3 TRP E 356 71.551 −7.992 36.501 1.00 50.27 C ATOM 5357 CZ2 TRP E 356 73.883 −8.080 38.137 1.00 50.52 C ATOM 5358 CZ3 TRP E 356 72.221 −6.824 36.883 1.00 50.86 C ATOM 5359 CH2 TRP E 356 73.375 −6.881 37.693 1.00 50.85 C ATOM 5360 N LEU E 357 72.163 −13.719 34.835 1.00 45.24 N ATOM 5361 CA LEU E 357 72.275 −15.165 34.929 1.00 46.28 C ATOM 5362 C LEU E 357 72.416 −15.529 36.404 1.00 47.03 C ATOM 5363 O LEU E 357 73.362 −15.085 37.064 1.00 47.09 O ATOM 5364 CB LEU E 357 73.516 −15.662 34.180 1.00 46.24 C ATOM 5365 CG LEU E 357 73.855 −17.138 34.418 1.00 46.22 C ATOM 5366 CD1 LEU E 357 72.722 −18.004 33.879 1.00 45.74 C ATOM 5367 CD2 LEU E 357 75.184 −17.493 33.742 1.00 45.83 C ATOM 5368 N THR E 358 71.481 −16.323 36.920 1.00 47.80 N ATOM 5369 CA THR E 358 71.525 −16.754 38.317 1.00 49.40 C ATOM 5370 C THR E 358 71.935 −18.221 38.360 1.00 49.88 C ATOM 5371 O THR E 358 71.300 −19.067 37.725 1.00 49.63 O ATOM 5372 CB THR E 358 70.144 −16.626 39.010 1.00 50.27 C ATOM 5373 OG1 THR E 358 69.709 −15.263 38.980 1.00 51.35 O ATOM 5374 CG2 THR E 358 70.231 −17.083 40.466 1.00 51.00 C ATOM 5375 N VAL E 359 72.995 −18.515 39.108 1.00 50.99 N ATOM 5376 CA VAL E 359 73.496 −19.878 39.239 1.00 52.26 C ATOM 5377 C VAL E 359 73.291 −20.372 40.671 1.00 53.50 C ATOM 5378 O VAL E 359 73.879 −19.828 41.617 1.00 53.34 O ATOM 5379 CB VAL E 359 75.001 −19.954 38.883 1.00 52.03 C ATOM 5380 N LEU E 360 72.454 −21.405 40.806 1.00 54.72 N ATOM 5381 CA LEU E 360 72.118 −22.014 42.095 1.00 55.76 C ATOM 5382 C LEU E 360 73.006 −23.217 42.403 1.00 56.27 C ATOM 5383 O LEU E 360 73.018 −24.147 41.566 1.00 56.89 O ATOM 5384 CB LEU E 360 70.650 −22.456 42.095 1.00 55.94 C TER 5385 LEU E 360 ATOM 5386 N ASN F 150 27.465 32.706 43.234 1.00 47.18 N ATOM 5387 CA ASN F 150 26.839 33.873 43.929 1.00 46.68 C ATOM 5388 C ASN F 150 25.823 34.566 43.015 1.00 45.81 C ATOM 5389 O ASN F 150 25.993 34.593 41.797 1.00 46.29 O ATOM 5390 CB ASN F 150 27.924 34.872 44.357 1.00 46.26 C ATOM 5391 N LYS F 151 24.769 35.116 43.612 1.00 45.07 N ATOM 5392 CA LYS F 151 23.717 35.815 42.874 1.00 43.78 C ATOM 5393 C LYS F 151 24.148 37.251 42.548 1.00 43.34 C ATOM 5394 O LYS F 151 24.545 38.007 43.432 1.00 42.87 O ATOM 5395 CB LYS F 151 22.421 35.835 43.695 1.00 43.03 C ATOM 5396 N ARG F 152 24.073 37.627 41.274 1.00 42.12 N ATOM 5397 CA ARG F 152 24.472 38.973 40.878 1.00 40.51 C ATOM 5398 C ARG F 152 23.794 39.481 39.608 1.00 39.03 C ATOM 5399 O ARG F 152 23.353 38.706 38.754 1.00 38.69 O ATOM 5400 CB ARG F 152 25.988 39.035 40.701 1.00 40.57 C ATOM 5401 CG ARG F 152 26.528 38.034 39.696 1.00 41.38 C ATOM 5402 CD ARG F 152 28.045 38.053 39.645 1.00 40.83 C ATOM 5403 NE ARG F 152 28.574 39.325 39.162 1.00 40.31 N ATOM 5404 CZ ARG F 152 29.816 39.487 38.712 1.00 40.01 C ATOM 5405 NH1 ARG F 152 30.657 38.461 38.693 1.00 39.33 N ATOM 5406 NH2 ARG F 152 30.211 40.665 38.250 1.00 40.37 N ATOM 5407 N ALA F 153 23.725 40.802 39.503 1.00 37.59 N ATOM 5408 CA ALA F 153 23.127 41.470 38.361 1.00 36.00 C ATOM 5409 C ALA F 153 23.905 41.142 37.085 1.00 34.93 C ATOM 5410 O ALA F 153 25.018 40.633 37.139 1.00 34.72 O ATOM 5411 CB ALA F 153 23.105 42.987 38.604 1.00 35.68 C ATOM 5412 N PRO F 154 23.322 41.436 35.916 1.00 34.45 N ATOM 5413 CA PRO F 154 23.987 41.158 34.640 1.00 33.61 C ATOM 5414 C PRO F 154 25.229 42.013 34.427 1.00 33.12 C ATOM 5415 O PRO F 154 25.312 43.137 34.922 1.00 32.79 O ATOM 5416 CB PRO F 154 22.894 41.447 33.624 1.00 33.95 C ATOM 5417 CG PRO F 154 22.131 42.546 34.284 1.00 34.26 C ATOM 5418 CD PRO F 154 22.018 42.086 35.698 1.00 33.81 C ATOM 5419 N TYR F 155 26.194 41.465 33.697 1.00 33.26 N ATOM 5420 CA TYR F 155 27.432 42.171 33.406 1.00 34.23 C ATOM 5421 C TYR F 155 28.054 41.642 32.109 1.00 34.53 C ATOM 5422 O TYR F 155 27.912 40.466 31.786 1.00 34.70 O ATOM 5423 CB TYR F 155 28.416 42.010 34.571 1.00 35.21 C ATOM 5424 CG TYR F 155 28.879 40.587 34.807 1.00 36.38 C ATOM 5425 CD1 TYR F 155 28.033 39.637 35.387 1.00 37.46 C ATOM 5426 CD2 TYR F 155 30.153 40.183 34.422 1.00 36.66 C ATOM 5427 CE1 TYR F 155 28.450 38.317 35.573 1.00 37.51 C ATOM 5428 CE2 TYR F 155 30.579 38.871 34.602 1.00 37.68 C ATOM 5429 CZ TYR F 155 29.725 37.944 35.172 1.00 38.34 C ATOM 5430 OH TYR F 155 30.150 36.637 35.313 1.00 39.80 O ATOM 5431 N TRP F 156 28.731 42.519 31.373 1.00 34.56 N ATOM 5432 CA TRP F 156 29.385 42.141 30.123 1.00 36.40 C ATOM 5433 C TRP F 156 30.610 41.270 30.415 1.00 38.32 C ATOM 5434 O TRP F 156 31.454 41.648 31.229 1.00 39.35 O ATOM 5435 CB TRP F 156 29.828 43.402 29.369 1.00 34.91 C ATOM 5436 CG TRP F 156 28.743 44.408 29.136 1.00 33.24 C ATOM 5437 CD1 TRP F 156 28.809 45.743 29.385 1.00 32.54 C ATOM 5438 CD2 TRP F 156 27.434 44.162 28.598 1.00 32.50 C ATOM 5439 NE1 TRP F 156 27.630 46.352 29.041 1.00 31.97 N ATOM 5440 CE2 TRP F 156 26.764 45.409 28.553 1.00 32.15 C ATOM 5441 CE3 TRP F 156 26.761 43.011 28.147 1.00 31.76 C ATOM 5442 CZ2 TRP F 156 25.447 45.544 28.079 1.00 31.23 C ATOM 5443 CZ3 TRP F 156 25.445 43.143 27.670 1.00 31.94 C ATOM 5444 CH2 TRP F 156 24.806 44.404 27.642 1.00 31.30 C ATOM 5445 N THR F 157 30.710 40.121 29.748 1.00 40.38 N ATOM 5446 CA THR F 157 31.826 39.198 29.952 1.00 42.48 C ATOM 5447 C THR F 157 32.970 39.388 28.967 1.00 43.74 C ATOM 5448 O THR F 157 33.988 38.708 29.059 1.00 44.97 O ATOM 5449 CB THR F 157 31.353 37.738 29.878 1.00 43.02 C ATOM 5450 OG1 THR F 157 30.716 37.495 28.613 1.00 43.13 O ATOM 5451 CG2 THR F 157 30.371 37.453 31.004 1.00 43.29 C ATOM 5452 N ASN F 158 32.808 40.306 28.022 1.00 45.46 N ATOM 5453 CA ASN F 158 33.862 40.578 27.046 1.00 46.50 C ATOM 5454 C ASN F 158 33.649 41.918 26.355 1.00 46.39 C ATOM 5455 O ASN F 158 33.122 41.974 25.246 1.00 46.75 O ATOM 5456 CB ASN F 158 33.936 39.472 25.988 1.00 48.38 C ATOM 5457 CG ASN F 158 35.162 39.613 25.080 1.00 50.17 C ATOM 5458 OD1 ASN F 158 35.297 40.586 24.326 1.00 50.24 O ATOM 5459 ND2 ASN F 158 36.063 38.640 25.158 1.00 50.64 N ATOM 5460 N THR F 159 34.075 42.992 27.015 1.00 46.28 N ATOM 5461 CA THR F 159 33.927 44.340 26.480 1.00 46.80 C ATOM 5462 C THR F 159 34.772 44.588 25.240 1.00 47.39 C ATOM 5463 O THR F 159 34.495 45.516 24.479 1.00 47.37 O ATOM 5464 CB THR F 159 34.302 45.422 27.530 1.00 47.53 C ATOM 5465 OG1 THR F 159 35.591 45.130 28.084 1.00 48.04 O ATOM 5466 CG2 THR F 159 33.269 45.471 28.657 1.00 48.15 C ATOM 5467 N GLU F 160 35.807 43.770 25.048 1.00 47.49 N ATOM 5468 CA GLU F 160 36.695 43.913 23.900 1.00 47.50 C ATOM 5469 C GLU F 160 35.894 43.832 22.602 1.00 47.37 C ATOM 5470 O GLU F 160 36.019 44.683 21.727 1.00 47.28 O ATOM 5471 CB GLU F 160 37.764 42.812 23.922 1.00 47.86 C ATOM 5472 N LYS F 161 35.058 42.805 22.505 1.00 46.88 N ATOM 5473 CA LYS F 161 34.225 42.574 21.335 1.00 46.63 C ATOM 5474 C LYS F 161 33.062 43.566 21.194 1.00 45.96 C ATOM 5475 O LYS F 161 32.268 43.452 20.261 1.00 45.92 O ATOM 5476 CB LYS F 161 33.663 41.144 21.386 1.00 47.58 C ATOM 5477 N MET F 162 32.962 44.528 22.111 1.00 45.07 N ATOM 5478 CA MET F 162 31.876 45.514 22.088 1.00 44.13 C ATOM 5479 C MET F 162 32.350 46.941 21.834 1.00 43.91 C ATOM 5480 O MET F 162 31.532 47.852 21.671 1.00 43.60 O ATOM 5481 CB MET F 162 31.110 45.491 23.417 1.00 43.45 C ATOM 5482 CG MET F 162 30.339 44.215 23.708 1.00 42.75 C ATOM 5483 SD MET F 162 29.681 44.224 25.407 1.00 44.78 S ATOM 5484 CE MET F 162 28.618 45.682 25.364 1.00 42.60 C ATOM 5485 N GLU F 163 33.663 47.139 21.796 1.00 43.66 N ATOM 5486 CA GLU F 163 34.228 48.474 21.595 1.00 43.05 C ATOM 5487 C GLU F 163 33.900 49.117 20.245 1.00 42.02 C ATOM 5488 O GLU F 163 33.747 50.336 20.150 1.00 42.39 O ATOM 5489 CB GLU F 163 35.748 48.432 21.790 1.00 43.51 C ATOM 5490 N LYS F 164 33.801 48.302 19.201 1.00 40.60 N ATOM 5491 CA LYS F 164 33.482 48.806 17.866 1.00 38.52 C ATOM 5492 C LYS F 164 31.982 49.137 17.821 1.00 37.22 C ATOM 5493 O LYS F 164 31.152 48.253 17.609 1.00 36.84 O ATOM 5494 CB LYS F 164 33.835 47.742 16.820 1.00 37.86 C ATOM 5495 CG LYS F 164 33.861 48.266 15.410 1.00 37.96 C ATOM 5496 CD LYS F 164 34.340 47.228 14.408 1.00 37.78 C ATOM 5497 CE LYS F 164 33.188 46.490 13.757 1.00 38.14 C ATOM 5498 NZ LYS F 164 33.621 45.853 12.478 1.00 39.11 N ATOM 5499 N ARG F 165 31.644 50.407 18.025 1.00 35.96 N ATOM 5500 CA ARG F 165 30.247 50.843 18.044 1.00 35.34 C ATOM 5501 C ARG F 165 29.614 51.005 16.672 1.00 33.90 C ATOM 5502 O ARG F 165 28.468 50.609 16.466 1.00 32.97 O ATOM 5503 CB ARG F 165 30.110 52.151 18.833 1.00 36.33 C ATOM 5504 CG ARG F 165 30.254 51.954 20.333 1.00 39.65 C ATOM 5505 CD ARG F 165 30.371 53.273 21.066 1.00 42.36 C ATOM 5506 NE ARG F 165 30.713 53.076 22.472 1.00 45.53 N ATOM 5507 CZ ARG F 165 29.837 52.783 23.429 1.00 47.06 C ATOM 5508 NH1 ARG F 165 28.540 52.656 23.148 1.00 47.85 N ATOM 5509 NH2 ARG F 165 30.262 52.607 24.671 1.00 47.69 N ATOM 5510 N LEU F 166 30.364 51.593 15.746 1.00 33.06 N ATOM 5511 CA LEU F 166 29.905 51.808 14.379 1.00 32.49 C ATOM 5512 C LEU F 166 30.309 50.638 13.497 1.00 32.80 C ATOM 5513 O LEU F 166 31.498 50.360 13.350 1.00 32.69 O ATOM 5514 CB LEU F 166 30.528 53.083 13.801 1.00 30.33 C ATOM 5515 CG LEU F 166 30.342 53.309 12.288 1.00 31.08 C ATOM 5516 CD1 LEU F 166 28.859 53.376 11.924 1.00 28.89 C ATOM 5517 CD2 LEU F 166 31.033 54.592 11.879 1.00 28.85 C ATOM 5518 N HIS F 167 29.322 49.957 12.918 1.00 32.67 N ATOM 5519 CA HIS F 167 29.565 48.837 12.015 1.00 32.58 C ATOM 5520 C HIS F 167 29.153 49.268 10.614 1.00 33.20 C ATOM 5521 O HIS F 167 27.959 49.316 10.302 1.00 33.21 O ATOM 5522 CB HIS F 167 28.737 47.609 12.413 1.00 33.93 C ATOM 5523 CG HIS F 167 29.317 46.814 13.541 1.00 35.95 C ATOM 5524 ND1 HIS F 167 29.561 47.350 14.788 1.00 37.05 N ATOM 5525 CD2 HIS F 167 29.699 45.516 13.609 1.00 35.66 C ATOM 5526 CE1 HIS F 167 30.070 46.418 15.574 1.00 36.41 C ATOM 5527 NE2 HIS F 167 30.164 45.296 14.882 1.00 36.24 N ATOM 5528 N ALA F 168 30.135 49.601 9.782 1.00 32.49 N ATOM 5529 CA ALA F 168 29.872 50.015 8.408 1.00 32.62 C ATOM 5530 C ALA F 168 30.255 48.815 7.562 1.00 32.27 C ATOM 5531 O ALA F 168 31.394 48.362 7.614 1.00 32.31 O ATOM 5532 CB ALA F 168 30.739 51.224 8.040 1.00 33.46 C ATOM 5533 N VAL F 169 29.310 48.299 6.786 1.00 31.84 N ATOM 5534 CA VAL F 169 29.574 47.125 5.965 1.00 31.85 C ATOM 5535 C VAL F 169 29.011 47.239 4.557 1.00 31.61 C ATOM 5536 O VAL F 169 28.063 47.977 4.311 1.00 31.56 O ATOM 5537 CB VAL F 169 28.959 45.859 6.596 1.00 32.55 C ATOM 5538 CG1 VAL F 169 29.416 45.725 8.046 1.00 33.61 C ATOM 5539 CG2 VAL F 169 27.441 45.928 6.515 1.00 31.02 C ATOM 5540 N PRO F 170 29.592 46.491 3.616 1.00 31.38 N ATOM 5541 CA PRO F 170 29.123 46.525 2.234 1.00 31.61 C ATOM 5542 C PRO F 170 27.809 45.763 2.103 1.00 32.21 C ATOM 5543 O PRO F 170 27.585 44.761 2.789 1.00 31.90 O ATOM 5544 CB PRO F 170 30.267 45.863 1.472 1.00 31.99 C ATOM 5545 CG PRO F 170 30.758 44.824 2.463 1.00 31.40 C ATOM 5546 CD PRO F 170 30.722 45.556 3.784 1.00 30.53 C ATOM 5547 N ALA F 171 26.931 46.251 1.234 1.00 33.14 N ATOM 5548 CA ALA F 171 25.640 45.606 1.009 1.00 33.63 C ATOM 5549 C ALA F 171 25.821 44.140 0.596 1.00 33.79 C ATOM 5550 O ALA F 171 26.811 43.779 −0.049 1.00 32.97 O ATOM 5551 CB ALA F 171 24.863 46.362 −0.063 1.00 33.56 C ATOM 5552 N ALA F 172 24.863 43.303 1.001 1.00 33.61 N ATOM 5553 CA ALA F 172 24.849 41.872 0.699 1.00 33.16 C ATOM 5554 C ALA F 172 25.643 41.011 1.684 1.00 33.77 C ATOM 5555 O ALA F 172 25.654 39.778 1.579 1.00 33.75 O ATOM 5556 CB ALA F 172 25.328 41.622 −0.744 1.00 33.35 C ATOM 5557 N ASN F 173 26.310 41.640 2.642 1.00 33.18 N ATOM 5558 CA ASN F 173 27.061 40.866 3.629 1.00 33.48 C ATOM 5559 C ASN F 173 26.191 40.528 4.839 1.00 32.36 C ATOM 5560 O ASN F 173 25.077 41.033 4.980 1.00 31.26 O ATOM 5561 CB ASN F 173 28.314 41.636 4.062 1.00 34.43 C ATOM 5562 CG ASN F 173 29.483 41.423 3.108 1.00 36.77 C ATOM 5563 OD1 ASN F 173 29.307 41.276 1.890 1.00 37.96 O ATOM 5564 ND2 ASN F 173 30.683 41.413 3.657 1.00 38.51 N ATOM 5565 N THR F 174 26.698 39.648 5.693 1.00 31.64 N ATOM 5566 CA THR F 174 26.000 39.268 6.913 1.00 30.65 C ATOM 5567 C THR F 174 26.589 40.107 8.047 1.00 30.96 C ATOM 5568 O THR F 174 27.799 40.333 8.083 1.00 31.98 O ATOM 5569 CB THR F 174 26.217 37.779 7.249 1.00 29.86 C ATOM 5570 OG1 THR F 174 25.397 36.961 6.402 1.00 30.18 O ATOM 5571 CG2 THR F 174 25.869 37.507 8.692 1.00 29.82 C ATOM 5572 N VAL F 175 25.741 40.573 8.961 1.00 30.45 N ATOM 5573 CA VAL F 175 26.200 41.363 10.100 1.00 30.13 C ATOM 5574 C VAL F 175 25.868 40.632 11.394 1.00 30.00 C ATOM 5575 O VAL F 175 24.807 40.009 11.514 1.00 29.84 O ATOM 5576 CB VAL F 175 25.521 42.754 10.153 1.00 30.57 C ATOM 5577 CG1 VAL F 175 26.040 43.542 11.348 1.00 31.35 C ATOM 5578 CG2 VAL F 175 25.807 43.510 8.890 1.00 30.75 C ATOM 5579 N LYS F 176 26.775 40.693 12.360 1.00 29.06 N ATOM 5580 CA LYS F 176 26.538 40.047 13.640 1.00 29.99 C ATOM 5581 C LYS F 176 26.914 40.962 14.805 1.00 30.49 C ATOM 5582 O LYS F 176 28.048 41.443 14.894 1.00 30.73 O ATOM 5583 CB LYS F 176 27.328 38.734 13.733 1.00 32.08 C ATOM 5584 CG LYS F 176 27.054 37.893 15.000 1.00 34.61 C ATOM 5585 CD LYS F 176 27.852 36.559 15.005 1.00 35.52 C ATOM 5586 CE LYS F 176 27.675 35.791 16.324 1.00 38.38 C ATOM 5587 NZ LYS F 176 28.376 34.451 16.397 1.00 37.91 N ATOM 5588 N PHE F 177 25.953 41.213 15.688 1.00 29.86 N ATOM 5589 CA PHE F 177 26.198 42.038 16.861 1.00 29.32 C ATOM 5590 C PHE F 177 26.219 41.125 18.065 1.00 29.40 C ATOM 5591 O PHE F 177 25.412 40.210 18.156 1.00 30.08 O ATOM 5592 CB PHE F 177 25.095 43.080 17.024 1.00 28.12 C ATOM 5593 CG PHE F 177 25.075 44.108 15.931 1.00 28.38 C ATOM 5594 CD1 PHE F 177 26.193 44.903 15.689 1.00 27.55 C ATOM 5595 CD2 PHE F 177 23.929 44.306 15.163 1.00 28.25 C ATOM 5596 CE1 PHE F 177 26.170 45.877 14.709 1.00 27.35 C ATOM 5597 CE2 PHE F 177 23.897 45.285 14.176 1.00 28.12 C ATOM 5598 CZ PHE F 177 25.021 46.073 13.949 1.00 28.28 C ATOM 5599 N ARG F 178 27.142 41.371 18.988 1.00 29.44 N ATOM 5600 CA ARG F 178 27.254 40.549 20.187 1.00 29.63 C ATOM 5601 C ARG F 178 27.345 41.365 21.481 1.00 29.59 C ATOM 5602 O ARG F 178 27.910 42.467 21.513 1.00 27.47 O ATOM 5603 CB ARG F 178 28.489 39.639 20.097 1.00 30.99 C ATOM 5604 CG ARG F 178 28.567 38.762 18.847 1.00 36.16 C ATOM 5605 CD ARG F 178 29.692 37.737 18.978 1.00 38.76 C ATOM 5606 NE ARG F 178 29.502 36.952 20.194 1.00 43.37 N ATOM 5607 CZ ARG F 178 30.425 36.178 20.760 1.00 45.05 C ATOM 5608 NH1 ARG F 178 31.636 36.065 20.222 1.00 46.10 N ATOM 5609 NH2 ARG F 178 30.138 35.537 21.888 1.00 45.60 N ATOM 5610 N CYS F 179 26.790 40.799 22.549 1.00 28.88 N ATOM 5611 CA CYS F 179 26.820 41.419 23.863 1.00 30.56 C ATOM 5612 C CYS F 179 27.008 40.310 24.903 1.00 30.82 C ATOM 5613 O CYS F 179 26.125 40.044 25.719 1.00 30.14 O ATOM 5614 CB CYS F 179 25.522 42.197 24.090 1.00 31.07 C ATOM 5615 SG CYS F 179 25.381 43.590 22.916 1.00 32.29 S ATOM 5616 N PRO F 180 28.178 39.646 24.877 1.00 31.38 N ATOM 5617 CA PRO F 180 28.499 38.554 25.806 1.00 31.88 C ATOM 5618 C PRO F 180 28.193 38.983 27.228 1.00 31.88 C ATOM 5619 O PRO F 180 28.736 39.975 27.700 1.00 31.46 O ATOM 5620 CB PRO F 180 29.997 38.330 25.572 1.00 31.52 C ATOM 5621 CG PRO F 180 30.177 38.721 24.136 1.00 31.75 C ATOM 5622 CD PRO F 180 29.353 39.988 24.049 1.00 30.52 C ATOM 5623 N ALA F 181 27.325 38.242 27.908 1.00 33.13 N ATOM 5624 CA ALA F 181 26.956 38.600 29.271 1.00 34.09 C ATOM 5625 C ALA F 181 26.984 37.457 30.285 1.00 35.33 C ATOM 5626 O ALA F 181 26.913 36.283 29.931 1.00 35.01 O ATOM 5627 CB ALA F 181 25.573 39.242 29.261 1.00 33.08 C ATOM 5628 N GLY F 182 27.078 37.836 31.558 1.00 37.02 N ATOM 5629 CA GLY F 182 27.078 36.882 32.653 1.00 37.61 C ATOM 5630 C GLY F 182 26.039 37.337 33.661 1.00 38.86 C ATOM 5631 O GLY F 182 25.473 38.427 33.512 1.00 39.18 O ATOM 5632 N GLY F 183 25.787 36.523 34.684 1.00 39.21 N ATOM 5633 CA GLY F 183 24.808 36.877 35.696 1.00 39.07 C ATOM 5634 C GLY F 183 24.147 35.664 36.334 1.00 39.97 C ATOM 5635 O GLY F 183 24.067 34.593 35.724 1.00 39.49 O ATOM 5636 N ASN F 184 23.669 35.833 37.563 1.00 40.16 N ATOM 5637 CA ASN F 184 23.009 34.753 38.289 1.00 41.28 C ATOM 5638 C ASN F 184 21.817 35.278 39.081 1.00 41.39 C ATOM 5639 O ASN F 184 21.978 36.018 40.042 1.00 41.84 O ATOM 5640 CB ASN F 184 24.000 34.069 39.239 1.00 40.91 C ATOM 5641 N PRO F 185 20.602 34.861 38.713 1.00 42.38 N ATOM 5642 CA PRO F 185 20.293 33.939 37.617 1.00 42.85 C ATOM 5643 C PRO F 185 20.635 34.437 36.212 1.00 44.15 C ATOM 5644 O PRO F 185 20.856 35.633 35.990 1.00 44.57 O ATOM 5645 CB PRO F 185 18.798 33.686 37.794 1.00 42.29 C ATOM 5646 CG PRO F 185 18.307 34.969 38.373 1.00 42.96 C ATOM 5647 CD PRO F 185 19.370 35.301 39.391 1.00 42.46 C ATOM 5648 N MET F 186 20.681 33.495 35.273 1.00 44.62 N ATOM 5649 CA MET F 186 20.972 33.778 33.873 1.00 44.74 C ATOM 5650 C MET F 186 20.074 34.892 33.347 1.00 43.80 C ATOM 5651 O MET F 186 18.852 34.763 33.322 1.00 43.60 O ATOM 5652 CB MET F 186 20.750 32.518 33.040 1.00 46.95 C ATOM 5653 CG MET F 186 22.018 31.918 32.466 1.00 49.12 C ATOM 5654 SD MET F 186 22.712 32.953 31.179 1.00 50.87 S ATOM 5655 CE MET F 186 24.474 32.841 31.516 1.00 50.04 C ATOM 5656 N PRO F 187 20.676 36.002 32.905 1.00 42.90 N ATOM 5657 CA PRO F 187 19.878 37.117 32.387 1.00 42.25 C ATOM 5658 C PRO F 187 19.261 36.852 31.009 1.00 41.47 C ATOM 5659 O PRO F 187 19.778 36.048 30.228 1.00 40.21 O ATOM 5660 CB PRO F 187 20.881 38.268 32.368 1.00 42.05 C ATOM 5661 CG PRO F 187 22.173 37.575 32.047 1.00 42.87 C ATOM 5662 CD PRO F 187 22.118 36.317 32.891 1.00 42.21 C ATOM 5663 N THR F 188 18.145 37.522 30.728 1.00 40.55 N ATOM 5664 CA THR F 188 17.483 37.381 29.440 1.00 40.68 C ATOM 5665 C THR F 188 18.042 38.446 28.505 1.00 40.77 C ATOM 5666 O THR F 188 18.683 39.409 28.936 1.00 39.68 O ATOM 5667 CB THR F 188 15.957 37.599 29.524 1.00 40.57 C ATOM 5668 OG1 THR F 188 15.692 38.944 29.937 1.00 40.81 O ATOM 5669 CG2 THR F 188 15.321 36.621 30.493 1.00 39.87 C ATOM 5670 N MET F 189 17.782 38.272 27.219 1.00 40.70 N ATOM 5671 CA MET F 189 18.267 39.206 26.220 1.00 40.97 C ATOM 5672 C MET F 189 17.187 39.622 25.233 1.00 39.67 C ATOM 5673 O MET F 189 16.418 38.789 24.758 1.00 39.80 O ATOM 5674 CB MET F 189 19.424 38.574 25.444 1.00 42.23 C ATOM 5675 CG MET F 189 19.761 39.298 24.151 1.00 44.84 C ATOM 5676 SD MET F 189 21.320 38.752 23.419 1.00 49.58 S ATOM 5677 CE MET F 189 22.406 40.078 24.039 1.00 47.75 C ATOM 5678 N ARG F 190 17.146 40.912 24.922 1.00 37.90 N ATOM 5679 CA ARG F 190 16.190 41.442 23.957 1.00 37.20 C ATOM 5680 C ARG F 190 16.918 42.458 23.076 1.00 35.36 C ATOM 5681 O ARG F 190 17.806 43.176 23.553 1.00 34.22 O ATOM 5682 CB ARG F 190 15.033 42.143 24.661 1.00 38.85 C ATOM 5683 CG ARG F 190 14.391 41.342 25.768 1.00 41.45 C ATOM 5684 CD ARG F 190 13.371 42.202 26.488 1.00 43.93 C ATOM 5685 NE ARG F 190 13.785 43.603 26.530 1.00 45.35 N ATOM 5686 CZ ARG F 190 13.242 44.517 27.324 1.00 46.53 C ATOM 5687 NH1 ARG F 190 12.262 44.177 28.152 1.00 47.49 N ATOM 5688 NH2 ARG F 190 13.677 45.771 27.295 1.00 47.13 N ATOM 5689 N TRP F 191 16.554 42.516 21.797 1.00 32.45 N ATOM 5690 CA TRP F 191 17.175 43.468 20.881 1.00 30.87 C ATOM 5691 C TRP F 191 16.179 44.513 20.361 1.00 30.74 C ATOM 5692 O TRP F 191 15.050 44.182 19.983 1.00 30.08 O ATOM 5693 CB TRP F 191 17.822 42.747 19.691 1.00 29.23 C ATOM 5694 CG TRP F 191 19.069 41.961 20.031 1.00 27.86 C ATOM 5695 CD1 TRP F 191 19.136 40.676 20.505 1.00 28.00 C ATOM 5696 CD2 TRP F 191 20.419 42.424 19.945 1.00 26.19 C ATOM 5697 NE1 TRP F 191 20.447 40.314 20.716 1.00 26.72 N ATOM 5698 CE2 TRP F 191 21.255 41.368 20.378 1.00 26.84 C ATOM 5699 CE3 TRP F 191 21.007 43.629 19.542 1.00 26.52 C ATOM 5700 CZ2 TRP F 191 22.651 41.484 20.415 1.00 27.25 C ATOM 5701 CZ3 TRP F 191 22.393 43.746 19.581 1.00 27.35 C ATOM 5702 CH2 TRP F 191 23.200 42.677 20.015 1.00 26.74 C ATOM 5703 N LEU F 192 16.599 45.776 20.357 1.00 29.31 N ATOM 5704 CA LEU F 192 15.753 46.855 19.869 1.00 29.21 C ATOM 5705 C LEU F 192 16.342 47.464 18.597 1.00 29.29 C ATOM 5706 O LEU F 192 17.563 47.476 18.411 1.00 30.46 O ATOM 5707 CB LEU F 192 15.635 47.979 20.913 1.00 28.58 C ATOM 5708 CG LEU F 192 15.310 47.719 22.389 1.00 29.75 C ATOM 5709 CD1 LEU F 192 15.487 49.003 23.168 1.00 30.04 C ATOM 5710 CD2 LEU F 192 13.895 47.195 22.555 1.00 28.67 C ATOM 5711 N LYS F 193 15.472 47.940 17.712 1.00 28.31 N ATOM 5712 CA LYS F 193 15.902 48.633 16.508 1.00 28.68 C ATOM 5713 C LYS F 193 15.378 50.065 16.685 1.00 29.44 C ATOM 5714 O LYS F 193 14.165 50.283 16.814 1.00 28.28 O ATOM 5715 CB LYS F 193 15.296 48.028 15.243 1.00 28.12 C ATOM 5716 CG LYS F 193 15.691 48.806 13.977 1.00 28.39 C ATOM 5717 CD LYS F 193 15.047 48.252 12.710 1.00 30.20 C ATOM 5718 CE LYS F 193 15.479 49.044 11.469 1.00 31.28 C ATOM 5719 NZ LYS F 193 14.810 48.560 10.212 1.00 31.21 N ATOM 5720 N ASN F 194 16.287 51.035 16.693 1.00 29.56 N ATOM 5721 CA ASN F 194 15.899 52.424 16.883 1.00 30.70 C ATOM 5722 C ASN F 194 15.035 52.598 18.138 1.00 31.61 C ATOM 5723 O ASN F 194 13.974 53.210 18.091 1.00 32.50 O ATOM 5724 CB ASN F 194 15.141 52.947 15.659 1.00 28.93 C ATOM 5725 CG ASN F 194 15.998 52.970 14.409 1.00 28.90 C ATOM 5726 OD1 ASN F 194 17.194 53.287 14.464 1.00 26.90 O ATOM 5727 ND2 ASN F 194 15.389 52.645 13.266 1.00 27.33 N ATOM 5728 N GLY F 195 15.492 52.028 19.250 1.00 32.59 N ATOM 5729 CA GLY F 195 14.785 52.139 20.518 1.00 32.86 C ATOM 5730 C GLY F 195 13.434 51.455 20.666 1.00 33.71 C ATOM 5731 O GLY F 195 12.741 51.692 21.648 1.00 33.71 O ATOM 5732 N LYS F 196 13.051 50.612 19.712 1.00 34.46 N ATOM 5733 CA LYS F 196 11.759 49.927 19.783 1.00 35.48 C ATOM 5734 C LYS F 196 11.935 48.442 19.500 1.00 35.38 C ATOM 5735 O LYS F 196 12.905 48.042 18.867 1.00 34.41 O ATOM 5736 CB LYS F 196 10.795 50.528 18.749 1.00 36.77 C ATOM 5737 CG LYS F 196 10.686 52.047 18.820 1.00 38.24 C ATOM 5738 CD LYS F 196 10.084 52.649 17.555 1.00 39.91 C ATOM 5739 CE LYS F 196 10.911 52.325 16.318 1.00 40.90 C ATOM 5740 NZ LYS F 196 10.542 53.178 15.150 1.00 41.25 N ATOM 5741 N GLU F 197 10.991 47.630 19.963 1.00 35.86 N ATOM 5742 CA GLU F 197 11.047 46.194 19.735 1.00 36.04 C ATOM 5743 C GLU F 197 11.352 45.921 18.264 1.00 35.04 C ATOM 5744 O GLU F 197 10.765 46.539 17.372 1.00 33.77 O ATOM 5745 CB GLU F 197 9.718 45.535 20.138 1.00 37.85 C ATOM 5746 CG GLU F 197 9.555 44.092 19.646 1.00 40.50 C ATOM 5747 CD GLU F 197 8.268 43.420 20.142 1.00 42.49 C ATOM 5748 OE1 GLU F 197 7.216 44.098 20.218 1.00 43.04 O ATOM 5749 OE2 GLU F 197 8.311 42.207 20.437 1.00 42.34 O ATOM 5750 N PHE F 198 12.297 45.013 18.033 1.00 34.31 N ATOM 5751 CA PHE F 198 12.721 44.626 16.695 1.00 33.94 C ATOM 5752 C PHE F 198 11.964 43.334 16.386 1.00 34.49 C ATOM 5753 O PHE F 198 12.159 42.328 17.062 1.00 33.96 O ATOM 5754 CB PHE F 198 14.234 44.373 16.708 1.00 32.03 C ATOM 5755 CG PHE F 198 14.851 44.172 15.345 1.00 30.37 C ATOM 5756 CD1 PHE F 198 16.076 43.523 15.223 1.00 29.72 C ATOM 5757 CD2 PHE F 198 14.238 44.659 14.195 1.00 29.77 C ATOM 5758 CE1 PHE F 198 16.688 43.359 13.965 1.00 29.73 C ATOM 5759 CE2 PHE F 198 14.840 44.500 12.936 1.00 30.25 C ATOM 5760 CZ PHE F 198 16.071 43.847 12.828 1.00 28.74 C ATOM 5761 N LYS F 199 11.099 43.372 15.377 1.00 35.60 N ATOM 5762 CA LYS F 199 10.304 42.204 14.994 1.00 36.11 C ATOM 5763 C LYS F 199 10.760 41.601 13.675 1.00 35.77 C ATOM 5764 O LYS F 199 11.331 42.293 12.836 1.00 35.67 O ATOM 5765 CB LYS F 199 8.825 42.584 14.896 1.00 36.91 C ATOM 5766 CG LYS F 199 8.226 43.120 16.196 1.00 38.98 C ATOM 5767 CD LYS F 199 6.748 43.447 16.026 1.00 40.85 C ATOM 5768 CE LYS F 199 6.103 43.833 17.358 1.00 42.06 C ATOM 5769 NZ LYS F 199 4.614 43.950 17.244 1.00 42.75 N ATOM 5770 N GLN F 200 10.490 40.308 13.502 1.00 35.69 N ATOM 5771 CA GLN F 200 10.855 39.582 12.295 1.00 35.41 C ATOM 5772 C GLN F 200 10.372 40.266 11.021 1.00 35.51 C ATOM 5773 O GLN F 200 11.083 40.306 10.027 1.00 35.58 O ATOM 5774 CB GLN F 200 10.288 38.155 12.351 1.00 34.06 C ATOM 5775 CG GLN F 200 10.978 37.228 13.347 1.00 31.65 C ATOM 5776 CD GLN F 200 12.453 37.037 13.039 1.00 29.88 C ATOM 5777 OE1 GLN F 200 12.855 37.003 11.878 1.00 29.84 O ATOM 5778 NE2 GLN F 200 13.261 36.889 14.080 1.00 29.62 N ATOM 5779 N GLU F 201 9.166 40.821 11.059 1.00 36.04 N ATOM 5780 CA GLU F 201 8.593 41.469 9.887 1.00 36.60 C ATOM 5781 C GLU F 201 9.204 42.833 9.576 1.00 35.96 C ATOM 5782 O GLU F 201 8.845 43.461 8.579 1.00 35.12 O ATOM 5783 CB GLU F 201 7.082 41.619 10.071 1.00 37.56 C ATOM 5784 CG GLU F 201 6.709 42.533 11.220 1.00 41.31 C ATOM 5785 CD GLU F 201 6.054 41.798 12.385 1.00 44.04 C ATOM 5786 OE1 GLU F 201 6.638 40.813 12.917 1.00 43.75 O ATOM 5787 OE2 GLU F 201 4.945 42.224 12.775 1.00 45.55 O ATOM 5788 N HIS F 202 10.124 43.296 10.420 1.00 35.49 N ATOM 5789 CA HIS F 202 10.751 44.597 10.196 1.00 35.12 C ATOM 5790 C HIS F 202 11.755 44.647 9.038 1.00 34.73 C ATOM 5791 O HIS F 202 12.200 45.730 8.653 1.00 35.10 O ATOM 5792 CB HIS F 202 11.409 45.115 11.481 1.00 35.18 C ATOM 5793 CG HIS F 202 10.434 45.600 12.513 1.00 35.87 C ATOM 5794 ND1 HIS F 202 9.222 46.175 12.185 1.00 36.51 N ATOM 5795 CD2 HIS F 202 10.504 45.623 13.866 1.00 34.64 C ATOM 5796 CE1 HIS F 202 8.590 46.527 13.289 1.00 35.55 C ATOM 5797 NE2 HIS F 202 9.348 46.204 14.324 1.00 35.01 N ATOM 5798 N ARG F 203 12.115 43.487 8.488 1.00 33.96 N ATOM 5799 CA ARG F 203 13.035 43.430 7.341 1.00 33.38 C ATOM 5800 C ARG F 203 12.815 42.138 6.550 1.00 33.55 C ATOM 5801 O ARG F 203 12.358 41.135 7.103 1.00 32.74 O ATOM 5802 CB ARG F 203 14.512 43.525 7.795 1.00 30.83 C ATOM 5803 CG ARG F 203 15.093 42.255 8.435 1.00 29.74 C ATOM 5804 CD ARG F 203 16.514 42.509 8.978 1.00 29.31 C ATOM 5805 NE ARG F 203 17.452 42.893 7.923 1.00 26.83 N ATOM 5806 CZ ARG F 203 18.149 42.032 7.186 1.00 25.96 C ATOM 5807 NH1 ARG F 203 18.030 40.728 7.391 1.00 24.85 N ATOM 5808 NH2 ARG F 203 18.945 42.473 6.221 1.00 26.60 N ATOM 5809 N ILE F 204 13.128 42.168 5.257 1.00 34.22 N ATOM 5810 CA ILE F 204 12.976 40.982 4.427 1.00 35.18 C ATOM 5811 C ILE F 204 13.856 39.882 5.023 1.00 35.19 C ATOM 5812 O ILE F 204 15.038 40.109 5.311 1.00 34.84 O ATOM 5813 CB ILE F 204 13.431 41.235 2.976 1.00 35.88 C ATOM 5814 CG1 ILE F 204 12.668 42.424 2.379 1.00 36.13 C ATOM 5815 CG2 ILE F 204 13.229 39.962 2.149 1.00 36.91 C ATOM 5816 CD1 ILE F 204 11.167 42.264 2.392 1.00 36.71 C ATOM 5817 N GLY F 205 13.269 38.705 5.233 1.00 34.69 N ATOM 5818 CA GLY F 205 14.012 37.588 5.793 1.00 34.34 C ATOM 5819 C GLY F 205 14.237 37.647 7.299 1.00 34.39 C ATOM 5820 O GLY F 205 14.865 36.755 7.869 1.00 34.69 O ATOM 5821 N GLY F 206 13.734 38.690 7.952 1.00 32.99 N ATOM 5822 CA GLY F 206 13.901 38.800 9.393 1.00 33.37 C ATOM 5823 C GLY F 206 15.328 38.694 9.924 1.00 33.23 C ATOM 5824 O GLY F 206 16.289 39.114 9.276 1.00 32.48 O ATOM 5825 N TYR F 207 15.472 38.136 11.117 1.00 32.64 N ATOM 5826 CA TYR F 207 16.790 37.986 11.711 1.00 33.77 C ATOM 5827 C TYR F 207 16.896 36.712 12.548 1.00 34.46 C ATOM 5828 O TYR F 207 15.899 36.020 12.764 1.00 34.79 O ATOM 5829 CB TYR F 207 17.118 39.209 12.583 1.00 33.55 C ATOM 5830 CG TYR F 207 16.153 39.441 13.732 1.00 32.75 C ATOM 5831 CD1 TYR F 207 15.015 40.246 13.571 1.00 32.44 C ATOM 5832 CD2 TYR F 207 16.374 38.850 14.979 1.00 33.03 C ATOM 5833 CE1 TYR F 207 14.119 40.460 14.628 1.00 32.42 C ATOM 5834 CE2 TYR F 207 15.477 39.052 16.054 1.00 32.73 C ATOM 5835 CZ TYR F 207 14.355 39.856 15.865 1.00 33.10 C ATOM 5836 OH TYR F 207 13.462 40.028 16.896 1.00 31.83 O ATOM 5837 N LYS F 208 18.107 36.419 13.019 1.00 34.55 N ATOM 5838 CA LYS F 208 18.361 35.237 13.840 1.00 35.20 C ATOM 5839 C LYS F 208 19.072 35.628 15.129 1.00 37.32 C ATOM 5840 O LYS F 208 19.902 36.539 15.139 1.00 37.39 O ATOM 5841 CB LYS F 208 19.236 34.236 13.083 1.00 33.89 C ATOM 5842 CG LYS F 208 18.622 33.695 11.804 1.00 33.01 C ATOM 5843 CD LYS F 208 19.638 32.897 11.002 1.00 31.73 C ATOM 5844 CE LYS F 208 19.003 32.362 9.729 1.00 31.93 C ATOM 5845 NZ LYS F 208 19.951 31.576 8.907 1.00 31.97 N ATOM 5846 N VAL F 209 18.742 34.941 16.216 1.00 39.09 N ATOM 5847 CA VAL F 209 19.364 35.204 17.507 1.00 41.34 C ATOM 5848 C VAL F 209 19.850 33.902 18.134 1.00 43.43 C ATOM 5849 O VAL F 209 19.107 32.916 18.204 1.00 44.61 O ATOM 5850 CB VAL F 209 18.384 35.897 18.489 1.00 40.99 C ATOM 5851 CG1 VAL F 209 18.955 35.882 19.897 1.00 41.66 C ATOM 5852 CG2 VAL F 209 18.143 37.332 18.060 1.00 40.70 C ATOM 5853 N ARG F 210 21.105 33.897 18.572 1.00 44.15 N ATOM 5854 CA ARG F 210 21.688 32.727 19.216 1.00 45.63 C ATOM 5855 C ARG F 210 21.983 33.107 20.671 1.00 46.74 C ATOM 5856 O ARG F 210 23.029 33.684 20.979 1.00 46.52 O ATOM 5857 CB ARG F 210 22.972 32.302 18.499 1.00 45.37 C ATOM 5858 N ASN F 211 21.044 32.794 21.560 1.00 48.22 N ATOM 5859 CA ASN F 211 21.191 33.119 22.974 1.00 49.06 C ATOM 5860 C ASN F 211 22.512 32.641 23.558 1.00 48.57 C ATOM 5861 O ASN F 211 23.121 33.336 24.370 1.00 48.61 O ATOM 5862 CB ASN F 211 20.019 32.552 23.774 1.00 50.40 C ATOM 5863 CG ASN F 211 18.688 33.151 23.348 1.00 52.24 C ATOM 5864 OD1 ASN F 211 18.489 34.370 23.409 1.00 53.07 O ATOM 5865 ND2 ASN F 211 17.773 32.296 22.906 1.00 52.36 N ATOM 5866 N GLN F 212 22.960 31.463 23.136 1.00 47.95 N ATOM 5867 CA GLN F 212 24.222 30.906 23.622 1.00 47.07 C ATOM 5868 C GLN F 212 25.408 31.839 23.341 1.00 46.07 C ATOM 5869 O GLN F 212 26.396 31.832 24.076 1.00 46.29 O ATOM 5870 CB GLN F 212 24.479 29.536 22.981 1.00 47.25 C ATOM 5871 N HIS F 213 25.312 32.638 22.279 1.00 43.99 N ATOM 5872 CA HIS F 213 26.384 33.569 21.932 1.00 41.91 C ATOM 5873 C HIS F 213 26.008 35.040 22.164 1.00 40.31 C ATOM 5874 O HIS F 213 26.784 35.938 21.833 1.00 39.47 O ATOM 5875 CB HIS F 213 26.796 33.384 20.467 1.00 42.21 C ATOM 5876 N TRP F 214 24.825 35.280 22.733 1.00 38.43 N ATOM 5877 CA TRP F 214 24.343 36.647 22.988 1.00 36.90 C ATOM 5878 C TRP F 214 24.485 37.477 21.710 1.00 35.65 C ATOM 5879 O TRP F 214 24.998 38.596 21.732 1.00 34.83 O ATOM 5880 CB TRP F 214 25.156 37.310 24.117 1.00 37.32 C ATOM 5881 CG TRP F 214 25.253 36.467 25.357 1.00 38.36 C ATOM 5882 CD1 TRP F 214 26.254 35.591 25.680 1.00 39.05 C ATOM 5883 CD2 TRP F 214 24.268 36.348 26.391 1.00 38.90 C ATOM 5884 NE1 TRP F 214 25.947 34.929 26.846 1.00 38.91 N ATOM 5885 CE2 TRP F 214 24.735 35.374 27.304 1.00 39.07 C ATOM 5886 CE3 TRP F 214 23.032 36.968 26.635 1.00 39.11 C ATOM 5887 CZ2 TRP F 214 24.011 35.005 28.443 1.00 39.13 C ATOM 5888 CZ3 TRP F 214 22.310 36.600 27.769 1.00 39.21 C ATOM 5889 CH2 TRP F 214 22.803 35.627 28.658 1.00 39.44 C ATOM 5890 N SER F 215 24.018 36.929 20.594 1.00 34.42 N ATOM 5891 CA SER F 215 24.159 37.615 19.321 1.00 33.05 C ATOM 5892 C SER F 215 22.886 37.824 18.506 1.00 32.30 C ATOM 5893 O SER F 215 21.909 37.071 18.633 1.00 31.69 O ATOM 5894 CB SER F 215 25.167 36.853 18.457 1.00 34.47 C ATOM 5895 OG SER F 215 24.645 35.578 18.095 1.00 34.50 O ATOM 5896 N LEU F 216 22.936 38.850 17.653 1.00 30.67 N ATOM 5897 CA LEU F 216 21.854 39.202 16.735 1.00 29.22 C ATOM 5898 C LEU F 216 22.477 39.122 15.347 1.00 28.34 C ATOM 5899 O LEU F 216 23.507 39.757 15.086 1.00 27.30 O ATOM 5900 CB LEU F 216 21.358 40.633 16.967 1.00 28.18 C ATOM 5901 CG LEU F 216 20.462 41.142 15.821 1.00 28.87 C ATOM 5902 CD1 LEU F 216 19.159 40.357 15.846 1.00 29.36 C ATOM 5903 CD2 LEU F 216 20.176 42.639 15.964 1.00 28.49 C ATOM 5904 N ILE F 217 21.853 38.357 14.456 1.00 28.20 N ATOM 5905 CA ILE F 217 22.364 38.187 13.098 1.00 28.31 C ATOM 5906 C ILE F 217 21.402 38.618 12.000 1.00 28.13 C ATOM 5907 O ILE F 217 20.230 38.227 11.999 1.00 27.90 O ATOM 5908 CB ILE F 217 22.779 36.718 12.872 1.00 28.75 C ATOM 5909 CG1 ILE F 217 24.022 36.418 13.716 1.00 30.55 C ATOM 5910 CG2 ILE F 217 23.053 36.452 11.397 1.00 28.99 C ATOM 5911 CD1 ILE F 217 24.513 34.974 13.624 1.00 32.18 C ATOM 5912 N MET F 218 21.909 39.432 11.074 1.00 27.45 N ATOM 5913 CA MET F 218 21.129 39.915 9.933 1.00 29.12 C ATOM 5914 C MET F 218 21.899 39.570 8.646 1.00 29.98 C ATOM 5915 O MET F 218 23.030 40.027 8.436 1.00 29.81 O ATOM 5916 CB MET F 218 20.905 41.434 10.047 1.00 29.43 C ATOM 5917 CG MET F 218 19.911 41.835 11.138 1.00 28.75 C ATOM 5918 SD MET F 218 19.910 43.607 11.546 1.00 29.55 S ATOM 5919 CE MET F 218 19.497 44.305 10.031 1.00 29.23 C ATOM 5920 N GLU F 219 21.285 38.752 7.795 1.00 29.80 N ATOM 5921 CA GLU F 219 21.907 38.325 6.542 1.00 29.89 C ATOM 5922 C GLU F 219 21.525 39.213 5.365 1.00 29.76 C ATOM 5923 O GLU F 219 20.452 39.815 5.360 1.00 29.81 O ATOM 5924 CB GLU F 219 21.512 36.872 6.259 1.00 30.00 C ATOM 5925 CG GLU F 219 21.882 35.928 7.401 1.00 30.20 C ATOM 5926 CD GLU F 219 21.026 34.680 7.437 1.00 30.77 C ATOM 5927 OE1 GLU F 219 19.794 34.814 7.316 1.00 31.01 O ATOM 5928 OE2 GLU F 219 21.581 33.571 7.598 1.00 31.65 O ATOM 5929 N SER F 220 22.420 39.301 4.383 1.00 29.62 N ATOM 5930 CA SER F 220 22.210 40.096 3.175 1.00 29.82 C ATOM 5931 C SER F 220 21.701 41.506 3.441 1.00 29.76 C ATOM 5932 O SER F 220 20.651 41.897 2.921 1.00 29.19 O ATOM 5933 CB SER F 220 21.219 39.388 2.240 1.00 30.67 C ATOM 5934 OG SER F 220 21.669 38.089 1.907 1.00 31.43 O ATOM 5935 N VAL F 221 22.451 42.283 4.217 1.00 28.67 N ATOM 5936 CA VAL F 221 22.021 43.637 4.541 1.00 28.32 C ATOM 5937 C VAL F 221 21.880 44.555 3.323 1.00 29.51 C ATOM 5938 O VAL F 221 22.542 44.370 2.293 1.00 29.53 O ATOM 5939 CB VAL F 221 22.971 44.284 5.594 1.00 28.01 C ATOM 5940 CG1 VAL F 221 23.139 43.337 6.781 1.00 26.11 C ATOM 5941 CG2 VAL F 221 24.324 44.609 4.983 1.00 26.82 C ATOM 5942 N VAL F 222 20.988 45.533 3.449 1.00 29.96 N ATOM 5943 CA VAL F 222 20.716 46.507 2.404 1.00 31.14 C ATOM 5944 C VAL F 222 20.671 47.892 3.056 1.00 32.51 C ATOM 5945 O VAL F 222 20.606 48.007 4.281 1.00 32.13 O ATOM 5946 CB VAL F 222 19.341 46.236 1.704 1.00 31.92 C ATOM 5947 CG1 VAL F 222 19.393 44.934 0.889 1.00 32.22 C ATOM 5948 CG2 VAL F 222 18.229 46.149 2.749 1.00 30.96 C ATOM 5949 N PRO F 223 20.717 48.961 2.242 1.00 33.33 N ATOM 5950 CA PRO F 223 20.678 50.337 2.744 1.00 33.05 C ATOM 5951 C PRO F 223 19.621 50.612 3.808 1.00 32.75 C ATOM 5952 O PRO F 223 19.888 51.306 4.779 1.00 31.69 O ATOM 5953 CB PRO F 223 20.449 51.149 1.472 1.00 32.99 C ATOM 5954 CG PRO F 223 21.301 50.414 0.489 1.00 33.35 C ATOM 5955 CD PRO F 223 20.963 48.949 0.786 1.00 33.24 C ATOM 5956 N SER F 224 18.428 50.051 3.636 1.00 32.51 N ATOM 5957 CA SER F 224 17.348 50.278 4.584 1.00 31.69 C ATOM 5958 C SER F 224 17.599 49.727 5.999 1.00 31.73 C ATOM 5959 O SER F 224 16.884 50.077 6.937 1.00 31.16 O ATOM 5960 CB SER F 224 16.057 49.697 4.013 1.00 31.66 C ATOM 5961 OG SER F 224 16.199 48.307 3.774 1.00 32.99 O ATOM 5962 N ASP F 225 18.604 48.867 6.160 1.00 31.38 N ATOM 5963 CA ASP F 225 18.912 48.311 7.484 1.00 30.26 C ATOM 5964 C ASP F 225 19.669 49.309 8.378 1.00 30.11 C ATOM 5965 O ASP F 225 19.874 49.068 9.570 1.00 28.77 O ATOM 5966 CB ASP F 225 19.741 47.028 7.364 1.00 29.82 C ATOM 5967 CG ASP F 225 18.952 45.864 6.793 1.00 29.68 C ATOM 5968 OD1 ASP F 225 17.802 45.623 7.242 1.00 28.36 O ATOM 5969 OD2 ASP F 225 19.500 45.174 5.909 1.00 27.10 O ATOM 5970 N LYS F 226 20.089 50.429 7.797 1.00 30.34 N ATOM 5971 CA LYS F 226 20.809 51.438 8.566 1.00 30.46 C ATOM 5972 C LYS F 226 19.980 51.868 9.778 1.00 30.07 C ATOM 5973 O LYS F 226 18.763 52.049 9.667 1.00 29.46 O ATOM 5974 CB LYS F 226 21.134 52.656 7.691 1.00 31.03 C ATOM 5975 CG LYS F 226 21.782 53.802 8.481 1.00 32.45 C ATOM 5976 CD LYS F 226 22.034 55.040 7.619 1.00 33.36 C ATOM 5977 CE LYS F 226 22.717 56.153 8.434 1.00 34.79 C ATOM 5978 NZ LYS F 226 23.090 57.326 7.587 1.00 35.90 N ATOM 5979 N GLY F 227 20.644 52.018 10.928 1.00 28.53 N ATOM 5980 CA GLY F 227 19.955 52.421 12.142 1.00 28.88 C ATOM 5981 C GLY F 227 20.679 51.982 13.403 1.00 29.17 C ATOM 5982 O GLY F 227 21.838 51.556 13.346 1.00 28.63 O ATOM 5983 N ASN F 228 20.012 52.102 14.546 1.00 28.73 N ATOM 5984 CA ASN F 228 20.608 51.697 15.815 1.00 29.18 C ATOM 5985 C ASN F 228 20.029 50.382 16.314 1.00 28.27 C ATOM 5986 O ASN F 228 18.821 50.157 16.229 1.00 28.24 O ATOM 5987 CB ASN F 228 20.386 52.755 16.888 1.00 31.52 C ATOM 5988 CG ASN F 228 20.888 54.112 16.469 1.00 33.14 C ATOM 5989 OD1 ASN F 228 21.966 54.241 15.897 1.00 34.19 O ATOM 5990 ND2 ASN F 228 20.108 55.138 16.760 1.00 34.39 N ATOM 5991 N TYR F 229 20.902 49.521 16.832 1.00 26.46 N ATOM 5992 CA TYR F 229 20.502 48.229 17.374 1.00 25.52 C ATOM 5993 C TYR F 229 21.014 48.118 18.801 1.00 25.73 C ATOM 5994 O TYR F 229 22.227 48.156 19.062 1.00 25.37 O ATOM 5995 CB TYR F 229 21.034 47.088 16.505 1.00 23.62 C ATOM 5996 CG TYR F 229 20.487 47.141 15.104 1.00 24.17 C ATOM 5997 CD1 TYR F 229 21.007 48.028 14.167 1.00 24.31 C ATOM 5998 CD2 TYR F 229 19.383 46.368 14.735 1.00 24.16 C ATOM 5999 CE1 TYR F 229 20.429 48.154 12.901 1.00 25.39 C ATOM 6000 CE2 TYR F 229 18.811 46.482 13.488 1.00 22.86 C ATOM 6001 CZ TYR F 229 19.325 47.374 12.576 1.00 24.60 C ATOM 6002 OH TYR F 229 18.706 47.529 11.356 1.00 26.12 O ATOM 6003 N THR F 230 20.069 47.979 19.724 1.00 25.46 N ATOM 6004 CA THR F 230 20.374 47.917 21.148 1.00 24.62 C ATOM 6005 C THR F 230 20.056 46.583 21.807 1.00 25.10 C ATOM 6006 O THR F 230 18.980 46.005 21.613 1.00 24.11 O ATOM 6007 CB THR F 230 19.587 49.004 21.896 1.00 23.96 C ATOM 6008 OG1 THR F 230 19.859 50.274 21.289 1.00 23.10 O ATOM 6009 CG2 THR F 230 19.961 49.021 23.373 1.00 22.18 C ATOM 6010 N CYS F 231 21.004 46.099 22.598 1.00 25.89 N ATOM 6011 CA CYS F 231 20.822 44.855 23.315 1.00 26.87 C ATOM 6012 C CYS F 231 20.512 45.213 24.771 1.00 27.21 C ATOM 6013 O CYS F 231 21.214 46.020 25.370 1.00 26.18 O ATOM 6014 CB CYS F 231 22.099 44.007 23.237 1.00 27.34 C ATOM 6015 SG CYS F 231 23.556 44.785 24.032 1.00 27.77 S ATOM 6016 N VAL F 232 19.443 44.631 25.315 1.00 27.93 N ATOM 6017 CA VAL F 232 19.050 44.853 26.705 1.00 29.90 C ATOM 6018 C VAL F 232 19.155 43.504 27.432 1.00 30.42 C ATOM 6019 O VAL F 232 18.573 42.517 27.006 1.00 31.57 O ATOM 6020 CB VAL F 232 17.609 45.396 26.778 1.00 30.35 C ATOM 6021 CG1 VAL F 232 17.246 45.772 28.211 1.00 29.59 C ATOM 6022 CG2 VAL F 232 17.482 46.603 25.853 1.00 29.86 C ATOM 6023 N VAL F 233 19.921 43.464 28.516 1.00 31.25 N ATOM 6024 CA VAL F 233 20.130 42.231 29.269 1.00 32.28 C ATOM 6025 C VAL F 233 19.688 42.432 30.716 1.00 32.94 C ATOM 6026 O VAL F 233 20.094 43.403 31.363 1.00 32.94 O ATOM 6027 CB VAL F 233 21.624 41.825 29.239 1.00 31.65 C ATOM 6028 CG1 VAL F 233 21.830 40.525 29.969 1.00 33.89 C ATOM 6029 CG2 VAL F 233 22.088 41.687 27.817 1.00 33.22 C ATOM 6030 N GLU F 234 18.879 41.510 31.236 1.00 32.73 N ATOM 6031 CA GLU F 234 18.375 41.667 32.590 1.00 34.27 C ATOM 6032 C GLU F 234 18.012 40.423 33.407 1.00 34.49 C ATOM 6033 O GLU F 234 17.763 39.344 32.865 1.00 34.80 O ATOM 6034 CB GLU F 234 17.139 42.573 32.539 1.00 34.06 C ATOM 6035 N ASN F 235 18.003 40.607 34.725 1.00 35.03 N ATOM 6036 CA ASN F 235 17.590 39.585 35.690 1.00 35.08 C ATOM 6037 C ASN F 235 17.034 40.378 36.868 1.00 35.26 C ATOM 6038 O ASN F 235 16.921 41.603 36.781 1.00 34.94 O ATOM 6039 CB ASN F 235 18.734 38.635 36.108 1.00 34.70 C ATOM 6040 CG ASN F 235 19.857 39.323 36.869 1.00 35.25 C ATOM 6041 OD1 ASN F 235 19.681 40.395 37.436 1.00 35.24 O ATOM 6042 ND2 ASN F 235 21.019 38.678 36.909 1.00 35.44 N ATOM 6043 N GLU F 236 16.679 39.700 37.952 1.00 36.51 N ATOM 6044 CA GLU F 236 16.100 40.364 39.123 1.00 37.07 C ATOM 6045 C GLU F 236 16.963 41.442 39.798 1.00 37.35 C ATOM 6046 O GLU F 236 16.432 42.300 40.503 1.00 37.63 O ATOM 6047 CB GLU F 236 15.704 39.305 40.162 1.00 37.52 C ATOM 6048 N TYR F 237 18.276 41.407 39.578 1.00 37.29 N ATOM 6049 CA TYR F 237 19.180 42.367 40.215 1.00 37.37 C ATOM 6050 C TYR F 237 19.685 43.499 39.317 1.00 36.07 C ATOM 6051 O TYR F 237 20.510 44.312 39.737 1.00 35.50 O ATOM 6052 CB TYR F 237 20.362 41.603 40.822 1.00 39.38 C ATOM 6053 CG TYR F 237 19.925 40.411 41.654 1.00 41.87 C ATOM 6054 CD1 TYR F 237 20.347 39.114 41.334 1.00 42.98 C ATOM 6055 CD2 TYR F 237 19.066 40.574 42.738 1.00 42.55 C ATOM 6056 CE1 TYR F 237 19.920 38.010 42.075 1.00 44.44 C ATOM 6057 CE2 TYR F 237 18.633 39.484 43.482 1.00 44.45 C ATOM 6058 CZ TYR F 237 19.062 38.205 43.146 1.00 45.27 C ATOM 6059 OH TYR F 237 18.618 37.126 43.877 1.00 47.09 O ATOM 6060 N GLY F 238 19.202 43.563 38.082 1.00 34.94 N ATOM 6061 CA GLY F 238 19.656 44.642 37.223 1.00 34.17 C ATOM 6062 C GLY F 238 19.327 44.554 35.746 1.00 33.32 C ATOM 6063 O GLY F 238 18.889 43.521 35.243 1.00 32.51 O ATOM 6064 N SER F 239 19.543 45.669 35.058 1.00 32.77 N ATOM 6065 CA SER F 239 19.303 45.767 33.628 1.00 32.73 C ATOM 6066 C SER F 239 20.334 46.705 33.004 1.00 31.60 C ATOM 6067 O SER F 239 20.501 47.836 33.457 1.00 31.83 O ATOM 6068 CB SER F 239 17.885 46.290 33.362 1.00 32.31 C ATOM 6069 OG SER F 239 17.611 46.293 31.973 1.00 34.81 O ATOM 6070 N ILE F 240 21.009 46.234 31.958 1.00 30.55 N ATOM 6071 CA ILE F 240 22.032 47.020 31.277 1.00 29.37 C ATOM 6072 C ILE F 240 21.857 46.909 29.766 1.00 28.68 C ATOM 6073 O ILE F 240 21.298 45.928 29.274 1.00 29.57 O ATOM 6074 CB ILE F 240 23.441 46.524 31.671 1.00 28.30 C ATOM 6075 CG1 ILE F 240 23.599 45.056 31.276 1.00 29.24 C ATOM 6076 CG2 ILE F 240 23.632 46.649 33.186 1.00 26.87 C ATOM 6077 CD1 ILE F 240 25.001 44.480 31.564 1.00 30.18 C ATOM 6078 N ASN F 241 22.330 47.913 29.031 1.00 27.35 N ATOM 6079 CA ASN F 241 22.214 47.917 27.579 1.00 25.92 C ATOM 6080 C ASN F 241 23.425 48.525 26.885 1.00 26.07 C ATOM 6081 O ASN F 241 24.235 49.227 27.503 1.00 24.87 O ATOM 6082 CB ASN F 241 20.957 48.672 27.141 1.00 24.51 C ATOM 6083 CG ASN F 241 20.884 50.075 27.724 1.00 25.67 C ATOM 6084 OD1 ASN F 241 20.311 50.290 28.796 1.00 28.27 O ATOM 6085 ND2 ASN F 241 21.488 51.033 27.036 1.00 24.93 N ATOM 6086 N HIS F 242 23.527 48.243 25.589 1.00 25.58 N ATOM 6087 CA HIS F 242 24.613 48.730 24.747 1.00 25.88 C ATOM 6088 C HIS F 242 24.040 48.965 23.356 1.00 26.14 C ATOM 6089 O HIS F 242 23.170 48.213 22.907 1.00 25.21 O ATOM 6090 CB HIS F 242 25.726 47.695 24.656 1.00 26.14 C ATOM 6091 CG HIS F 242 26.838 48.095 23.741 1.00 26.54 C ATOM 6092 ND1 HIS F 242 27.732 49.097 24.052 1.00 26.56 N ATOM 6093 CD2 HIS F 242 27.196 47.632 22.521 1.00 27.55 C ATOM 6094 CE1 HIS F 242 28.598 49.231 23.063 1.00 28.63 C ATOM 6095 NE2 HIS F 242 28.296 48.353 22.122 1.00 28.19 N ATOM 6096 N THR F 243 24.542 49.980 22.663 1.00 25.54 N ATOM 6097 CA THR F 243 24.025 50.303 21.342 1.00 26.51 C ATOM 6098 C THR F 243 25.042 50.299 20.210 1.00 27.85 C ATOM 6099 O THR F 243 26.136 50.842 20.343 1.00 28.40 O ATOM 6100 CB THR F 243 23.316 51.690 21.356 1.00 26.25 C ATOM 6101 OG1 THR F 243 22.214 51.657 22.273 1.00 24.68 O ATOM 6102 CG2 THR F 243 22.793 52.048 19.958 1.00 26.04 C ATOM 6103 N TYR F 244 24.664 49.664 19.103 1.00 28.22 N ATOM 6104 CA TYR F 244 25.496 49.602 17.909 1.00 29.85 C ATOM 6105 C TYR F 244 24.807 50.413 16.816 1.00 31.08 C ATOM 6106 O TYR F 244 23.583 50.536 16.800 1.00 30.67 O ATOM 6107 CB TYR F 244 25.659 48.168 17.398 1.00 29.24 C ATOM 6108 CG TYR F 244 26.503 47.274 18.264 1.00 29.23 C ATOM 6109 CD1 TYR F 244 25.934 46.213 18.969 1.00 28.57 C ATOM 6110 CD2 TYR F 244 27.882 47.476 18.370 1.00 28.39 C ATOM 6111 CE1 TYR F 244 26.715 45.370 19.754 1.00 28.64 C ATOM 6112 CE2 TYR F 244 28.669 46.644 19.158 1.00 29.07 C ATOM 6113 CZ TYR F 244 28.081 45.593 19.846 1.00 28.99 C ATOM 6114 OH TYR F 244 28.859 44.775 20.630 1.00 30.62 O ATOM 6115 N HIS F 245 25.601 50.973 15.913 1.00 32.15 N ATOM 6116 CA HIS F 245 25.069 51.741 14.797 1.00 33.59 C ATOM 6117 C HIS F 245 25.457 50.986 13.534 1.00 33.68 C ATOM 6118 O HIS F 245 26.611 50.581 13.387 1.00 33.99 O ATOM 6119 CB HIS F 245 25.674 53.145 14.786 1.00 34.56 C ATOM 6120 CG HIS F 245 25.480 53.882 16.077 1.00 37.38 C ATOM 6121 ND1 HIS F 245 24.287 54.476 16.421 1.00 37.28 N ATOM 6122 CD2 HIS F 245 26.310 54.066 17.132 1.00 39.21 C ATOM 6123 CE1 HIS F 245 24.385 54.991 17.636 1.00 37.94 C ATOM 6124 NE2 HIS F 245 25.606 54.753 18.090 1.00 38.49 N ATOM 6125 N LEU F 246 24.499 50.777 12.638 1.00 33.16 N ATOM 6126 CA LEU F 246 24.778 50.063 11.399 1.00 33.00 C ATOM 6127 C LEU F 246 24.638 50.957 10.174 1.00 34.03 C ATOM 6128 O LEU F 246 23.694 51.746 10.065 1.00 34.12 O ATOM 6129 CB LEU F 246 23.842 48.854 11.246 1.00 31.62 C ATOM 6130 CG LEU F 246 23.884 48.127 9.894 1.00 31.04 C ATOM 6131 CD1 LEU F 246 25.269 47.475 9.679 1.00 30.18 C ATOM 6132 CD2 LEU F 246 22.789 47.071 9.849 1.00 29.52 C ATOM 6133 N ASP F 247 25.592 50.834 9.257 1.00 34.91 N ATOM 6134 CA ASP F 247 25.560 51.598 8.018 1.00 36.30 C ATOM 6135 C ASP F 247 25.917 50.642 6.887 1.00 36.31 C ATOM 6136 O ASP F 247 26.820 49.813 7.036 1.00 36.41 O ATOM 6137 CB ASP F 247 26.540 52.777 8.075 1.00 36.95 C ATOM 6138 CG ASP F 247 26.118 53.919 7.161 1.00 38.99 C ATOM 6139 OD1 ASP F 247 26.603 55.059 7.335 1.00 39.74 O ATOM 6140 OD2 ASP F 247 25.288 53.672 6.262 1.00 40.23 O ATOM 6141 N VAL F 248 25.196 50.740 5.771 1.00 36.55 N ATOM 6142 CA VAL F 248 25.430 49.864 4.633 1.00 36.46 C ATOM 6143 C VAL F 248 25.844 50.650 3.400 1.00 36.82 C ATOM 6144 O VAL F 248 25.231 51.664 3.070 1.00 37.84 O ATOM 6145 CB VAL F 248 24.167 49.053 4.312 1.00 36.17 C ATOM 6146 CG1 VAL F 248 24.465 48.007 3.249 1.00 34.16 C ATOM 6147 CG2 VAL F 248 23.643 48.411 5.592 1.00 35.63 C ATOM 6148 N VAL F 249 26.889 50.171 2.726 1.00 36.57 N ATOM 6149 CA VAL F 249 27.415 50.820 1.527 1.00 36.43 C ATOM 6150 C VAL F 249 27.369 49.875 0.325 1.00 36.89 C ATOM 6151 O VAL F 249 27.897 48.761 0.371 1.00 36.55 O ATOM 6152 CB VAL F 249 28.898 51.264 1.735 1.00 36.50 C ATOM 6153 CG1 VAL F 249 29.419 51.953 0.480 1.00 35.80 C ATOM 6154 CG2 VAL F 249 29.013 52.186 2.933 1.00 35.90 C ATOM 6155 N GLU F 250 26.750 50.323 −0.756 1.00 36.94 N ATOM 6156 CA GLU F 250 26.664 49.503 −1.953 1.00 36.91 C ATOM 6157 C GLU F 250 27.923 49.681 −2.792 1.00 35.51 C ATOM 6158 O GLU F 250 28.315 50.796 −3.100 1.00 35.05 O ATOM 6159 CB GLU F 250 25.419 49.902 −2.747 1.00 39.01 C ATOM 6160 CG GLU F 250 24.131 49.722 −1.952 1.00 42.23 C ATOM 6161 CD GLU F 250 22.889 50.095 −2.742 1.00 43.94 C ATOM 6162 OE1 GLU F 250 22.643 51.304 −2.949 1.00 44.73 O ATOM 6163 OE2 GLU F 250 22.165 49.169 −3.159 1.00 44.81 O ATOM 6164 N ARG F 251 28.561 48.573 −3.149 1.00 34.53 N ATOM 6165 CA ARG F 251 29.776 48.607 −3.948 1.00 33.88 C ATOM 6166 C ARG F 251 29.417 48.222 −5.380 1.00 35.00 C ATOM 6167 O ARG F 251 28.527 47.416 −5.595 1.00 34.89 O ATOM 6168 CB ARG F 251 30.804 47.628 −3.379 1.00 31.60 C ATOM 6169 CG ARG F 251 31.185 47.893 −1.923 1.00 28.57 C ATOM 6170 CD ARG F 251 31.457 49.373 −1.673 1.00 26.81 C ATOM 6171 NE ARG F 251 32.497 49.913 −2.550 1.00 24.43 N ATOM 6172 CZ ARG F 251 33.800 49.670 −2.431 1.00 22.96 C ATOM 6173 NH1 ARG F 251 34.269 48.885 −1.463 1.00 24.68 N ATOM 6174 NH2 ARG F 251 34.642 50.229 −3.280 1.00 24.66 N ATOM 6175 N SER F 252 30.098 48.796 −6.362 1.00 35.23 N ATOM 6176 CA SER F 252 29.834 48.520 −7.772 1.00 36.16 C ATOM 6177 C SER F 252 31.103 48.052 −8.482 1.00 36.13 C ATOM 6178 O SER F 252 31.930 48.859 −8.882 1.00 36.17 O ATOM 6179 CB SER F 252 29.299 49.794 −8.433 1.00 36.21 C ATOM 6180 OG SER F 252 29.342 49.697 −9.841 1.00 37.53 O ATOM 6181 N PRO F 253 31.269 46.739 −8.660 1.00 37.26 N ATOM 6182 CA PRO F 253 32.471 46.219 −9.326 1.00 37.37 C ATOM 6183 C PRO F 253 32.490 46.310 −10.859 1.00 37.89 C ATOM 6184 O PRO F 253 32.809 45.334 −11.539 1.00 39.08 O ATOM 6185 CB PRO F 253 32.539 44.784 −8.820 1.00 38.19 C ATOM 6186 CG PRO F 253 31.080 44.407 −8.743 1.00 37.95 C ATOM 6187 CD PRO F 253 30.429 45.643 −8.134 1.00 37.11 C ATOM 6188 N HIS F 254 32.153 47.479 −11.400 1.00 37.46 N ATOM 6189 CA HIS F 254 32.164 47.669 −12.847 1.00 37.94 C ATOM 6190 C HIS F 254 33.273 48.623 −13.293 1.00 36.74 C ATOM 6191 O HIS F 254 33.769 49.419 −12.504 1.00 36.07 O ATOM 6192 CB HIS F 254 30.828 48.236 −13.339 1.00 39.88 C ATOM 6193 CG HIS F 254 29.663 47.320 −13.131 1.00 43.40 C ATOM 6194 ND1 HIS F 254 28.911 47.319 −11.973 1.00 45.10 N ATOM 6195 CD2 HIS F 254 29.129 46.364 −13.928 1.00 43.84 C ATOM 6196 CE1 HIS F 254 27.962 46.404 −12.068 1.00 44.84 C ATOM 6197 NE2 HIS F 254 28.072 45.811 −13.244 1.00 45.80 N ATOM 6198 N ARG F 255 33.665 48.530 −14.559 1.00 35.84 N ATOM 6199 CA ARG F 255 34.663 49.440 −15.092 1.00 35.46 C ATOM 6200 C ARG F 255 33.904 50.769 −15.210 1.00 34.55 C ATOM 6201 O ARG F 255 32.676 50.787 −15.132 1.00 34.11 O ATOM 6202 CB ARG F 255 35.151 48.974 −16.463 1.00 37.28 C ATOM 6203 CG ARG F 255 34.118 49.080 −17.581 1.00 39.45 C ATOM 6204 CD ARG F 255 34.768 48.839 −18.938 1.00 41.55 C ATOM 6205 NE ARG F 255 33.868 49.155 −20.044 1.00 43.96 N ATOM 6206 CZ ARG F 255 32.917 48.343 −20.504 1.00 45.46 C ATOM 6207 NH1 ARG F 255 32.733 47.144 −19.959 1.00 45.92 N ATOM 6208 NH2 ARG F 255 32.133 48.741 −21.499 1.00 46.26 N ATOM 6209 N PRO F 256 34.617 51.895 −15.389 1.00 33.51 N ATOM 6210 CA PRO F 256 33.905 53.176 −15.498 1.00 32.69 C ATOM 6211 C PRO F 256 32.861 53.255 −16.609 1.00 31.51 C ATOM 6212 O PRO F 256 33.050 52.718 −17.692 1.00 31.64 O ATOM 6213 CB PRO F 256 35.037 54.201 −15.656 1.00 32.52 C ATOM 6214 CG PRO F 256 36.175 53.394 −16.206 1.00 34.71 C ATOM 6215 CD PRO F 256 36.072 52.086 −15.469 1.00 33.91 C ATOM 6216 N ILE F 257 31.749 53.917 −16.313 1.00 31.13 N ATOM 6217 CA ILE F 257 30.666 54.087 −17.274 1.00 31.66 C ATOM 6218 C ILE F 257 30.536 55.570 −17.682 1.00 31.23 C ATOM 6219 O ILE F 257 30.545 56.453 −16.826 1.00 30.88 O ATOM 6220 CB ILE F 257 29.349 53.559 −16.662 1.00 32.97 C ATOM 6221 CG1 ILE F 257 29.440 52.035 −16.513 1.00 33.66 C ATOM 6222 CG2 ILE F 257 28.168 53.949 −17.520 1.00 33.20 C ATOM 6223 CD1 ILE F 257 28.245 51.397 −15.849 1.00 35.77 C ATOM 6224 N LEU F 258 30.459 55.836 −18.987 1.00 30.39 N ATOM 6225 CA LEU F 258 30.332 57.212 −19.481 1.00 31.22 C ATOM 6226 C LEU F 258 28.921 57.482 −19.989 1.00 31.52 C ATOM 6227 O LEU F 258 28.228 56.570 −20.453 1.00 30.67 O ATOM 6228 CB LEU F 258 31.300 57.502 −20.638 1.00 30.74 C ATOM 6229 CG LEU F 258 32.788 57.122 −20.641 1.00 33.91 C ATOM 6230 CD1 LEU F 258 33.515 58.017 −21.628 1.00 32.56 C ATOM 6231 CD2 LEU F 258 33.403 57.258 −19.266 1.00 33.90 C ATOM 6232 N GLN F 259 28.504 58.740 −19.917 1.00 31.91 N ATOM 6233 CA GLN F 259 27.183 59.120 −20.396 1.00 32.58 C ATOM 6234 C GLN F 259 27.157 59.096 −21.928 1.00 32.23 C ATOM 6235 O GLN F 259 28.054 59.630 −22.585 1.00 31.49 O ATOM 6236 CB GLN F 259 26.818 60.517 −19.911 1.00 33.90 C ATOM 6237 CG GLN F 259 25.487 61.010 −20.429 1.00 36.31 C ATOM 6238 CD GLN F 259 25.313 62.486 −20.182 1.00 38.12 C ATOM 6239 OE1 GLN F 259 25.448 62.954 −19.055 1.00 39.31 O ATOM 6240 NE2 GLN F 259 25.017 63.234 −21.237 1.00 39.46 N ATOM 6241 N ALA F 260 26.128 58.475 −22.492 1.00 31.76 N ATOM 6242 CA ALA F 260 26.003 58.406 −23.946 1.00 32.37 C ATOM 6243 C ALA F 260 25.815 59.798 −24.551 1.00 32.72 C ATOM 6244 O ALA F 260 25.125 60.644 −23.986 1.00 32.74 O ATOM 6245 CB ALA F 260 24.836 57.495 −24.337 1.00 32.31 C ATOM 6246 N GLY F 261 26.448 60.033 −25.697 1.00 32.61 N ATOM 6247 CA GLY F 261 26.335 61.326 −26.350 1.00 33.50 C ATOM 6248 C GLY F 261 27.459 62.302 −26.036 1.00 34.44 C ATOM 6249 O GLY F 261 27.607 63.312 −26.722 1.00 34.82 O ATOM 6250 N LEU F 262 28.251 62.011 −25.006 1.00 34.98 N ATOM 6251 CA LEU F 262 29.355 62.891 −24.617 1.00 34.75 C ATOM 6252 C LEU F 262 30.702 62.179 −24.682 1.00 35.24 C ATOM 6253 O LEU F 262 30.838 61.045 −24.233 1.00 35.56 O ATOM 6254 CB LEU F 262 29.132 63.427 −23.201 1.00 34.91 C ATOM 6255 CG LEU F 262 27.927 64.352 −22.989 1.00 35.98 C ATOM 6256 CD1 LEU F 262 27.868 64.788 −21.524 1.00 33.73 C ATOM 6257 CD2 LEU F 262 28.049 65.581 −23.898 1.00 34.07 C ATOM 6258 N PRO F 263 31.719 62.840 −25.252 1.00 36.31 N ATOM 6259 CA PRO F 263 31.645 64.190 −25.821 1.00 36.64 C ATOM 6260 C PRO F 263 30.835 64.242 −27.118 1.00 37.59 C ATOM 6261 O PRO F 263 30.571 63.214 −27.744 1.00 37.44 O ATOM 6262 CB PRO F 263 33.114 64.546 −26.041 1.00 36.68 C ATOM 6263 CG PRO F 263 33.717 63.220 −26.402 1.00 35.47 C ATOM 6264 CD PRO F 263 33.079 62.284 −25.395 1.00 35.79 C ATOM 6265 N ALA F 264 30.446 65.444 −27.518 1.00 38.85 N ATOM 6266 CA ALA F 264 29.673 65.619 −28.742 1.00 40.21 C ATOM 6267 C ALA F 264 30.528 66.217 −29.850 1.00 40.87 C ATOM 6268 O ALA F 264 31.480 66.958 −29.588 1.00 41.01 O ATOM 6269 CB ALA F 264 28.456 66.512 −28.477 1.00 40.32 C ATOM 6270 N ASN F 265 30.192 65.881 −31.093 1.00 42.16 N ATOM 6271 CA ASN F 265 30.925 66.408 −32.237 1.00 43.51 C ATOM 6272 C ASN F 265 30.826 67.928 −32.203 1.00 44.31 C ATOM 6273 O ASN F 265 29.859 68.485 −31.678 1.00 44.07 O ATOM 6274 CB ASN F 265 30.334 65.901 −33.560 1.00 43.88 C ATOM 6275 CG ASN F 265 30.430 64.392 −33.709 1.00 45.38 C ATOM 6276 OD1 ASN F 265 31.428 63.776 −33.337 1.00 43.80 O ATOM 6277 ND2 ASN F 265 29.392 63.792 −34.277 1.00 46.59 N ATOM 6278 N ALA F 266 31.832 68.595 −32.753 1.00 45.27 N ATOM 6279 CA ALA F 266 31.835 70.052 −32.792 1.00 46.52 C ATOM 6280 C ALA F 266 32.421 70.556 −34.111 1.00 47.37 C ATOM 6281 O ALA F 266 33.250 69.883 −34.732 1.00 47.43 O ATOM 6282 CB ALA F 266 32.623 70.610 −31.609 1.00 45.85 C ATOM 6283 N SER F 267 31.968 71.734 −34.532 1.00 49.00 N ATOM 6284 CA SER F 267 32.423 72.370 −35.771 1.00 51.19 C ATOM 6285 C SER F 267 32.706 73.849 −35.469 1.00 52.95 C ATOM 6286 O SER F 267 31.914 74.499 −34.782 1.00 53.04 O ATOM 6287 CB SER F 267 31.340 72.264 −36.853 1.00 50.75 C ATOM 6288 N THR F 268 33.844 74.373 −35.941 1.00 55.40 N ATOM 6289 CA THR F 268 34.232 75.777 −35.692 1.00 58.15 C ATOM 6290 C THR F 268 34.768 76.485 −36.953 1.00 59.75 C ATOM 6291 O THR F 268 34.357 76.170 −38.069 1.00 60.60 O ATOM 6292 CB THR F 268 35.320 75.880 −34.580 1.00 58.09 C ATOM 6293 OG1 THR F 268 34.939 75.080 −33.455 1.00 59.93 O ATOM 6294 CG2 THR F 268 35.477 77.321 −34.105 1.00 58.09 C ATOM 6295 H VAL F 269 35.698 77.424 −36.775 1.00 61.40 N ATOM 6296 CA VAL F 269 36.251 78.165 −37.901 1.00 62.82 C ATOM 6297 C VAL F 269 37.752 78.435 −37.833 1.00 64.22 C ATOM 6298 O VAL F 269 38.540 77.810 −38.553 1.00 64.66 O ATOM 6299 CB VAL F 269 35.531 79.508 −38.057 1.00 62.42 C ATOM 6300 N VAL F 270 38.153 79.376 −36.985 1.00 65.60 N ATOM 6301 CA VAL F 270 39.572 79.711 −36.876 1.00 66.74 C ATOM 6302 C VAL F 270 39.911 80.441 −35.578 1.00 67.67 C ATOM 6303 O VAL F 270 41.053 80.815 −35.342 1.00 67.88 O ATOM 6304 CB VAL F 270 40.035 80.596 −38.049 1.00 66.63 C ATOM 6305 N GLY F 271 38.909 80.640 −34.738 1.00 68.56 N ATOM 6306 CA GLY F 271 39.123 81.314 −33.470 1.00 69.14 C ATOM 6307 C GLY F 271 38.476 80.536 −32.347 1.00 70.00 C ATOM 6308 O GLY F 271 38.561 79.312 −32.314 1.00 70.36 O ATOM 6309 N ASP F 273 36.760 78.957 −30.970 1.00 53.40 N ATOM 6310 CA ASP F 273 36.988 78.210 −29.739 1.00 53.60 C ATOM 6311 C ASP F 273 35.983 77.068 −29.585 1.00 53.06 C ATOM 6312 O ASP F 273 34.844 77.157 −30.052 1.00 53.49 O ATOM 6313 CB ASP F 273 36.917 79.147 −28.527 1.00 54.74 C ATOM 6314 CG ASP F 273 38.227 79.891 −28.287 1.00 56.07 C ATOM 6315 OD1 ASP F 273 38.832 80.363 −29.271 1.00 56.61 O ATOM 6316 OD2 ASP F 273 38.649 80.014 −27.116 1.00 55.76 O ATOM 6317 N VAL F 274 36.408 75.991 −28.929 1.00 51.73 N ATOM 6318 CA VAL F 274 35.535 74.839 −28.740 1.00 50.50 C ATOM 6319 C VAL F 274 35.823 74.060 −27.455 1.00 49.86 C ATOM 6320 O VAL F 274 36.870 74.227 −26.824 1.00 49.68 O ATOM 6321 CB VAL F 274 35.653 73.865 −29.931 1.00 50.21 C ATOM 6322 CG1 VAL F 274 36.962 73.093 −29.849 1.00 49.57 C ATOM 6323 CG2 VAL F 274 34.466 72.925 −29.949 1.00 51.04 C ATOM 6324 N GLU F 275 34.880 73.208 −27.070 1.00 49.12 N ATOM 6325 CA GLU F 275 35.046 72.382 −25.888 1.00 48.19 C ATOM 6326 C GLU F 275 34.438 71.004 −26.089 1.00 47.10 C ATOM 6327 O GLU F 275 33.559 70.808 −26.928 1.00 47.91 O ATOM 6328 CB GLU F 275 34.413 73.037 −24.663 1.00 48.81 C ATOM 6329 CG GLU F 275 32.915 73.193 −24.749 1.00 49.77 C ATOM 6330 CD GLU F 275 32.298 73.481 −23.397 1.00 50.13 C ATOM 6331 OE1 GLU F 275 32.974 74.114 −22.553 1.00 50.91 O ATOM 6332 OE2 GLU F 275 31.136 73.083 −23.185 1.00 50.57 O ATOM 6333 N PHE F 276 34.934 70.050 −25.312 1.00 45.40 N ATOM 6334 CA PHE F 276 34.458 68.680 −25.342 1.00 42.98 C ATOM 6335 C PHE F 276 34.182 68.306 −23.899 1.00 41.88 C ATOM 6336 O PHE F 276 35.051 68.445 −23.042 1.00 40.61 O ATOM 6337 CB PHE F 276 35.529 67.759 −25.918 1.00 44.18 C ATOM 6338 CG PHE F 276 35.672 67.858 −27.405 1.00 45.07 C ATOM 6339 CD1 PHE F 276 34.645 67.426 −28.242 1.00 45.08 C ATOM 6340 CD2 PHE F 276 36.838 68.367 −27.972 1.00 45.06 C ATOM 6341 CE1 PHE F 276 34.776 67.496 −29.625 1.00 46.84 C ATOM 6342 CE2 PHE F 276 36.985 68.443 −29.352 1.00 46.77 C ATOM 6343 CZ PHE F 276 35.950 68.006 −30.187 1.00 46.46 C ATOM 6344 N VAL F 277 32.969 67.842 −23.630 1.00 40.76 N ATOM 6345 CA VAL F 277 32.597 67.471 −22.278 1.00 40.08 C ATOM 6346 C VAL F 277 32.449 65.969 −22.130 1.00 39.86 C ATOM 6347 O VAL F 277 32.090 65.262 −23.075 1.00 40.39 O ATOM 6348 CB VAL F 277 31.283 68.161 −21.857 1.00 39.97 C ATOM 6349 CG1 VAL F 277 30.900 67.749 −20.444 1.00 40.02 C ATOM 6350 CG2 VAL F 277 31.451 69.675 −21.935 1.00 40.07 C ATOM 6351 N CYS F 278 32.735 65.483 −20.932 1.00 38.84 N ATOM 6352 CA CYS F 278 32.625 64.068 −20.649 1.00 38.38 C ATOM 6353 C CYS F 278 32.048 63.891 −19.253 1.00 37.50 C ATOM 6354 O CYS F 278 32.347 64.685 −18.361 1.00 37.83 O ATOM 6355 CB CYS F 278 33.999 63.410 −20.730 1.00 39.41 C ATOM 6356 SG CYS F 278 33.903 61.622 −20.662 1.00 42.56 S ATOM 6357 N LYS F 279 31.217 62.865 −19.068 1.00 35.92 N ATOM 6358 CA LYS F 279 30.609 62.579 −17.764 1.00 34.91 C ATOM 6359 C LYS F 279 30.873 61.137 −17.332 1.00 33.60 C ATOM 6360 O LYS F 279 30.325 60.190 −17.921 1.00 32.70 O ATOM 6361 CB LYS F 279 29.094 62.816 −17.798 1.00 35.37 C ATOM 6362 CG LYS F 279 28.663 64.219 −17.399 1.00 38.47 C ATOM 6363 CD LYS F 279 29.108 64.582 −15.965 1.00 37.93 C ATOM 6364 CE LYS F 279 28.428 63.709 −14.913 1.00 38.82 C ATOM 6365 NZ LYS F 279 28.779 64.089 −13.513 1.00 37.70 N ATOM 6366 N VAL F 280 31.679 60.977 −16.281 1.00 31.94 N ATOM 6367 CA VAL F 280 32.053 59.653 −15.778 1.00 29.99 C ATOM 6368 C VAL F 280 31.469 59.231 −14.432 1.00 30.83 C ATOM 6369 O VAL F 280 31.258 60.050 −13.534 1.00 30.77 O ATOM 6370 CB VAL F 280 33.600 59.531 −15.683 1.00 29.69 C ATOM 6371 CG1 VAL F 280 33.992 58.184 −15.095 1.00 29.19 C ATOM 6372 CG2 VAL F 280 34.231 59.738 −17.073 1.00 28.52 C ATOM 6373 N TYR F 281 31.213 57.931 −14.310 1.00 31.35 N ATOM 6374 CA TYR F 281 30.701 57.320 −13.082 1.00 32.39 C ATOM 6375 C TYR F 281 31.546 56.084 −12.767 1.00 30.82 C ATOM 6376 O TYR F 281 31.819 55.279 −13.652 1.00 31.49 O ATOM 6377 CB TYR F 281 29.246 56.882 −13.239 1.00 35.65 C ATOM 6378 CG TYR F 281 28.314 57.977 −13.697 1.00 39.56 C ATOM 6379 CD1 TYR F 281 28.202 58.313 −15.054 1.00 41.11 C ATOM 6380 CD2 TYR F 281 27.532 58.672 −12.779 1.00 41.01 C ATOM 6381 CE1 TYR F 281 27.330 59.311 −15.479 1.00 42.28 C ATOM 6382 CE2 TYR F 281 26.658 59.675 −13.195 1.00 43.31 C ATOM 6383 CZ TYR F 281 26.560 59.986 −14.546 1.00 43.29 C ATOM 6384 OH TYR F 281 25.675 60.962 −14.951 1.00 45.14 O ATOM 6385 N SER F 282 31.958 55.935 −11.516 1.00 29.47 N ATOM 6386 CA SER F 282 32.762 54.789 −11.105 1.00 28.89 C ATOM 6387 C SER F 282 32.877 54.700 −9.579 1.00 28.68 C ATOM 6388 O SER F 282 32.899 55.722 −8.897 1.00 28.67 O ATOM 6389 CB SER F 282 34.158 54.890 −11.734 1.00 28.94 C ATOM 6390 OG SER F 282 35.021 53.879 −11.237 1.00 28.16 O ATOM 6391 N ASP F 283 32.940 53.478 −9.050 1.00 28.16 N ATOM 6392 CA ASP F 283 33.070 53.258 −7.605 1.00 27.16 C ATOM 6393 C ASP F 283 34.568 53.311 −7.323 1.00 27.79 C ATOM 6394 O ASP F 283 35.035 54.178 −6.589 1.00 27.96 O ATOM 6395 CB ASP F 283 32.502 51.890 −7.229 1.00 26.32 C ATOM 6396 CG ASP F 283 32.484 51.639 −5.723 1.00 25.14 C ATOM 6397 OD1 ASP F 283 31.759 50.709 −5.315 1.00 25.10 O ATOM 6398 OD2 ASP F 283 33.175 52.338 −4.947 1.00 22.71 O ATOM 6399 N ALA F 284 35.310 52.376 −7.918 1.00 27.44 N ATOM 6400 CA ALA F 284 36.757 52.357 −7.786 1.00 27.90 C ATOM 6401 C ALA F 284 37.213 53.672 −8.427 1.00 27.70 C ATOM 6402 O ALA F 284 36.701 54.064 −9.481 1.00 27.71 O ATOM 6403 CB ALA F 284 37.349 51.171 −8.552 1.00 27.12 C ATOM 6404 N GLN F 285 38.159 54.356 −7.795 1.00 26.74 N ATOM 6405 CA GLN F 285 38.652 55.631 −8.327 1.00 27.03 C ATOM 6406 C GLN F 285 39.040 55.505 −9.810 1.00 25.88 C ATOM 6407 O GLN F 285 39.871 54.673 −10.180 1.00 25.70 O ATOM 6408 CB GLN F 285 39.842 56.111 −7.487 1.00 26.84 C ATOM 6409 CG GLN F 285 39.982 57.622 −7.332 1.00 27.07 C ATOM 6410 CD GLN F 285 38.761 58.293 −6.718 1.00 26.94 C ATOM 6411 OE1 GLN F 285 38.175 57.792 −5.760 1.00 25.31 O ATOM 6412 NE2 GLN F 285 38.381 59.452 −7.269 1.00 27.07 N ATOM 6413 N PRO F 286 38.422 56.327 −10.677 1.00 26.08 N ATOM 6414 CA PRO F 286 38.702 56.308 −12.117 1.00 26.74 C ATOM 6415 C PRO F 286 39.795 57.301 −12.539 1.00 27.03 C ATOM 6416 O PRO F 286 39.980 58.335 −11.902 1.00 27.72 O ATOM 6417 CB PRO F 286 37.338 56.653 −12.726 1.00 26.78 C ATOM 6418 CG PRO F 286 36.815 57.707 −11.769 1.00 26.69 C ATOM 6419 CD PRO F 286 37.252 57.182 −10.376 1.00 26.14 C ATOM 6420 N HIS F 287 40.518 56.976 −13.606 1.00 27.57 N ATOM 6421 CA HIS F 287 41.559 57.854 −14.119 1.00 27.86 C ATOM 6422 C HIS F 287 41.125 58.318 −15.508 1.00 28.19 C ATOM 6423 O HIS F 287 40.935 57.510 −16.423 1.00 27.70 O ATOM 6424 CB HIS F 287 42.904 57.142 −14.188 1.00 28.47 C ATOM 6425 CG HIS F 287 44.023 58.038 −14.607 1.00 30.28 C ATOM 6426 ND1 HIS F 287 44.491 58.089 −15.902 1.00 30.79 N ATOM 6427 CD2 HIS F 287 44.723 58.971 −13.915 1.00 29.73 C ATOM 6428 CE1 HIS F 287 45.430 59.015 −15.993 1.00 31.36 C ATOM 6429 NE2 HIS F 287 45.588 59.568 −14.802 1.00 30.56 N ATOM 6430 N ILE F 288 40.948 59.626 −15.644 1.00 27.95 N ATOM 6431 CA ILE F 288 40.477 60.214 −16.890 1.00 28.99 C ATOM 6432 C ILE F 288 41.541 60.990 −17.665 1.00 30.28 C ATOM 6433 O ILE F 288 42.351 61.713 −17.084 1.00 30.94 O ATOM 6434 CB ILE F 288 39.277 61.150 −16.600 1.00 27.26 C ATOM 6435 CG1 ILE F 288 38.228 60.385 −15.786 1.00 27.85 C ATOM 6436 CG2 ILE F 288 38.678 61.671 −17.889 1.00 27.58 C ATOM 6437 CD1 ILE F 288 37.120 61.269 −15.233 1.00 24.83 C ATOM 6438 N GLN F 289 41.537 60.823 −18.982 1.00 31.52 N ATOM 6439 CA GLN F 289 42.470 61.533 −19.849 1.00 33.66 C ATOM 6440 C GLN F 289 41.800 61.828 −21.185 1.00 33.68 C ATOM 6441 O GLN F 289 40.826 61.175 −21.560 1.00 33.89 O ATOM 6442 CB GLN F 289 43.757 60.715 −20.065 1.00 35.33 C ATOM 6443 CG GLN F 289 43.567 59.332 −20.668 1.00 37.11 C ATOM 6444 CD GLN F 289 44.875 58.559 −20.767 1.00 39.44 C ATOM 6445 OE1 GLN F 289 45.823 59.003 −21.418 1.00 41.60 O ATOM 6446 NE2 GLN F 289 44.934 57.397 −20.119 1.00 39.39 N ATOM 6447 N TRP F 290 42.307 62.838 −21.879 1.00 34.29 N ATOM 6448 CA TRP F 290 41.785 63.227 −23.182 1.00 35.09 C ATOM 6449 C TRP F 290 42.849 62.919 −24.225 1.00 36.73 C ATOM 6450 O TRP F 290 44.013 63.311 −24.073 1.00 36.45 O ATOM 6451 CB TRP F 290 41.442 64.720 −23.205 1.00 34.27 C ATOM 6452 CG TRP F 290 40.162 65.060 −22.494 1.00 33.19 C ATOM 6453 CD1 TRP F 290 40.019 65.480 −21.202 1.00 33.69 C ATOM 6454 CD2 TRP F 290 38.839 65.012 −23.048 1.00 32.32 C ATOM 6455 NE1 TRP F 290 38.688 65.702 −20.916 1.00 31.67 N ATOM 6456 CE2 TRP F 290 37.944 65.419 −22.030 1.00 32.16 C ATOM 6457 CE3 TRP F 290 38.325 64.661 −24.300 1.00 32.46 C ATOM 6458 CZ2 TRP F 290 36.565 65.488 −22.229 1.00 31.05 C ATOM 6459 CZ3 TRP F 290 36.953 64.730 −24.501 1.00 32.67 C ATOM 6460 CH2 TRP F 290 36.088 65.141 −23.466 1.00 33.18 C ATOM 6461 N ILE F 291 42.448 62.217 −25.281 1.00 38.06 N ATOM 6462 CA ILE F 291 43.372 61.828 −26.336 1.00 40.00 C ATOM 6463 C ILE F 291 42.960 62.279 −27.740 1.00 41.89 C ATOM 6464 O ILE F 291 41.778 62.297 −28.086 1.00 42.04 O ATOM 6465 CB ILE F 291 43.551 60.297 −26.352 1.00 39.88 C ATOM 6466 CG1 ILE F 291 44.070 59.823 −24.988 1.00 39.61 C ATOM 6467 CG2 ILE F 291 44.500 59.891 −27.473 1.00 39.23 C ATOM 6468 CD1 ILE F 291 44.104 58.317 −24.832 1.00 40.37 C ATOM 6469 N LYS F 292 43.956 62.641 −28.542 1.00 43.38 N ATOM 6470 CA LYS F 292 43.734 63.066 −29.918 1.00 45.28 C ATOM 6471 C LYS F 292 44.359 62.001 −30.811 1.00 46.12 C ATOM 6472 O LYS F 292 45.498 61.586 −30.585 1.00 46.03 O ATOM 6473 CB LYS F 292 44.397 64.416 −30.166 1.00 45.89 C ATOM 6474 CG LYS F 292 43.655 65.304 −31.149 1.00 47.53 C ATOM 6475 CD LYS F 292 44.127 65.104 −32.576 1.00 48.59 C ATOM 6476 CE LYS F 292 43.530 66.187 −33.472 1.00 48.61 C ATOM 6477 NZ LYS F 292 44.350 66.408 −34.692 1.00 49.06 N ATOM 6478 N HIS F 293 43.603 61.546 −31.804 1.00 47.10 N ATOM 6479 CA HIS F 293 44.085 60.517 −32.719 1.00 47.96 C ATOM 6480 C HIS F 293 44.955 61.142 −33.804 1.00 47.99 C ATOM 6481 O HIS F 293 44.450 61.845 −34.678 1.00 48.84 O ATOM 6482 CB HIS F 293 42.897 59.790 −33.358 1.00 47.51 C ATOM 6483 N TYR F 308 48.337 55.850 −33.701 1.00 56.86 N ATOM 6484 CA TYR F 308 49.140 56.969 −33.210 1.00 56.77 C ATOM 6485 C TYR F 308 48.287 57.894 −32.341 1.00 56.10 C ATOM 6486 O TYR F 308 47.397 58.586 −32.841 1.00 56.75 O ATOM 6487 CB TYR F 308 49.724 57.759 −34.387 1.00 56.75 C ATOM 6488 N LEU F 309 48.575 57.916 −31.044 1.00 54.88 N ATOM 6489 CA LEU F 309 47.818 58.737 −30.108 1.00 53.64 C ATOM 6490 C LEU F 309 48.662 59.831 −29.461 1.00 52.36 C ATOM 6491 O LEU F 309 49.884 59.709 −29.362 1.00 52.73 O ATOM 6492 CB LEU F 309 47.231 57.836 −29.025 1.00 53.75 C ATOM 6493 CG LEU F 309 46.554 56.586 −29.590 1.00 54.37 C ATOM 6494 CD1 LEU F 309 46.186 55.641 −28.454 1.00 55.15 C ATOM 6495 CD2 LEU F 309 45.330 56.990 −30.403 1.00 54.08 C ATOM 6496 N LYS F 310 48.002 60.898 −29.026 1.00 50.33 N ATOM 6497 CA LYS F 310 48.675 62.011 −28.361 1.00 48.17 C ATOM 6498 C LYS F 310 47.847 62.434 −27.150 1.00 46.65 C ATOM 6499 O LYS F 310 46.684 62.822 −27.291 1.00 45.61 O ATOM 6500 CB LYS F 310 48.826 63.194 −29.316 1.00 48.37 C ATOM 6501 N VAL F 311 48.449 62.362 −25.964 1.00 44.95 N ATOM 6502 CA VAL F 311 47.753 62.729 −24.731 1.00 43.52 C ATOM 6503 C VAL F 311 47.706 64.238 −24.530 1.00 42.93 C ATOM 6504 O VAL F 311 48.733 64.881 −24.312 1.00 43.27 O ATOM 6505 CB VAL F 311 48.422 62.093 −23.486 1.00 43.34 C ATOM 6506 CG1 VAL F 311 47.686 62.534 −22.219 1.00 41.56 C ATOM 6507 CG2 VAL F 311 48.420 60.575 −23.608 1.00 42.02 C ATOM 6508 N LEU F 312 46.505 64.798 −24.588 1.00 41.63 N ATOM 6509 CA LEU F 312 46.342 66.233 −24.417 1.00 40.85 C ATOM 6510 C LEU F 312 46.282 66.655 −22.962 1.00 39.66 C ATOM 6511 O LEU F 312 46.784 67.714 −22.597 1.00 39.35 O ATOM 6512 CB LEU F 312 45.061 66.709 −25.108 1.00 41.96 C ATOM 6513 CG LEU F 312 44.861 66.260 −26.556 1.00 43.95 C ATOM 6514 CD1 LEU F 312 43.761 67.101 −27.185 1.00 43.41 C ATOM 6515 CD2 LEU F 312 46.163 66.417 −27.342 1.00 44.19 C ATOM 6516 N LYS F 313 45.679 65.812 −22.131 1.00 38.22 N ATOM 6517 CA LYS F 313 45.478 66.140 −20.730 1.00 37.23 C ATOM 6518 C LYS F 313 45.204 64.855 −19.957 1.00 36.19 C ATOM 6519 O LYS F 313 44.510 63.969 −20.462 1.00 36.44 O ATOM 6520 CB LYS F 313 44.261 67.069 −20.661 1.00 37.39 C ATOM 6521 CG LYS F 313 43.925 67.678 −19.334 1.00 38.92 C ATOM 6522 CD LYS F 313 42.674 68.528 −19.501 1.00 39.81 C ATOM 6523 CE LYS F 313 42.284 69.241 −18.217 1.00 41.61 C ATOM 6524 NZ LYS F 313 40.973 69.945 −18.387 1.00 41.89 N ATOM 6525 N ALA F 314 45.731 64.755 −18.738 1.00 33.97 N ATOM 6526 CA ALA F 314 45.535 63.563 −17.917 1.00 32.58 C ATOM 6527 C ALA F 314 45.420 63.900 −16.432 1.00 32.38 C ATOM 6528 O ALA F 314 46.160 64.752 −15.911 1.00 31.85 O ATOM 6529 CB ALA F 314 46.674 62.590 −18.148 1.00 32.22 C ATOM 6530 N ALA F 315 44.486 63.229 −15.757 1.00 31.35 N ATOM 6531 CA ALA F 315 44.232 63.436 −14.331 1.00 30.87 C ATOM 6532 C ALA F 315 45.429 63.080 −13.452 1.00 30.61 C ATOM 6533 O ALA F 315 46.245 62.226 −13.804 1.00 30.29 O ATOM 6534 CB ALA F 315 43.004 62.623 −13.891 1.00 30.19 C ATOM 6535 N GLY F 316 45.520 63.750 −12.309 1.00 30.74 N ATOM 6536 CA GLY F 316 46.598 63.512 −11.374 1.00 32.31 C ATOM 6537 C GLY F 316 46.654 64.590 −10.309 1.00 34.07 C ATOM 6538 O GLY F 316 45.778 65.449 −10.234 1.00 33.07 O ATOM 6539 N VAL F 317 47.686 64.535 −9.479 1.00 35.99 N ATOM 6540 CA VAL F 317 47.876 65.509 −8.412 1.00 38.96 C ATOM 6541 C VAL F 317 47.938 66.947 −8.941 1.00 39.46 C ATOM 6542 O VAL F 317 47.459 67.868 −8.291 1.00 39.05 O ATOM 6543 CB VAL F 317 49.170 65.196 −7.629 1.00 39.98 C ATOM 6544 CG1 VAL F 317 49.543 66.364 −6.738 1.00 42.38 C ATOM 6545 CG2 VAL F 317 48.962 63.936 −6.776 1.00 40.44 C ATOM 6546 N ASN F 318 48.519 67.127 −10.124 1.00 41.29 N ATOM 6547 CA ASN F 318 48.641 68.457 −10.716 1.00 43.00 C ATOM 6548 C ASN F 318 47.511 68.828 −11.665 1.00 43.30 C ATOM 6549 O ASN F 318 47.473 69.939 −12.184 1.00 43.85 O ATOM 6550 CB ASN F 318 49.977 68.598 −11.442 1.00 44.26 C ATOM 6551 CG ASN F 318 51.132 68.755 −10.482 1.00 45.68 C ATOM 6552 OD1 ASN F 318 51.083 69.578 −9.571 1.00 46.62 O ATOM 6553 ND2 ASN F 318 52.182 67.968 −10.680 1.00 47.19 N ATOM 6554 N THR F 319 46.603 67.891 −11.901 1.00 42.99 N ATOM 6555 CA THR F 319 45.457 68.141 −12.765 1.00 42.33 C ATOM 6556 C THR F 319 44.283 67.370 −12.167 1.00 41.92 C ATOM 6557 O THR F 319 43.915 66.291 −12.637 1.00 41.66 O ATOM 6558 CB THR F 319 45.709 67.671 −14.218 1.00 42.29 C ATOM 6559 OG1 THR F 319 46.962 68.179 −14.689 1.00 42.83 O ATOM 6560 CG2 THR F 319 44.618 68.191 −15.126 1.00 41.88 C ATOM 6561 N THR F 320 43.721 67.951 −11.114 1.00 41.14 N ATOM 6562 CA THR F 320 42.604 67.406 −10.347 1.00 40.93 C ATOM 6563 C THR F 320 41.342 67.029 −11.133 1.00 40.66 C ATOM 6564 O THR F 320 41.114 67.531 −12.234 1.00 40.21 O ATOM 6565 CB THR F 320 42.246 68.416 −9.215 1.00 40.83 C ATOM 6566 OG1 THR F 320 43.268 68.369 −8.217 1.00 41.48 O ATOM 6567 CG2 THR F 320 40.905 68.104 −8.572 1.00 41.34 C ATOM 6568 N ASP F 321 40.530 66.141 −10.550 1.00 39.85 N ATOM 6569 CA ASP F 321 39.279 65.691 −11.164 1.00 40.39 C ATOM 6570 C ASP F 321 38.250 66.816 −11.303 1.00 40.53 C ATOM 6571 O ASP F 321 37.332 66.725 −12.117 1.00 40.60 O ATOM 6572 CB ASP F 321 38.623 64.566 −10.341 1.00 40.53 C ATOM 6573 CG ASP F 321 39.375 63.252 −10.417 1.00 40.72 C ATOM 6574 OD1 ASP F 321 40.091 63.029 −11.411 1.00 40.02 O ATOM 6575 OD2 ASP F 321 39.230 62.434 −9.483 1.00 40.69 O ATOM 6576 N LYS F 322 38.389 67.863 −10.497 1.00 40.77 N ATOM 6577 CA LYS F 322 37.443 68.979 −10.526 1.00 40.58 C ATOM 6578 C LYS F 322 37.221 69.549 −11.922 1.00 40.18 C ATOM 6579 O LYS F 322 36.099 69.875 −12.291 1.00 40.21 O ATOM 6580 CB LYS F 322 37.914 70.098 −9.589 1.00 40.95 C ATOM 6581 N GLU F 323 38.288 69.653 −12.704 1.00 40.02 N ATOM 6582 CA GLU F 323 38.184 70.221 −14.046 1.00 40.16 C ATOM 6583 C GLU F 323 38.671 69.305 −15.174 1.00 40.12 C ATOM 6584 O GLU F 323 38.862 69.755 −16.308 1.00 39.87 O ATOM 6585 CB GLU F 323 38.971 71.537 −14.096 1.00 40.79 C ATOM 6586 N ILE F 324 38.856 68.024 −14.872 1.00 39.58 N ATOM 6587 CA ILE F 324 39.353 67.066 −15.857 1.00 38.68 C ATOM 6588 C ILE F 324 38.302 66.638 −16.897 1.00 37.55 C ATOM 6589 O ILE F 324 38.649 66.236 −18.002 1.00 36.91 O ATOM 6590 CB ILE F 324 39.925 65.801 −15.118 1.00 39.46 C ATOM 6591 CG1 ILE F 324 41.225 65.329 −15.772 1.00 40.20 C ATOM 6592 CG2 ILE F 324 38.890 64.689 −15.079 1.00 39.11 C ATOM 6593 CD1 ILE F 324 41.097 64.896 −17.187 1.00 40.48 C ATOM 6594 N GLU F 325 37.024 66.742 −16.560 1.00 37.08 N ATOM 6595 CA GLU F 325 35.976 66.321 −17.489 1.00 38.65 C ATOM 6596 C GLU F 325 35.615 67.265 −18.641 1.00 39.40 C ATOM 6597 O GLU F 325 34.725 66.964 −19.440 1.00 39.05 O ATOM 6598 CB GLU F 325 34.710 65.951 −16.713 1.00 38.67 C ATOM 6599 CG GLU F 325 34.796 64.584 −16.035 1.00 39.54 C ATOM 6600 CD GLU F 325 33.660 64.342 −15.059 1.00 40.30 C ATOM 6601 OE1 GLU F 325 33.587 65.078 −14.055 1.00 41.21 O ATOM 6602 OE2 GLU F 325 32.840 63.424 −15.288 1.00 41.44 O ATOM 6603 N VAL F 326 36.292 68.402 −18.735 1.00 39.99 N ATOM 6604 CA VAL F 326 36.025 69.327 −19.833 1.00 40.92 C ATOM 6605 C VAL F 326 37.345 69.692 −20.492 1.00 41.51 C ATOM 6606 O VAL F 326 38.309 70.024 −19.813 1.00 41.96 O ATOM 6607 CB VAL F 326 35.331 70.608 −19.343 1.00 41.03 C ATOM 6608 CG1 VAL F 326 35.075 71.542 −20.522 1.00 41.22 C ATOM 6609 CG2 VAL F 326 34.028 70.253 −18.646 1.00 40.81 C ATOM 6610 N LEU F 327 37.390 69.602 −21.816 1.00 42.42 N ATOM 6611 CA LEU F 327 38.595 69.920 −22.579 1.00 43.76 C ATOM 6612 C LEU F 327 38.346 71.154 −23.442 1.00 44.79 C ATOM 6613 O LEU F 327 37.456 71.144 −24.295 1.00 44.63 O ATOM 6614 CB LEU F 327 38.968 68.742 −23.486 1.00 44.26 C ATOM 6615 CG LEU F 327 40.164 68.970 −24.420 1.00 44.64 C ATOM 6616 CD1 LEU F 327 41.459 68.949 −23.619 1.00 44.42 C ATOM 6617 CD2 LEU F 327 40.195 67.903 −25.495 1.00 44.68 C ATOM 6618 N TYR F 328 39.138 72.203 −23.225 1.00 45.43 N ATOM 6619 CA TYR F 328 38.996 73.448 −23.974 1.00 46.80 C ATOM 6620 C TYR F 328 40.084 73.598 −25.033 1.00 47.92 C ATOM 6621 O TYR F 328 41.247 73.287 −24.781 1.00 48.34 O ATOM 6622 CB TYR F 328 39.045 74.636 −23.010 1.00 46.06 C ATOM 6623 N ILE F 329 39.697 74.065 −26.218 1.00 49.45 N ATOM 6624 CA ILE F 329 40.630 74.285 −27.328 1.00 51.14 C ATOM 6625 C ILE F 329 40.308 75.646 −27.957 1.00 52.51 C ATOM 6626 O ILE F 329 39.272 75.797 −28.611 1.00 52.52 O ATOM 6627 CB ILE F 329 40.488 73.191 −28.414 1.00 50.82 C ATOM 6628 N ARG F 330 41.193 76.626 −27.762 1.00 54.06 N ATOM 6629 CA ARG F 330 40.991 77.982 −28.283 1.00 54.82 C ATOM 6630 C ARG F 330 41.824 78.308 −29.522 1.00 55.21 C ATOM 6631 O ARG F 330 42.884 77.714 −29.739 1.00 55.27 O ATOM 6632 CB ARG F 330 41.301 79.001 −27.182 1.00 55.05 C ATOM 6633 N ASN F 331 41.341 79.260 −30.321 1.00 55.59 N ATOM 6634 CA ASN F 331 42.038 79.685 −31.535 1.00 56.01 C ATOM 6635 C ASN F 331 42.474 78.463 −32.333 1.00 56.52 C ATOM 6636 O ASN F 331 43.660 78.282 −32.613 1.00 56.89 O ATOM 6637 CB ASN F 331 43.268 80.526 −31.167 1.00 55.05 C ATOM 6638 N VAL F 332 41.507 77.631 −32.704 1.00 56.90 N ATOM 6639 CA VAL F 332 41.789 76.407 −33.441 1.00 57.07 C ATOM 6640 C VAL F 332 42.386 76.615 −34.827 1.00 57.17 C ATOM 6641 O VAL F 332 42.114 77.608 −35.494 1.00 57.28 O ATOM 6642 CB VAL F 332 40.513 75.551 −33.590 1.00 56.97 C ATOM 6643 N THR F 333 43.212 75.662 −35.245 1.00 57.38 N ATOM 6644 CA THR F 333 43.837 75.689 −36.562 1.00 57.57 C ATOM 6645 C THR F 333 43.264 74.484 −37.305 1.00 57.51 C ATOM 6646 O THR F 333 42.549 73.677 −36.712 1.00 57.93 O ATOM 6647 CB THR F 333 45.372 75.542 −36.466 1.00 57.59 C ATOM 6648 N PHE F 334 43.562 74.357 −38.593 1.00 57.10 N ATOM 6649 CA PHE F 334 43.054 73.222 −39.355 1.00 56.54 C ATOM 6650 C PHE F 334 43.709 71.939 −38.841 1.00 56.06 C ATOM 6651 O PHE F 334 43.181 70.838 −39.017 1.00 56.04 O ATOM 6652 CB PHE F 334 43.341 73.407 −40.850 1.00 56.71 C ATOM 6653 N GLU F 335 44.858 72.091 −38.192 1.00 55.14 N ATOM 6654 CA GLU F 335 45.583 70.950 −37.650 1.00 54.37 C ATOM 6655 C GLU F 335 44.838 70.313 −36.470 1.00 53.76 C ATOM 6656 O GLU F 335 45.003 69.123 −36.193 1.00 53.58 O ATOM 6657 CB GLU F 335 46.986 71.383 −37.204 1.00 54.78 C ATOM 6658 N ASP F 336 44.018 71.102 −35.779 1.00 52.59 N ATOM 6659 CA ASP F 336 43.274 70.588 −34.631 1.00 51.94 C ATOM 6660 C ASP F 336 42.146 69.642 −35.007 1.00 50.68 C ATOM 6661 O ASP F 336 41.697 68.861 −34.176 1.00 50.39 O ATOM 6662 CB ASP F 336 42.716 71.735 −33.786 1.00 52.17 C ATOM 6663 CG ASP F 336 43.806 72.534 −33.113 1.00 52.82 C ATOM 6664 OD1 ASP F 336 44.685 71.904 −32.483 1.00 52.36 O ATOM 6665 OD2 ASP F 336 43.785 73.781 −33.216 1.00 52.92 O ATOM 6666 N ALA F 337 41.688 69.714 −36.252 1.00 49.61 N ATOM 6667 CA ALA F 337 40.614 68.846 −36.721 1.00 48.83 C ATOM 6668 C ALA F 337 40.971 67.392 −36.450 1.00 48.43 C ATOM 6669 O ALA F 337 42.145 67.018 −36.477 1.00 48.75 O ATOM 6670 CB ALA F 337 40.381 69.056 −38.219 1.00 48.56 C ATOM 6671 N GLY F 338 39.961 66.569 −36.188 1.00 47.59 N ATOM 6672 CA GLY F 338 40.228 65.166 −35.925 1.00 46.62 C ATOM 6673 C GLY F 338 39.363 64.546 −34.844 1.00 45.72 C ATOM 6674 O GLY F 338 38.417 65.166 −34.346 1.00 44.55 O ATOM 6675 N GLU F 339 39.707 63.315 −34.477 1.00 45.00 N ATOM 6676 CA GLU F 339 38.975 62.560 −33.470 1.00 44.63 C ATOM 6677 C GLU F 339 39.539 62.748 −32.054 1.00 43.23 C ATOM 6678 O GLU F 339 40.725 62.501 −31.812 1.00 42.62 O ATOM 6679 CB GLU F 339 39.001 61.075 −33.847 1.00 45.50 C ATOM 6680 CG GLU F 339 38.029 60.198 −33.080 1.00 46.92 C ATOM 6681 CD GLU F 339 38.054 58.768 −33.569 1.00 47.70 C ATOM 6682 OE1 GLU F 339 38.295 58.565 −34.775 1.00 48.96 O ATOM 6683 OE2 GLU F 339 37.821 57.845 −32.762 1.00 50.13 O ATOM 6684 N TYR F 340 38.678 63.194 −31.136 1.00 42.09 N ATOM 6685 CA TYR F 340 39.044 63.388 −29.732 1.00 40.89 C ATOM 6686 C TYR F 340 38.365 62.319 −28.872 1.00 39.87 C ATOM 6687 O TYR F 340 37.190 62.004 −29.067 1.00 40.00 O ATOM 6688 CB TYR F 340 38.646 64.789 −29.262 1.00 41.78 C ATOM 6689 CG TYR F 340 39.494 65.868 −29.898 1.00 43.99 C ATOM 6690 CD1 TYR F 340 39.330 66.207 −31.241 1.00 44.23 C ATOM 6691 CD2 TYR F 340 40.522 66.492 −29.180 1.00 44.40 C ATOM 6692 CE1 TYR F 340 40.171 67.132 −31.862 1.00 44.75 C ATOM 6693 CE2 TYR F 340 41.368 67.416 −29.787 1.00 45.18 C ATOM 6694 CZ TYR F 340 41.190 67.730 −31.135 1.00 45.70 C ATOM 6695 OH TYR F 340 42.047 68.613 −31.759 1.00 45.46 O ATOM 6696 N THR F 341 39.104 61.770 −27.911 1.00 38.19 N ATOM 6697 CA THR F 341 38.578 60.709 −27.065 1.00 36.42 C ATOM 6698 C THR F 341 38.723 60.932 −25.570 1.00 35.91 C ATOM 6699 O THR F 341 39.788 61.304 −25.091 1.00 35.96 O ATOM 6700 CB THR F 341 39.293 59.378 −27.379 1.00 36.28 C ATOM 6701 OG1 THR F 341 39.008 58.985 −28.724 1.00 36.27 O ATOM 6702 CG2 THR F 341 38.866 58.284 −26.418 1.00 35.37 C ATOM 6703 N CYS F 342 37.644 60.704 −24.833 1.00 35.02 N ATOM 6704 CA CYS F 342 37.707 60.793 −23.382 1.00 34.15 C ATOM 6705 C CYS F 342 37.847 59.344 −22.965 1.00 33.29 C ATOM 6706 O CYS F 342 36.980 58.520 −23.268 1.00 34.08 O ATOM 6707 CB CYS F 342 36.426 61.349 −22.777 1.00 33.61 C ATOM 6708 SG CYS F 342 36.368 61.103 −20.981 1.00 33.75 S ATOM 6709 N LEU F 343 38.937 59.025 −22.282 1.00 32.19 N ATOM 6710 CA LEU F 343 39.173 57.658 −21.842 1.00 30.69 C ATOM 6711 C LEU F 343 39.254 57.567 −20.320 1.00 30.23 C ATOM 6712 O LEU F 343 40.019 58.291 −19.680 1.00 29.47 O ATOM 6713 CB LEU F 343 40.446 57.130 −22.504 1.00 29.92 C ATOM 6714 CG LEU F 343 40.882 55.695 −22.237 1.00 29.64 C ATOM 6715 CD1 LEU F 343 41.521 55.097 −23.494 1.00 29.38 C ATOM 6716 CD2 LEU F 343 41.847 55.684 −21.070 1.00 29.69 C ATOM 6717 N ALA F 344 38.444 56.673 −19.753 1.00 29.04 N ATOM 6718 CA ALA F 344 38.374 56.471 −18.319 1.00 28.61 C ATOM 6719 C ALA F 344 38.688 55.031 −17.927 1.00 28.64 C ATOM 6720 O ALA F 344 38.107 54.086 −18.463 1.00 29.32 O ATOM 6721 CB ALA F 344 36.982 56.850 −17.818 1.00 27.84 C ATOM 6722 N GLY F 345 39.600 54.861 −16.977 1.00 27.93 N ATOM 6723 CA GLY F 345 39.933 53.517 −16.551 1.00 26.97 C ATOM 6724 C GLY F 345 40.122 53.366 −15.052 1.00 26.41 C ATOM 6725 O GLY F 345 40.504 54.320 −14.367 1.00 24.61 O ATOM 6726 N ASN F 346 39.803 52.175 −14.544 1.00 25.72 N ATOM 6727 CA ASN F 346 40.019 51.828 −13.135 1.00 27.21 C ATOM 6728 C ASN F 346 40.644 50.424 −13.115 1.00 27.92 C ATOM 6729 O ASN F 346 40.917 49.855 −14.176 1.00 26.78 O ATOM 6730 CB ASN F 346 38.722 51.866 −12.293 1.00 26.34 C ATOM 6731 CG ASN F 346 37.637 50.911 −12.800 1.00 26.84 C ATOM 6732 OD1 ASN F 346 37.935 49.865 −13.375 1.00 24.75 O ATOM 6733 ND2 ASN F 346 36.368 51.269 −12.563 1.00 24.95 N ATOM 6734 N SER F 347 40.879 49.866 −11.931 1.00 29.98 N ATOM 6735 CA SER F 347 41.499 48.539 −11.837 1.00 32.45 C ATOM 6736 C SER F 347 40.738 47.443 −12.569 1.00 33.80 C ATOM 6737 O SER F 347 41.347 46.475 −13.005 1.00 34.43 O ATOM 6738 CB SER F 347 41.695 48.102 −10.375 1.00 34.30 C ATOM 6739 OG SER F 347 40.460 47.838 −9.725 1.00 37.06 O ATOM 6740 N ILE F 348 39.419 47.582 −12.712 1.00 34.07 N ATOM 6741 CA ILE F 348 38.638 46.556 −13.415 1.00 34.74 C ATOM 6742 C ILE F 348 38.746 46.629 −14.942 1.00 34.67 C ATOM 6743 O ILE F 348 38.858 45.603 −15.606 1.00 34.73 O ATOM 6744 CB ILE F 348 37.117 46.608 −13.080 1.00 35.89 C ATOM 6745 CG1 ILE F 348 36.872 46.336 −11.594 1.00 36.06 C ATOM 6746 CG2 ILE F 348 36.370 45.572 −13.931 1.00 36.09 C ATOM 6747 CD1 ILE F 348 37.101 47.530 −10.702 1.00 38.46 C ATOM 6748 N GLY F 349 38.690 47.834 −15.502 1.00 34.21 N ATOM 6749 CA GLY F 349 38.766 47.970 −16.946 1.00 33.77 C ATOM 6750 C GLY F 349 38.755 49.395 −17.477 1.00 33.75 C ATOM 6751 O GLY F 349 38.798 50.361 −16.711 1.00 33.67 O ATOM 6752 N ILE F 350 38.670 49.511 −18.801 1.00 33.27 N ATOM 6753 CA ILE F 350 38.683 50.794 −19.498 1.00 33.45 C ATOM 6754 C ILE F 350 37.449 51.057 −20.370 1.00 33.70 C ATOM 6755 O ILE F 350 36.901 50.142 −20.983 1.00 33.76 O ATOM 6756 CB ILE F 350 39.926 50.894 −20.411 1.00 33.49 C ATOM 6757 CG1 ILE F 350 41.198 50.775 −19.567 1.00 34.27 C ATOM 6758 CG2 ILE F 350 39.907 52.199 −21.187 1.00 34.40 C ATOM 6759 CD1 ILE F 350 42.482 50.712 −20.381 1.00 36.09 C ATOM 6760 N SER F 351 37.029 52.321 −20.418 1.00 32.59 N ATOM 6761 CA SER F 351 35.903 52.764 −21.240 1.00 32.30 C ATOM 6762 C SER F 351 36.291 54.075 −21.921 1.00 32.43 C ATOM 6763 O SER F 351 37.085 54.848 −21.378 1.00 31.37 O ATOM 6764 CB SER F 351 34.655 53.006 −20.394 1.00 32.47 C ATOM 6765 CG SER F 351 34.115 51.793 −19.920 1.00 34.26 O ATOM 6766 N PHE F 352 35.735 54.329 −23.104 1.00 32.25 N ATOM 6767 CA PHE F 352 36.039 55.561 −23.828 1.00 33.49 C ATOM 6768 C PHE F 352 34.990 55.930 −24.873 1.00 33.58 C ATOM 6769 O PHE F 352 34.419 55.057 −25.537 1.00 33.77 O ATOM 6770 CB PHE F 352 37.414 55.455 −24.504 1.00 34.61 C ATOM 6771 CG PHE F 352 37.525 54.317 −25.491 1.00 36.55 C ATOM 6772 CD1 PHE F 352 37.059 54.453 −26.797 1.00 38.08 C ATOM 6773 CD2 PHE F 352 38.093 53.109 −25.109 1.00 37.89 C ATOM 6774 CE1 PHE F 352 37.161 53.396 −27.711 1.00 39.20 C ATOM 6775 CE2 PHE F 352 38.201 52.047 −26.010 1.00 38.88 C ATOM 6776 CZ PHE F 352 37.734 52.191 −27.313 1.00 39.32 C ATOM 6777 N HIS F 353 34.737 57.227 −25.011 1.00 33.60 N ATOM 6778 CA HIS F 353 33.787 57.731 −26.004 1.00 34.44 C ATOM 6779 C HIS F 353 34.539 58.773 −26.831 1.00 35.35 C ATOM 6780 O HIS F 353 35.359 59.528 −26.295 1.00 35.17 O ATOM 6781 CB HIS F 353 32.559 58.386 −25.351 1.00 34.07 C ATOM 6782 CG HIS F 353 31.579 57.416 −24.759 1.00 34.66 C ATOM 6783 ND1 HIS F 353 30.424 57.821 −24.121 1.00 33.93 N ATOM 6784 CD2 HIS F 353 31.571 56.059 −24.713 1.00 34.45 C ATOM 6785 CE1 HIS F 353 29.750 56.762 −23.711 1.00 32.42 C ATOM 6786 NE2 HIS F 353 30.424 55.682 −24.058 1.00 33.28 N ATOM 6787 N SER F 354 34.261 58.806 −28.133 1.00 35.90 N ATOM 6788 CA SER F 354 34.931 59.739 −29.032 1.00 36.78 C ATOM 6789 C SER F 354 33.997 60.684 −29.777 1.00 37.44 C ATOM 6790 O SER F 354 32.812 60.406 −29.968 1.00 36.86 O ATOM 6791 CB SER F 354 35.770 58.963 −30.045 1.00 36.92 C ATOM 6792 OG SER F 354 36.682 58.111 −29.379 1.00 38.08 O ATOM 6793 N ALA F 355 34.551 61.816 −30.187 1.00 38.59 N ATOM 6794 CA ALA F 355 33.801 62.813 −30.938 1.00 40.11 C ATOM 6795 C ALA F 355 34.737 63.388 −31.994 1.00 41.10 C ATOM 6796 O ALA F 355 35.963 63.223 −31.910 1.00 41.45 O ATOM 6797 CB ALA F 355 33.294 63.917 −30.008 1.00 39.80 C ATOM 6798 N TRP F 356 34.166 64.055 −32.990 1.00 42.22 N ATOM 6799 CA TRP F 356 34.970 64.638 −34.056 1.00 43.25 C ATOM 6800 C TRP F 356 34.915 66.155 −34.069 1.00 43.67 C ATOM 6801 O TRP F 356 33.884 66.760 −33.791 1.00 43.60 O ATOM 6802 CB TRP F 356 34.523 64.108 −35.424 1.00 43.57 C ATOM 6803 N LEU F 357 36.050 66.763 −34.383 1.00 44.42 N ATOM 6804 CA LEU F 357 36.142 68.208 −34.472 1.00 45.85 C ATOM 6805 C LEU F 357 36.305 68.570 −35.951 1.00 46.42 C ATOM 6806 O LEU F 357 37.254 68.123 −36.605 1.00 46.43 O ATOM 6807 CB LEU F 357 37.342 68.708 −33.656 1.00 46.03 C ATOM 6808 CG LEU F 357 37.664 70.206 −33.652 1.00 46.53 C ATOM 6809 CD1 LEU F 357 38.430 70.582 −34.910 1.00 47.10 C ATOM 6810 CD2 LEU F 357 36.371 71.007 −33.527 1.00 46.18 C ATOM 6811 N THR F 358 35.369 69.359 −36.473 1.00 46.98 N ATOM 6812 CA THR F 358 35.417 69.782 −37.870 1.00 48.32 C ATOM 6813 C THR F 358 35.811 71.256 −37.925 1.00 48.82 C ATOM 6814 O THR F 358 35.167 72.098 −37.293 1.00 48.73 O ATOM 6815 CB THR F 358 34.042 69.594 −38.558 1.00 48.28 C ATOM 6816 N VAL F 359 36.874 71.559 −38.667 1.00 49.50 N ATOM 6817 CA VAL F 359 37.359 72.929 −38.803 1.00 50.61 C ATOM 6818 C VAL F 359 37.176 73.433 −40.236 1.00 51.09 C ATOM 6819 O VAL F 359 37.789 72.839 −41.149 1.00 51.86 O ATOM 6820 CB VAL F 359 38.858 73.036 −38.419 1.00 50.22 C TER 6821 VAL F 359 ATOM 6822 N LYS G 151 32.215 55.396 −63.632 1.00 37.93 N ATOM 6823 CA LYS G 151 30.832 55.516 −63.096 1.00 39.08 C ATOM 6824 C LYS G 151 30.226 54.131 −62.828 1.00 39.20 C ATOM 6825 O LYS G 151 30.223 53.272 −63.708 1.00 39.64 O ATOM 6826 CB LYS G 151 29.955 56.276 −64.098 1.00 39.20 C ATOM 6827 N ARG G 152 29.735 53.910 −61.610 1.00 38.69 N ATOM 6828 CA ARG G 152 29.115 52.633 −61.251 1.00 38.05 C ATOM 6829 C ARG G 152 28.255 52.699 −59.993 1.00 36.80 C ATOM 6830 O ARG G 152 28.428 53.570 −59.139 1.00 36.86 O ATOM 6831 CB ARG G 152 30.172 51.535 −61.076 1.00 38.73 C ATOM 6832 CG ARG G 152 31.158 51.774 −59.951 1.00 39.40 C ATOM 6833 CD ARG G 152 32.297 50.750 −59.968 1.00 40.41 C ATOM 6834 NE ARG G 152 31.888 49.426 −59.504 1.00 39.75 N ATOM 6835 CZ ARG G 152 32.740 48.476 −59.120 1.00 40.46 C ATOM 6836 NH1 ARG G 152 34.048 48.702 −59.147 1.00 40.01 N ATOM 6837 NH2 ARG G 152 32.289 47.303 −58.692 1.00 39.42 N ATOM 6838 N ALA G 153 27.332 51.750 −59.901 1.00 35.27 N ATOM 6839 CA ALA G 153 26.412 51.632 −58.780 1.00 34.38 C ATOM 6840 C ALA G 153 27.175 51.335 −57.484 1.00 33.88 C ATOM 6841 O ALA G 153 28.335 50.936 −57.519 1.00 33.72 O ATOM 6842 CB ALA G 153 25.406 50.512 −59.066 1.00 32.93 C ATOM 6843 N PRO G 154 26.520 51.508 −56.322 1.00 33.31 N ATOM 6844 CA PRO G 154 27.177 51.247 −55.035 1.00 33.08 C ATOM 6845 C PRO G 154 27.519 49.772 −54.870 1.00 33.05 C ATOM 6846 O PRO G 154 26.828 48.901 −55.397 1.00 32.66 O ATOM 6847 CB PRO G 154 26.136 51.697 −54.001 1.00 32.74 C ATOM 6848 CG PRO G 154 25.197 52.610 −54.786 1.00 33.49 C ATOM 6849 CD PRO G 154 25.120 51.911 −56.118 1.00 33.51 C ATOM 6850 N TYR G 155 28.585 49.503 −54.131 1.00 32.79 N ATOM 6851 CA TYR G 155 29.015 48.139 −53.876 1.00 33.67 C ATOM 6852 C TYR G 155 29.807 48.061 −52.568 1.00 33.41 C ATOM 6853 O TYR G 155 30.494 49.013 −52.205 1.00 33.82 O ATOM 6854 CB TYR G 155 29.866 47.622 −55.045 1.00 33.62 C ATOM 6855 CG TYR G 155 31.211 48.304 −55.215 1.00 34.56 C ATOM 6856 CD1 TYR G 155 31.304 49.566 −55.793 1.00 35.11 C ATOM 6857 CD2 TYR G 155 32.391 47.677 −54.811 1.00 35.26 C ATOM 6858 CE1 TYR G 155 32.536 50.189 −55.975 1.00 36.15 C ATOM 6859 CE2 TYR G 155 33.636 48.294 −54.986 1.00 35.66 C ATOM 6860 CZ TYR G 155 33.695 49.551 −55.571 1.00 36.50 C ATOM 6861 OH TYR G 155 34.905 50.172 −55.769 1.00 38.56 O ATOM 6862 N TRP G 156 29.702 46.938 −51.861 1.00 33.53 N ATOM 6863 CA TRP G 156 30.424 46.757 −50.596 1.00 34.85 C ATOM 6864 C TRP G 156 31.911 46.557 −50.862 1.00 36.39 C ATOM 6865 O TRP G 156 32.288 45.709 −51.664 1.00 36.88 O ATOM 6866 CB TRP G 156 29.887 45.538 −49.827 1.00 32.98 C ATOM 6867 CG TRP G 156 28.412 45.584 −49.563 1.00 31.32 C ATOM 6868 CD1 TRP G 156 27.509 44.581 −49.784 1.00 29.97 C ATOM 6869 CD2 TRP G 156 27.665 46.694 −49.055 1.00 29.82 C ATOM 6870 NE1 TRP G 156 26.245 45.001 −49.450 1.00 29.21 N ATOM 6871 CE2 TRP G 156 26.310 46.293 −48.999 1.00 29.86 C ATOM 6872 CE3 TRP G 156 28.007 47.987 −48.643 1.00 29.96 C ATOM 6873 CZ2 TRP G 156 25.294 47.142 −48.548 1.00 29.44 C ATOM 6874 CZ3 TRP G 156 26.992 48.840 −48.191 1.00 30.20 C ATOM 6875 CH2 TRP G 156 25.653 48.410 −48.149 1.00 30.96 C ATOM 6876 N THR G 157 32.754 47.329 −50.182 1.00 38.26 N ATOM 6877 CA THR G 157 34.203 47.226 −50.366 1.00 40.35 C ATOM 6878 C THR C 157 34.873 46.270 −49.392 1.00 42.46 C ATOM 6879 O THR G 157 36.078 46.046 −49.484 1.00 43.05 O ATOM 6880 CB THR G 157 34.930 48.602 −50.213 1.00 39.64 C ATOM 6881 OG1 THR G 157 34.635 49.174 −48.933 1.00 38.76 O ATOM 6882 CG2 THR G 157 34.515 49.570 −51.308 1.00 39.60 C ATOM 6883 N ASN G 158 34.103 45.706 −48.466 1.00 43.84 N ATOM 6884 CA ASN G 158 34.670 44.792 −47.482 1.00 45.69 C ATOM 6885 C ASN G 158 33.595 43.928 −46.828 1.00 45.42 C ATOM 6886 O ASN G 158 33.163 44.209 −45.716 1.00 45.32 O ATOM 6887 CB ASN G 158 35.410 45.601 −46.408 1.00 47.44 C ATOM 6888 CG ASN G 158 36.131 44.719 −45.403 1.00 50.56 C ATOM 6889 OD1 ASN G 158 35.508 43.939 −44.678 1.00 52.48 O ATOM 6890 ND2 ASN G 158 37.457 44.834 −45.360 1.00 51.45 N ATOM 6891 N THR G 159 33.178 42.874 −47.520 1.00 46.07 N ATOM 6892 CA THR G 159 32.146 41.968 −47.020 1.00 46.62 C ATOM 6893 C THR G 159 32.564 41.185 −45.781 1.00 46.29 C ATOM 6894 O THR G 159 31.711 40.716 −45.029 1.00 46.39 O ATOM 6895 CB THR G 159 31.751 40.953 −48.096 1.00 46.81 C ATOM 6896 OG1 THR G 159 32.913 40.207 −48.495 1.00 47.00 O ATOM 6897 CG2 THR G 159 31.172 41.663 −49.297 1.00 46.53 C ATOM 6898 N GLU G 160 33.871 41.032 −45.579 1.00 46.49 N ATOM 6899 CA GLU G 160 34.393 40.294 −44.429 1.00 46.06 C ATOM 6900 C GLU G 160 33.858 40.887 −43.129 1.00 46.02 C ATOM 6901 O GLU G 160 33.367 40.164 −42.264 1.00 45.54 O ATOM 6902 CB GLU G 160 35.920 40.335 −44.413 1.00 46.21 C ATOM 6903 N LYS G 161 33.951 42.209 −43.007 1.00 45.89 N ATOM 6904 CA LYS G 161 33.483 42.926 −41.822 1.00 45.83 C ATOM 6905 C LYS G 161 31.959 42.991 −41.700 1.00 45.38 C ATOM 6906 O LYS G 161 31.445 43.581 −40.753 1.00 45.49 O ATOM 6907 CB LYS G 161 34.026 44.363 −41.819 1.00 46.64 C ATOM 6908 CG LYS G 161 35.547 44.475 −41.765 1.00 48.45 C ATOM 6909 CD LYS G 161 35.984 45.937 −41.698 1.00 49.04 C ATOM 6910 CE LYS G 161 37.496 46.060 −41.529 1.00 50.22 C ATOM 6911 NZ LYS G 161 37.949 47.487 −41.526 1.00 50.00 N ATOM 6912 N MET G 162 31.237 42.402 −42.650 1.00 44.59 N ATOM 6913 CA MET G 162 29.773 42.436 −42.624 1.00 43.97 C ATOM 6914 C MET G 162 29.138 41.062 −42.425 1.00 43.84 C ATOM 6915 O MET G 162 27.921 40.954 −42.286 1.00 44.07 O ATOM 6916 CB MET G 162 29.240 43.050 −43.928 1.00 42.91 C ATOM 6917 CG MET G 162 29.687 44.487 −44.197 1.00 40.62 C ATOM 6918 SD MET G 162 29.237 45.043 −45.875 1.00 39.77 S ATOM 6919 CE MET G 162 27.459 45.242 −45.697 1.00 39.45 C ATOM 6920 N GLU G 163 29.960 40.018 −42.405 1.00 44.03 N ATOM 6921 CA GLU G 163 29.468 38.651 −42.247 1.00 43.93 C ATOM 6922 C GLU G 163 28.762 38.384 −40.915 1.00 42.61 C ATOM 6923 O GLU G 163 27.810 37.613 −40.870 1.00 42.58 O ATOM 6924 CB GLU G 163 30.625 37.660 −42.431 1.00 45.99 C ATOM 6925 CG GLU G 163 31.400 37.853 −43.733 1.00 49.23 C ATOM 6926 CD GLU G 163 32.552 36.870 −43.893 1.00 51.45 C ATOM 6927 OE1 GLU G 163 33.169 36.510 −42.865 1.00 52.67 O ATOM 6928 OE2 GLU G 163 32.853 36.471 −45.045 1.00 52.43 O ATOM 6929 N LYS G 164 29.234 39.008 −39.837 1.00 41.12 N ATOM 6930 CA LYS G 164 28.631 38.836 −38.509 1.00 39.70 C ATOM 6931 C LYS G 164 27.307 39.618 −38.484 1.00 38.39 C ATOM 6932 O LYS G 164 27.299 40.830 −38.274 1.00 38.68 O ATOM 6933 CB LYS G 164 29.591 39.363 −37.418 1.00 39.23 C ATOM 6934 CG LYS G 164 29.140 39.093 −35.962 1.00 38.82 C ATOM 6935 CD LYS G 164 30.121 39.706 −34.939 1.00 38.47 C ATOM 6936 CE LYS G 164 29.622 39.572 −33.506 1.00 37.66 C ATOM 6937 NZ LYS G 164 30.524 40.217 −32.490 1.00 37.42 N ATOM 6938 N ARG G 165 26.192 38.924 −38.695 1.00 36.91 N ATOM 6939 CA ARG G 165 24.884 39.580 −38.738 1.00 36.31 C ATOM 6940 C ARG G 165 24.287 39.864 −37.370 1.00 35.60 C ATOM 6941 O ARG G 165 23.715 40.934 −37.146 1.00 34.92 O ATOM 6942 CB ARG G 165 23.899 38.746 −39.572 1.00 36.23 C ATOM 6943 N LEU G 166 24.406 38.903 −36.460 1.00 35.23 N ATOM 6944 CA LEU G 166 23.887 39.075 −35.113 1.00 34.50 C ATOM 6945 C LEU G 166 24.981 39.588 −34.171 1.00 34.23 C ATOM 6946 O LEU G 166 26.028 38.956 −34.004 1.00 34.46 O ATOM 6947 CB LEU G 166 23.306 37.757 −34.596 1.00 34.17 C ATOM 6948 CG LEU G 166 23.006 37.689 −33.090 1.00 35.92 C ATOM 6949 CD1 LEU G 166 22.123 38.851 −32.648 1.00 34.55 C ATOM 6950 CD2 LEU G 166 22.348 36.362 −32.777 1.00 35.42 C ATOM 6951 N HIS G 167 24.733 40.753 −33.582 1.00 33.90 N ATOM 6952 CA HIS G 167 25.652 41.369 −32.625 1.00 34.03 C ATOM 6953 C HIS G 167 25.037 41.301 −31.238 1.00 34.08 C ATOM 6954 O HIS G 167 24.132 42.078 −30.919 1.00 34.22 O ATOM 6955 CB HIS G 167 25.897 42.842 −32.949 1.00 34.75 C ATOM 6956 CG HIS G 167 26.975 43.069 −33.954 1.00 35.95 C ATOM 6957 ND1 HIS G 167 26.910 42.576 −35.239 1.00 36.61 N ATOM 6958 CD2 HIS G 167 28.160 43.715 −33.857 1.00 36.49 C ATOM 6959 CE1 HIS G 167 28.010 42.906 −35.891 1.00 36.40 C ATOM 6960 NE2 HIS G 167 28.786 43.597 −35.074 1.00 37.07 N ATOM 6961 N ALA G 168 25.505 40.370 −30.418 1.00 33.10 N ATOM 6962 CA ALA G 168 24.996 40.259 −29.061 1.00 32.60 C ATOM 6963 C ALA G 168 26.108 40.801 −28.175 1.00 32.87 C ATOM 6964 O ALA G 168 27.237 40.302 −28.212 1.00 33.14 O ATOM 6965 CB ALA G 168 24.682 38.809 −28.725 1.00 33.23 C ATOM 6966 N VAL G 169 25.799 41.838 −27.402 1.00 32.15 N ATOM 6967 CA VAL G 169 26.798 42.454 −26.546 1.00 33.09 C ATOM 6968 C VAL G 169 26.284 42.769 −25.156 1.00 33.02 C ATOM 6969 O VAL G 169 25.087 42.930 −24.935 1.00 33.52 O ATOM 6970 CB VAL G 169 27.341 43.768 −27.167 1.00 34.37 C ATOM 6971 CG1 VAL G 169 27.788 43.514 −28.609 1.00 35.12 C ATOM 6972 CG2 VAL G 169 26.268 44.858 −27.117 1.00 34.22 C ATOM 6973 N PRO G 170 27.198 42.859 −24.192 1.00 32.91 N ATOM 6974 CA PRO G 170 26.867 43.159 −22.800 1.00 32.72 C ATOM 6975 C PRO G 170 26.401 44.612 −22.658 1.00 34.03 C ATOM 6976 O PRO G 170 26.931 45.508 −23.333 1.00 33.46 O ATOM 6977 CB PRO G 170 28.192 42.936 −22.075 1.00 32.27 C ATOM 6978 CG PRO G 170 28.917 41.954 −22.950 1.00 33.28 C ATOM 6979 CD PRO G 170 28.616 42.475 −24.323 1.00 33.23 C ATOM 6980 N ALA G 171 25.430 44.840 −21.776 1.00 33.75 N ATOM 6981 CA ALA G 171 24.909 46.177 −21.524 1.00 34.33 C ATOM 6982 C ALA G 171 26.050 47.100 −21.120 1.00 34.09 C ATOM 6983 O ALA G 171 27.022 46.646 −20.512 1.00 33.95 O ATOM 6984 CB ALA G 171 23.859 46.130 −20.408 1.00 34.12 C ATOM 6985 N ALA G 172 25.931 48.380 −21.487 1.00 33.12 N ATOM 6986 CA ALA G 172 26.914 49.411 −21.157 1.00 33.26 C ATOM 6987 C ALA G 172 28.082 49.537 −22.136 1.00 33.48 C ATOM 6988 O ALA G 172 28.915 50.442 −22.014 1.00 34.33 O ATOM 6989 CB ALA G 172 27.446 49.198 −19.729 1.00 32.38 C ATOM 6990 N ASN G 173 28.155 48.634 −23.101 1.00 33.22 N ATOM 6991 CA ASN G 173 29.225 48.679 −24.091 1.00 33.37 C ATOM 6992 C ASN G 173 28.840 49.566 −25.272 1.00 32.71 C ATOM 6993 O ASN G 173 27.684 49.962 −25.423 1.00 32.68 O ATOM 6994 CB ASN G 173 29.524 47.269 −24.629 1.00 34.62 C ATOM 6995 CG ASN G 173 30.296 46.404 −23.640 1.00 34.28 C ATOM 6996 OD1 ASN G 173 30.170 46.554 −22.433 1.00 37.26 O ATOM 6997 ND2 ASN G 173 31.080 45.481 −24.158 1.00 34.66 N ATOM 6998 N THR G 174 29.830 49.873 −26.102 1.00 31.59 N ATOM 6999 CA THR G 174 29.627 50.659 −27.311 1.00 30.98 C ATOM 7000 C THR G 174 29.460 49.669 −28.472 1.00 30.95 C ATOM 7001 O THR G 174 30.179 48.669 −28.544 1.00 30.81 O ATOM 7002 CB THR G 174 30.860 51.529 −27.626 1.00 30.59 C ATOM 7003 OG1 THR G 174 30.907 52.642 −26.730 1.00 31.56 O ATOM 7004 CG2 THR G 174 30.812 52.029 −29.074 1.00 29.92 C ATOM 7005 N VAL G 175 28.523 49.939 −29.376 1.00 30.17 N ATOM 7006 CA VAL G 175 28.311 49.068 −30.530 1.00 29.66 C ATOM 7007 C VAL G 175 28.583 49.851 −31.809 1.00 28.77 C ATOM 7008 O VAL G 175 28.223 51.024 −31.913 1.00 28.77 O ATOM 7009 CB VAL G 175 26.853 48.534 −30.583 1.00 29.73 C ATOM 7010 CG1 VAL G 175 26.675 47.614 −31.785 1.00 30.00 C ATOM 7011 CG2 VAL G 175 26.530 47.784 −29.320 1.00 31.31 C ATOM 7012 N LYS G 176 29.229 49.214 −32.776 1.00 28.41 N ATOM 7013 CA LYS G 176 29.519 49.876 −34.046 1.00 28.60 C ATOM 7014 C LYS G 176 29.178 48.979 −35.240 1.00 29.11 C ATOM 7015 O LYS G 176 29.671 47.856 −35.342 1.00 28.32 O ATOM 7016 CB LYS G 176 30.991 50.284 −34.117 1.00 29.21 C ATOM 7017 N PHE G 177 28.313 49.473 −36.123 1.00 28.71 N ATOM 7018 CA PHE G 177 27.929 48.736 −37.325 1.00 29.28 C ATOM 7019 C PHE G 177 28.592 49.414 −38.521 1.00 29.86 C ATOM 7020 O PHE G 177 28.617 50.645 −38.610 1.00 29.26 O ATOM 7021 CB PHE G 177 26.401 48.741 −37.522 1.00 28.70 C ATOM 7022 CG PHE G 177 25.641 47.975 −36.464 1.00 29.03 C ATOM 7023 CD1 PHE G 177 25.956 46.649 −36.186 1.00 28.61 C ATOM 7024 CD2 PHE G 177 24.617 48.578 −35.746 1.00 27.96 C ATOM 7025 CE1 PHE G 177 25.264 45.942 −35.210 1.00 28.90 C ATOM 7026 CE2 PHE G 177 23.921 47.881 −34.771 1.00 27.66 C ATOM 7027 CZ PHE G 177 24.245 46.563 −34.502 1.00 28.37 C ATOM 7028 N ARG G 178 29.127 48.617 −39.439 1.00 30.54 N ATOM 7029 CA ARG G 178 29.780 49.169 −40.613 1.00 31.47 C ATOM 7030 C ARG G 178 29.292 48.544 −41.914 1.00 30.95 C ATOM 7031 O ARG G 178 28.922 47.374 −41.949 1.00 29.97 O ATOM 7032 CB ARG G 178 31.298 48.984 −40.515 1.00 34.36 C ATOM 7033 CG ARG G 178 31.931 49.644 −39.295 1.00 39.90 C ATOM 7034 CD ARG G 178 33.447 49.738 −39.439 1.00 43.10 C ATOM 7035 NE ARG G 178 33.818 50.394 −40.693 1.00 47.10 N ATOM 7036 CZ ARG G 178 35.069 50.570 −41.119 1.00 49.58 C ATOM 7037 NH1 ARG G 178 36.096 50.141 −40.390 1.00 50.61 N ATOM 7038 NH2 ARG G 178 35.292 51.172 −42.284 1.00 50.68 N ATOM 7039 N CYS G 179 29.300 49.348 −42.976 1.00 30.10 N ATOM 7040 CA CYS G 179 28.925 48.904 −44.315 1.00 31.02 C ATOM 7041 C CYS G 179 29.848 49.628 −45.305 1.00 31.31 C ATOM 7042 O CYS G 179 29.406 50.479 −46.087 1.00 28.70 O ATOM 7043 CB CYS G 179 27.453 49.233 −44.593 1.00 31.15 C ATOM 7044 SG CYS G 179 26.323 48.376 −43.429 1.00 33.32 S ATOM 7045 N PRO G 180 31.154 49.303 −45.268 1.00 31.92 N ATOM 7046 CA PRO G 180 32.110 49.953 −46.173 1.00 32.72 C ATOM 7047 C PRO G 180 31.664 49.828 −47.620 1.00 33.18 C ATOM 7048 O PRO G 180 31.438 48.731 −48.125 1.00 33.64 O ATOM 7049 CB PRO G 180 33.442 49.269 −45.843 1.00 32.69 C ATOM 7050 CG PRO G 180 33.050 47.991 −45.187 1.00 33.71 C ATOM 7051 CD PRO G 180 31.832 48.342 −44.386 1.00 31.74 C ATOM 7052 N ALA G 181 31.507 50.974 −48.275 1.00 33.47 N ATOM 7053 CA ALA G 181 31.027 50.985 −49.650 1.00 34.74 C ATOM 7054 C ALA G 181 31.848 51.813 −50.628 1.00 35.80 C ATOM 7055 O ALA G 181 32.599 52.709 −50.239 1.00 35.32 O ATOM 7056 CB ALA G 181 29.575 51.473 −49.674 1.00 33.88 C ATOM 7057 N GLY G 182 31.668 51.498 −51.909 1.00 36.73 N ATOM 7058 CA GLY G 182 32.338 52.206 −52.983 1.00 37.08 C ATOM 7059 C GLY G 182 31.282 52.606 −53.999 1.00 38.28 C ATOM 7060 O GLY G 182 30.121 52.197 −53.884 1.00 37.01 O ATOM 7061 N GLY G 183 31.674 53.404 −54.989 1.00 38.76 N ATOM 7062 CA GLY G 183 30.734 53.838 −56.010 1.00 39.76 C ATOM 7063 C GLY G 183 31.086 55.189 −56.613 1.00 40.59 C ATOM 7064 O GLY G 183 31.746 56.011 −55.979 1.00 40.19 O ATOM 7065 N ASN G 184 30.636 55.424 −57.841 1.00 41.17 N ATOM 7066 CA ASN G 184 30.909 56.678 −58.529 1.00 41.73 C ATOM 7067 C ASN G 184 29.700 57.116 −59.342 1.00 41.90 C ATOM 7068 O ASN G 184 29.334 56.478 −60.321 1.00 41.81 O ATOM 7069 CB ASN G 184 32.140 56.527 −59.433 1.00 42.19 C ATOM 7070 CG ASN G 184 32.410 57.766 −60.279 1.00 43.50 C ATOM 7071 OD1 ASN G 184 31.973 58.875 −59.953 1.00 44.29 O ATOM 7072 ND2 ASN G 184 33.147 57.581 −61.368 1.00 43.66 N ATOM 7073 N PRO G 185 29.088 58.245 −58.962 1.00 42.45 N ATOM 7074 CA PRO G 185 29.466 59.115 −57.846 1.00 43.00 C ATOM 7075 C PRO G 185 29.365 58.488 −56.455 1.00 43.89 C ATOM 7076 O PRO G 185 28.707 57.457 −56.261 1.00 44.36 O ATOM 7077 CB PRO G 185 28.522 60.303 −58.012 1.00 43.19 C ATOM 7078 CG PRO G 185 27.292 59.663 −58.551 1.00 43.35 C ATOM 7079 CD PRO G 185 27.844 58.720 −59.594 1.00 42.63 C ATOM 7080 N MET G 186 30.021 59.128 −55.492 1.00 44.05 N ATOM 7081 CA MET G 186 30.020 58.666 −54.111 1.00 44.25 C ATOM 7082 C MET G 186 28.606 58.465 −53.600 1.00 42.98 C ATOM 7083 O MET G 186 27.810 59.403 −53.552 1.00 42.87 O ATOM 7084 CB MET G 186 30.738 59.675 −53.214 1.00 46.35 C ATOM 7085 CG MET G 186 32.139 59.258 −52.808 1.00 50.04 C ATOM 7086 SD MET G 186 32.148 57.751 −51.802 1.00 52.71 S ATOM 7087 CE MET G 186 32.923 56.587 −52.955 1.00 51.94 C ATOM 7088 N PRO G 187 28.267 57.232 −53.213 1.00 41.91 N ATOM 7089 CA PRO G 187 26.917 56.975 −52.708 1.00 41.20 C ATOM 7090 C PRO G 187 26.649 57.562 −51.319 1.00 40.70 C ATOM 7091 O PRO G 187 27.570 57.776 −50.530 1.00 39.93 O ATOM 7092 CB PRO G 187 26.816 55.447 −52.737 1.00 41.16 C ATOM 7093 CG PRO G 187 28.227 55.001 −52.572 1.00 41.50 C ATOM 7094 CD PRO G 187 28.999 55.971 −53.438 1.00 41.38 C ATOM 7095 N THR G 188 25.378 57.839 −51.044 1.00 40.29 N ATOM 7096 CA THR G 188 24.976 58.375 −49.754 1.00 40.62 C ATOM 7097 C THR G 188 24.623 57.203 −48.849 1.00 40.45 C ATOM 7098 O THR G 188 24.425 56.084 −49.322 1.00 40.89 O ATOM 7099 CB THR G 188 23.747 59.299 −49.892 1.00 40.91 C ATOM 7100 OG1 THR G 188 22.685 58.591 −50.544 1.00 41.24 O ATOM 7101 CG2 THR G 188 24.103 60.538 −50.704 1.00 40.28 C ATOM 7102 N MET G 189 24.552 57.459 −47.551 1.00 40.54 N ATOM 7103 CA MET G 189 24.218 56.414 −46.603 1.00 40.70 C ATOM 7104 C MET G 189 23.158 56.852 −45.613 1.00 40.06 C ATOM 7105 O MET G 189 23.178 57.983 −45.124 1.00 40.47 O ATOM 7106 CB MET G 189 25.454 55.958 −45.836 1.00 43.01 C ATOM 7107 CG MET G 189 25.120 54.977 −44.729 1.00 46.26 C ATOM 7108 SD MET G 189 26.578 54.334 −43.921 1.00 51.42 S ATOM 7109 CE MET G 189 26.573 52.656 −44.569 1.00 48.28 C ATOM 7110 N ARG G 190 22.229 55.944 −45.331 1.00 38.37 N ATOM 7111 CA ARG G 190 21.156 56.193 −44.379 1.00 37.86 C ATOM 7112 C ARG G 190 20.976 54.940 −43.522 1.00 35.87 C ATOM 7113 O ARG G 190 21.118 53.823 −44.029 1.00 35.22 O ATOM 7114 CB ARG G 190 19.846 56.487 −45.108 1.00 39.91 C ATOM 7115 CG ARG G 190 19.989 57.359 −46.335 1.00 44.33 C ATOM 7116 CD ARG G 190 18.650 58.006 −46.693 1.00 47.36 C ATOM 7117 NE ARG G 190 17.538 57.053 −46.736 1.00 49.72 N ATOM 7118 CZ ARG G 190 17.388 56.103 −47.657 1.00 50.89 C ATOM 7119 NH1 ARG G 190 18.283 55.960 −48.627 1.00 51.57 N ATOM 7120 NH2 ARG G 190 16.329 55.303 −47.617 1.00 51.62 N ATOM 7121 N TRP G 191 20.658 55.127 −42.242 1.00 33.21 N ATOM 7122 CA TRP G 191 20.450 54.005 −41.329 1.00 32.38 C ATOM 7123 C TRP G 191 19.009 53.896 −40.842 1.00 31.73 C ATOM 7124 O TRP G 191 18.397 54.893 −40.474 1.00 32.66 O ATOM 7125 CB TRP G 191 21.373 54.140 −40.118 1.00 32.19 C ATOM 7126 CG TRP G 191 22.800 53.886 −40.446 1.00 32.15 C ATOM 7127 CD1 TRP G 191 23.724 54.792 −40.894 1.00 32.51 C ATOM 7128 CD2 TRP G 191 23.468 52.627 −40.378 1.00 31.70 C ATOM 7129 NE1 TRP G 191 24.929 54.166 −41.108 1.00 32.76 N ATOM 7130 CE2 TRP G 191 24.798 52.837 −40.797 1.00 31.62 C ATOM 7131 CE3 TRP G 191 23.068 51.338 −40.007 1.00 31.89 C ATOM 7132 CZ2 TRP G 191 25.734 51.805 −40.848 1.00 31.49 C ATOM 7133 CZ3 TRP G 191 23.994 50.313 −40.058 1.00 30.94 C ATOM 7134 CH2 TRP G 191 25.317 50.554 −40.477 1.00 31.73 C ATOM 7135 N LEU G 192 18.470 52.684 −40.827 1.00 30.78 N ATOM 7136 CA LEU G 192 17.109 52.480 −40.368 1.00 31.16 C ATOM 7137 C LEU G 192 17.086 51.589 −39.129 1.00 31.29 C ATOM 7138 O LEU G 192 17.950 50.721 −38.956 1.00 31.14 O ATOM 7139 CB LEU G 192 16.268 51.819 −41.468 1.00 31.89 C ATOM 7140 CG LEU G 192 16.364 52.423 −42.873 1.00 32.22 C ATOM 7141 CD1 LEU G 192 15.550 51.569 −43.842 1.00 32.92 C ATOM 7142 CD2 LEU G 192 15.869 53.877 −42.859 1.00 31.73 C ATOM 7143 N LYS G 193 16.111 51.824 −38.255 1.00 30.53 N ATOM 7144 CA LYS G 193 15.942 50.994 −37.079 1.00 30.93 C ATOM 7145 C LYS G 193 14.587 50.325 −37.276 1.00 31.82 C ATOM 7146 O LYS G 193 13.568 51.007 −37.385 1.00 32.06 O ATOM 7147 CB LYS G 193 15.939 51.812 −35.787 1.00 29.89 C ATOM 7148 CG LYS G 193 15.739 50.917 −34.559 1.00 30.55 C ATOM 7149 CD LYS G 193 15.637 51.684 −33.249 1.00 31.57 C ATOM 7150 CE LYS G 193 15.409 50.732 −32.072 1.00 31.81 C ATOM 7151 NZ LYS G 193 15.123 51.443 −30.793 1.00 32.09 N ATOM 7152 N ASN G 194 14.580 48.998 −37.327 1.00 32.57 N ATOM 7153 CA ASN G 194 13.350 48.248 −37.535 1.00 34.51 C ATOM 7154 C ASN G 194 12.611 48.741 −38.785 1.00 35.41 C ATOM 7155 O ASN G 194 11.406 49.008 −38.743 1.00 34.59 O ATOM 7156 CB ASN G 194 12.430 48.361 −36.315 1.00 35.04 C ATOM 7157 CG ASN G 194 13.044 47.770 −35.072 1.00 36.73 C ATOM 7158 OD1 ASN G 194 13.762 46.756 −35.131 1.00 36.07 O ATOM 7159 ND2 ASN G 194 12.760 48.387 −33.926 1.00 36.25 N ATOM 7160 N GLY G 195 13.357 48.879 −39.881 1.00 35.42 N ATOM 7161 CA GLY G 195 12.792 49.307 −41.150 1.00 35.86 C ATOM 7162 C GLY G 195 12.275 50.730 −41.289 1.00 36.25 C ATOM 7163 O GLY G 195 11.630 51.046 −42.287 1.00 36.76 O ATOM 7164 N LYS G 196 12.542 51.591 −40.313 1.00 36.25 N ATOM 7165 CA LYS G 196 12.081 52.973 −40.384 1.00 36.21 C ATOM 7166 C LYS G 196 13.219 53.913 −40.029 1.00 36.72 C ATOM 7167 O LYS G 196 14.177 53.515 −39.371 1.00 36.32 O ATOM 7168 CB LYS G 196 10.905 53.205 −39.422 1.00 36.17 C ATOM 7169 N GLU G 197 13.104 55.163 −40.462 1.00 37.23 N ATOM 7170 CA GLU G 197 14.127 56.157 −40.185 1.00 38.95 C ATOM 7171 C GLU G 197 14.525 56.124 −38.715 1.00 38.68 C ATOM 7172 O GLU G 197 13.670 56.072 −37.833 1.00 38.67 O ATOM 7173 CB GLU G 197 13.627 57.554 −40.539 1.00 40.62 C ATOM 7174 CG GLU G 197 14.594 58.641 −40.127 1.00 44.22 C ATOM 7175 CD GLU G 197 14.039 60.023 −40.356 1.00 46.08 C ATOM 7176 OE1 GLU G 197 12.815 60.199 −40.157 1.00 46.92 O ATOM 7177 OE2 GLU G 197 14.825 60.930 −40.718 1.00 46.94 O ATOM 7178 N PHE G 198 15.834 56.146 −38.474 1.00 38.58 N ATOM 7179 CA PHE G 198 16.411 56.120 −37.131 1.00 38.05 C ATOM 7180 C PHE G 198 16.716 57.575 −36.776 1.00 38.47 C ATOM 7181 O PHE G 198 17.557 58.210 −37.418 1.00 38.57 O ATOM 7182 CB PHE G 198 17.714 55.307 −37.156 1.00 38.22 C ATOM 7183 CG PHE G 198 18.332 55.058 −35.794 1.00 38.04 C ATOM 7184 CD1 PHE G 198 19.673 54.676 −35.695 1.00 37.65 C ATOM 7185 CD2 PHE G 198 17.579 55.153 −34.628 1.00 37.37 C ATOM 7186 CE1 PHE G 198 20.256 54.392 −34.455 1.00 37.94 C ATOM 7187 CE2 PHE G 198 18.147 54.870 −33.384 1.00 38.19 C ATOM 7188 CZ PHE G 198 19.488 54.487 −33.295 1.00 38.35 C ATOM 7189 N LYS G 199 16.035 58.096 −35.760 1.00 38.43 N ATOM 7190 CA LYS G 199 16.215 59.479 −35.332 1.00 39.45 C ATOM 7191 C LYS G 199 16.990 59.590 −34.016 1.00 39.07 C ATOM 7192 O LYS G 199 16.950 58.680 −33.190 1.00 38.70 O ATOM 7193 CB LYS G 199 14.847 60.142 −35.143 1.00 41.28 C ATOM 7194 CG LYS G 199 13.883 60.012 −36.318 1.00 43.58 C ATOM 7195 CD LYS G 199 12.657 60.899 −36.082 1.00 45.84 C ATOM 7196 CE LYS G 199 11.660 60.854 −37.242 1.00 46.93 C ATOM 7197 NZ LYS G 199 10.503 61.786 −37.021 1.00 47.65 N ATOM 7198 N GLN G 200 17.677 60.714 −33.819 1.00 38.63 N ATOM 7199 CA GLN G 200 18.447 60.941 −32.597 1.00 38.68 C ATOM 7200 C GLN G 200 17.597 60.759 −31.338 1.00 39.23 C ATOM 7201 O GLN G 200 18.073 60.228 −30.337 1.00 39.32 O ATOM 7202 CB GLN G 200 19.047 62.355 −32.573 1.00 38.64 C ATOM 7203 CG GLN G 200 20.185 62.623 −33.561 1.00 38.51 C ATOM 7204 CD GLN G 200 21.456 61.819 −33.266 1.00 39.24 C ATOM 7205 OE1 GLN G 200 21.841 61.627 −32.104 1.00 38.68 O ATOM 7206 NE2 GLN G 200 22.119 61.363 −34.320 1.00 38.44 N ATOM 7207 N GLU G 201 16.340 61.191 −31.380 1.00 39.57 N ATOM 7208 CA GLU G 201 15.485 61.075 −30.201 1.00 39.85 C ATOM 7209 C GLU G 201 14.982 59.656 −29.939 1.00 39.23 C ATOM 7210 O GLU G 201 14.292 59.411 −28.952 1.00 38.51 O ATOM 7211 CB GLU G 201 14.283 62.026 −30.299 1.00 41.90 C ATOM 7212 CG GLU G 201 13.335 61.713 −31.445 1.00 45.60 C ATOM 7213 CD GLU G 201 13.526 62.640 −32.627 1.00 47.66 C ATOM 7214 OE1 GLU G 201 14.694 62.871 −33.025 1.00 48.51 O ATOM 7215 OE2 GLU G 201 12.500 63.132 −33.158 1.00 49.36 O ATOM 7216 N HIS G 202 15.335 58.716 −30.809 1.00 39.29 N ATOM 7217 CA HIS G 202 14.892 57.339 −30.637 1.00 38.89 C ATOM 7218 C HIS G 202 15.560 56.598 −29.466 1.00 38.13 C ATOM 7219 O HIS G 202 15.130 55.499 −29.099 1.00 37.78 O ATOM 7220 CB HIS G 202 15.095 56.552 −31.934 1.00 40.98 C ATOM 7221 CG HIS G 202 14.088 56.862 −33.000 1.00 43.91 C ATOM 7222 ND1 HIS G 202 12.890 57.500 −32.740 1.00 43.84 N ATOM 7223 CD2 HIS G 202 14.085 56.586 −34.328 1.00 44.08 C ATOM 7224 CE1 HIS G 202 12.197 57.602 −33.860 1.00 44.30 C ATOM 7225 NE2 HIS G 202 12.899 57.056 −34.838 1.00 44.94 N ATOM 7226 N ARG G 203 16.602 57.195 −28.883 1.00 37.18 N ATOM 7227 CA ARG G 203 17.312 56.589 −27.748 1.00 36.74 C ATOM 7228 C ARG G 203 18.032 57.642 −26.908 1.00 36.51 C ATOM 7229 O ARG G 203 18.412 58.695 −27.411 1.00 35.86 O ATOM 7230 CB ARG G 203 18.345 55.561 −28.236 1.00 37.01 C ATOM 7231 N ILE G 204 18.224 57.358 −25.624 1.00 36.85 N ATOM 7232 CA ILE G 204 18.925 58.297 −24.749 1.00 37.60 C ATOM 7233 C ILE G 204 20.325 58.518 −25.334 1.00 37.66 C ATOM 7234 O ILE G 204 21.041 57.553 −25.629 1.00 37.54 O ATOM 7235 CB ILE G 204 19.074 57.736 −23.302 1.00 38.46 C ATOM 7236 CG1 ILE G 204 17.712 57.316 −22.748 1.00 39.56 C ATOM 7237 CG2 ILE G 204 19.677 58.800 −22.375 1.00 39.44 C ATOM 7238 CD1 ILE G 204 16.709 58.438 −22.672 1.00 40.21 C ATOM 7239 N GLY G 205 20.708 59.778 −25.515 1.00 37.64 N ATOM 7240 CA GLY G 205 22.021 60.082 −26.062 1.00 37.39 C ATOM 7241 C GLY G 205 22.170 59.934 −27.567 1.00 36.81 C ATOM 7242 O GLY G 205 23.245 60.185 −28.109 1.00 37.10 O ATOM 7243 N GLY G 206 21.101 59.525 −28.246 1.00 36.83 N ATOM 7244 CA GLY G 206 21.154 59.373 −29.692 1.00 35.77 C ATOM 7245 C GLY G 206 22.266 58.480 −30.216 1.00 35.37 C ATOM 7246 O GLY G 206 22.643 57.496 −29.581 1.00 33.92 O ATOM 7247 N TYR G 207 22.794 58.831 −31.383 1.00 35.95 N ATOM 7248 CA TYR G 207 23.841 58.042 −32.003 1.00 36.65 C ATOM 7249 C TYR G 207 24.812 58.905 −32.809 1.00 37.12 C ATOM 7250 O TYR G 207 24.598 60.104 −32.982 1.00 36.47 O ATOM 7251 CB TYR G 207 23.207 56.980 −32.907 1.00 37.46 C ATOM 7252 CG TYR G 207 22.328 57.548 −33.999 1.00 38.06 C ATOM 7253 CD1 TYR G 207 20.953 57.716 −33.813 1.00 38.07 C ATOM 7254 CD2 TYR G 207 22.880 57.942 −35.218 1.00 38.57 C ATOM 7255 CE1 TYR G 207 20.148 58.268 −34.827 1.00 38.11 C ATOM 7256 CE2 TYR G 207 22.097 58.496 −36.227 1.00 38.57 C ATOM 7257 CZ TYR G 207 20.737 58.661 −36.031 1.00 39.30 C ATOM 7258 OH TYR G 207 19.994 59.266 −37.028 1.00 40.42 O ATOM 7259 N LYS G 208 25.880 58.284 −33.300 1.00 37.02 N ATOM 7260 CA LYS G 208 26.874 58.997 −34.088 1.00 38.49 C ATOM 7261 C LYS G 208 27.150 58.251 −35.396 1.00 39.32 C ATOM 7262 O LYS G 208 27.144 57.019 −35.437 1.00 38.90 O ATOM 7263 CB LYS G 208 28.174 59.150 −33.285 1.00 38.12 C ATOM 7264 CG LYS G 208 28.008 59.852 −31.932 1.00 38.59 C ATOM 7265 CD LYS G 208 29.342 59.926 −31.187 1.00 37.31 C ATOM 7266 CE LYS G 208 29.213 60.616 −29.838 1.00 37.57 C ATOM 7267 NZ LYS G 208 30.504 60.595 −29.087 1.00 36.21 N ATOM 7268 N VAL G 209 27.385 59.007 −36.464 1.00 40.76 N ATOM 7269 CA VAL G 209 27.668 58.431 −37.776 1.00 42.75 C ATOM 7270 C VAL G 209 28.932 59.040 −38.363 1.00 44.10 C ATOM 7271 O VAL G 209 29.083 60.260 −38.399 1.00 44.90 O ATOM 7272 CB VAL G 209 26.500 58.673 −38.774 1.00 42.78 C ATOM 7273 CG1 VAL G 209 26.929 58.275 −40.184 1.00 43.23 C ATOM 7274 CG2 VAL G 209 25.276 57.864 −38.360 1.00 42.54 C ATOM 7275 N ARG G 210 29.844 58.184 −38.809 1.00 45.61 N ATOM 7276 CA ARG G 210 31.092 58.632 −39.422 1.00 46.69 C ATOM 7277 C ARG G 210 31.070 58.207 −40.890 1.00 47.12 C ATOM 7278 O ARG G 210 31.463 57.091 −41.222 1.00 47.50 O ATOM 7279 CB ARG G 210 32.297 57.997 −38.716 1.00 46.16 C ATOM 7280 N ASN G 211 30.596 59.097 −41.759 1.00 47.91 N ATOM 7281 CA ASN G 211 30.513 58.819 −43.191 1.00 48.52 C ATOM 7282 C ASN G 211 31.803 58.251 −43.771 1.00 48.05 C ATOM 7283 O ASN G 211 31.772 57.335 −44.592 1.00 47.81 O ATOM 7284 CB ASN G 211 30.132 60.088 −43.950 1.00 49.91 C ATOM 7285 CG ASN G 211 28.724 60.549 −43.636 1.00 51.73 C ATOM 7286 CD1 ASN G 211 27.756 59.808 −43.832 1.00 53.25 O ATOM 7287 ND2 ASN G 211 28.597 61.779 −43.146 1.00 52.48 N ATOM 7288 N GLN G 212 32.937 58.791 −43.336 1.00 47.63 N ATOM 7289 CA GLN G 212 34.231 58.327 −43.823 1.00 46.56 C ATOM 7290 C GLN G 212 34.453 56.835 −43.559 1.00 45.40 C ATOM 7291 O GLN G 212 35.177 56.172 −44.296 1.00 46.16 O ATOM 7292 CB GLN G 212 35.354 59.149 −43.185 1.00 46.95 C ATOM 7293 N HIS G 213 33.823 56.305 −42.514 1.00 43.32 N ATOM 7294 CA HIS G 213 33.971 54.894 −42.180 1.00 41.09 C ATOM 7295 C HIS G 213 32.695 54.078 −42.437 1.00 38.71 C ATOM 7296 O HIS G 213 32.653 52.878 −42.149 1.00 37.89 O ATOM 7297 CB HIS G 213 34.401 54.757 −40.712 1.00 41.66 C ATOM 7298 N TRP G 214 31.675 54.732 −42.991 1.00 36.16 N ATOM 7299 CA TRP G 214 30.386 54.094 −43.288 1.00 34.68 C ATOM 7300 C TRP G 214 29.892 53.347 −42.056 1.00 33.39 C ATOM 7301 O TRP G 214 29.474 52.189 −42.132 1.00 32.36 O ATOM 7302 CB TRP G 214 30.523 53.123 −44.465 1.00 34.65 C ATOM 7303 CG TRP G 214 31.183 53.713 −45.677 1.00 35.68 C ATOM 7304 CD1 TRP G 214 32.509 53.657 −45.992 1.00 35.69 C ATOM 7305 CD2 TRP G 214 30.552 54.467 −46.723 1.00 35.33 C ATOM 7306 NE1 TRP G 214 32.744 54.329 −47.168 1.00 36.32 N ATOM 7307 CE2 TRP G 214 31.561 54.837 −47.637 1.00 35.75 C ATOM 7308 CE3 TRP G 214 29.232 54.867 −46.975 1.00 36.44 C ATOM 7309 CZ2 TRP G 214 31.293 55.592 −48.790 1.00 35.48 C ATOM 7310 CZ3 TRP G 214 28.963 55.620 −48.128 1.00 36.36 C ATOM 7311 CH2 TRP G 214 29.993 55.972 −49.017 1.00 35.54 C ATOM 7312 N SER G 215 29.918 54.032 −40.918 1.00 32.58 N ATOM 7313 CA SER G 215 29.522 53.412 −39.665 1.00 31.88 C ATOM 7314 C SER G 215 28.440 54.113 −38.852 1.00 31.15 C ATOM 7315 O SER G 215 28.246 55.321 −38.949 1.00 31.31 O ATOM 7316 CB SER G 215 30.758 53.283 −38.786 1.00 32.21 C ATOM 7317 OG SER G 215 31.302 54.577 −38.596 1.00 32.73 O ATOM 7318 N LEU G 216 27.761 53.319 −38.028 1.00 30.57 N ATOM 7319 CA LEU G 216 26.729 53.798 −37.111 1.00 29.12 C ATOM 7320 C LEU G 216 27.234 53.394 −35.724 1.00 27.81 C ATOM 7321 O LEU G 216 27.577 52.231 −35.506 1.00 26.76 O ATOM 7322 CB LEU G 216 25.382 53.120 −37.391 1.00 29.27 C ATOM 7323 CG LEU G 216 24.282 53.271 −36.319 1.00 29.94 C ATOM 7324 CD1 LEU G 216 23.772 54.696 −36.292 1.00 28.63 C ATOM 7325 CD2 LEU G 216 23.128 52.337 −36.620 1.00 28.50 C ATOM 7326 N ILE G 217 27.277 54.347 −34.798 1.00 27.49 N ATOM 7327 CA ILE G 217 27.759 54.084 −33.433 1.00 27.69 C ATOM 7328 C ILE G 217 26.751 54.413 −32.329 1.00 28.49 C ATOM 7329 O ILE G 217 26.180 55.515 −32.293 1.00 27.54 O ATOM 7330 CB ILE G 217 29.057 54.888 −33.145 1.00 29.03 C ATOM 7331 CG1 ILE G 217 30.190 54.373 −34.025 1.00 29.08 C ATOM 7332 CG2 ILE G 217 29.447 54.777 −31.676 1.00 28.67 C ATOM 7333 CD1 ILE G 217 31.406 55.232 −33.972 1.00 30.72 C ATOM 7334 N MET G 218 26.534 53.452 −31.430 1.00 28.14 N ATOM 7335 CA MET G 218 25.636 53.638 −30.295 1.00 29.05 C ATOM 7336 C MET G 218 26.429 53.316 −29.019 1.00 30.12 C ATOM 7337 O MET G 218 26.945 52.206 −28.856 1.00 29.60 O ATOM 7338 CB MET G 218 24.391 52.736 −30.397 1.00 28.75 C ATOM 7339 CG MET G 218 23.349 53.184 −31.437 1.00 30.25 C ATOM 7340 SD MET G 218 21.994 51.978 −31.723 1.00 31.16 S ATOM 7341 CE MET G 218 22.916 50.662 −32.561 1.00 31.17 C ATOM 7342 N GLU G 219 26.534 54.300 −28.132 1.00 29.92 N ATOM 7343 CA GLU G 219 27.273 54.150 −26.882 1.00 30.46 C ATOM 7344 C GLU G 219 26.370 53.744 −25.722 1.00 31.49 C ATOM 7345 O GLU G 219 25.172 54.041 −25.718 1.00 32.13 O ATOM 7346 CB GLU G 219 27.991 55.463 −26.546 1.00 31.02 C ATOM 7347 CG GLU G 219 28.927 55.949 −27.656 1.00 30.31 C ATOM 7348 CD GLU G 219 29.071 57.461 −27.685 1.00 31.67 C ATOM 7349 OE1 GLU G 219 28.054 58.150 −27.465 1.00 30.77 O ATOM 7350 OE2 GLU G 219 30.189 57.964 −27.951 1.00 32.04 O ATOM 7351 N SER G 220 26.953 53.035 −24.756 1.00 31.30 N ATOM 7352 CA SER G 220 26.254 52.572 −23.561 1.00 31.39 C ATOM 7353 C SER G 220 24.907 51.908 −23.847 1.00 31.55 C ATOM 7354 O SER G 220 23.869 52.337 −23.324 1.00 31.32 O ATOM 7355 CB SER G 220 26.054 53.752 −22.615 1.00 31.91 C ATOM 7356 OG SER G 220 27.249 54.506 −22.530 1.00 33.28 O ATOM 7357 N VAL G 221 24.923 50.843 −24.643 1.00 30.54 N ATOM 7358 CA VAL G 221 23.681 50.167 −24.998 1.00 31.16 C ATOM 7359 C VAL G 221 22.921 49.566 −23.818 1.00 32.05 C ATOM 7360 O VAL G 221 23.508 49.195 −22.792 1.00 31.21 O ATOM 7361 CB VAL G 221 23.908 49.060 −26.065 1.00 29.94 C ATOM 7362 CG1 VAL G 221 24.596 49.656 −27.279 1.00 30.06 C ATOM 7363 CG2 VAL G 221 24.719 47.916 −25.486 1.00 30.26 C ATOM 7364 N VAL G 222 21.602 49.472 −23.985 1.00 32.24 N ATOM 7365 CA VAL G 222 20.721 48.926 −22.965 1.00 32.79 C ATOM 7366 C VAL G 222 19.743 47.970 −23.629 1.00 33.65 C ATOM 7367 O VAL G 222 19.616 47.951 −24.855 1.00 33.38 O ATOM 7368 CB VAL G 222 19.942 50.049 −22.257 1.00 32.50 C ATOM 7369 CG1 VAL G 222 20.904 50.904 −21.451 1.00 32.43 C ATOM 7370 CG2 VAL G 222 19.224 50.913 −23.282 1.00 32.13 C ATOM 7371 N PRO G 223 19.043 47.151 −22.832 1.00 34.22 N ATOM 7372 CA PRO G 223 18.076 46.193 −23.376 1.00 34.37 C ATOM 7373 C PRO G 223 17.116 46.751 −24.430 1.00 34.67 C ATOM 7374 O PRO G 223 16.834 46.079 −25.418 1.00 35.07 O ATOM 7375 CB PRO G 223 17.353 45.699 −22.128 1.00 34.63 C ATOM 7376 CG PRO G 223 18.475 45.652 −21.127 1.00 34.57 C ATOM 7377 CD PRO G 223 19.208 46.963 −21.376 1.00 34.70 C ATOM 7378 N SER G 224 16.619 47.973 −24.240 1.00 34.52 N ATOM 7379 CA SER G 224 15.690 48.548 −25.214 1.00 34.43 C ATOM 7380 C SER G 224 16.277 48.819 −26.607 1.00 34.27 C ATOM 7381 O SER G 224 15.532 49.086 −27.550 1.00 33.93 O ATOM 7382 CB SER G 224 15.047 49.830 −24.659 1.00 35.29 C ATOM 7383 OG SER G 224 16.016 50.750 −24.181 1.00 37.46 O ATOM 7384 N ASP G 225 17.602 48.745 −26.748 1.00 34.38 N ATOM 7385 CA ASP G 225 18.246 48.966 −28.047 1.00 33.59 C ATOM 7386 C ASP G 225 18.114 47.746 −28.976 1.00 33.29 C ATOM 7387 O ASP G 225 18.444 47.810 −30.160 1.00 33.56 O ATOM 7388 CB ASP G 225 19.731 49.312 −27.860 1.00 33.90 C ATOM 7389 CG ASP G 225 19.940 50.698 −27.272 1.00 34.04 C ATOM 7390 OD1 ASP G 225 19.312 51.661 −27.760 1.00 34.35 O ATOM 7391 OD2 ASP G 225 20.744 50.832 −26.328 1.00 33.86 O ATOM 7392 N LYS G 226 17.634 46.630 −28.436 1.00 33.97 N ATOM 7393 CA LYS G 226 17.460 45.415 −29.238 1.00 33.58 C ATOM 7394 C LYS G 226 16.601 45.713 −30.452 1.00 32.76 C ATOM 7395 O LYS G 226 15.591 46.410 −30.348 1.00 33.24 O ATOM 7396 CB LYS G 226 16.782 44.311 −28.420 1.00 34.76 C ATOM 7397 N GLY G 227 17.002 45.187 −31.604 1.00 31.91 N ATOM 7398 CA GLY G 227 16.240 45.404 −32.818 1.00 31.44 C ATOM 7399 C GLY G 227 17.077 45.219 −34.073 1.00 32.34 C ATOM 7400 O GLY G 227 18.197 44.694 −34.010 1.00 32.28 O ATOM 7401 N ASN G 228 16.533 45.643 −35.211 1.00 31.51 N ATOM 7402 CA ASN G 228 17.231 45.543 −36.485 1.00 31.35 C ATOM 7403 C ASN G 228 17.734 46.889 −36.940 1.00 30.18 C ATOM 7404 O ASN G 228 17.019 47.885 −36.845 1.00 31.12 O ATOM 7405 CB ASN G 228 16.316 44.998 −37.568 1.00 32.51 C ATOM 7406 CG ASN G 228 15.927 43.586 −37.311 1.00 34.95 C ATOM 7407 OD1 ASN G 228 16.696 42.829 −36.730 1.00 35.67 O ATOM 7408 ND2 ASN G 228 14.732 43.206 −37.745 1.00 36.62 N ATOM 7409 N TYR G 229 18.965 46.911 −37.436 1.00 28.15 N ATOM 7410 CA TYR G 229 19.568 48.135 −37.933 1.00 28.01 C ATOM 7411 C TYR G 229 20.032 47.899 −39.365 1.00 27.46 C ATOM 7412 O TYR G 229 20.885 47.053 −39.630 1.00 26.42 O ATOM 7413 CB TYR G 229 20.721 48.568 −37.021 1.00 28.59 C ATOM 7414 CG TYR G 229 20.240 48.915 −35.629 1.00 29.21 C ATOM 7415 CD1 TYR G 229 20.033 47.925 −34.672 1.00 29.80 C ATOM 7416 CD2 TYR G 229 19.915 50.229 −35.293 1.00 30.39 C ATOM 7417 CE1 TYR G 229 19.505 48.236 −33.415 1.00 30.65 C ATOM 7418 CE2 TYR G 229 19.391 50.553 −34.040 1.00 29.83 C ATOM 7419 CZ TYR G 229 19.188 49.552 −33.108 1.00 30.76 C ATOM 7420 OH TYR G 229 18.659 49.867 −31.872 1.00 32.33 O ATOM 7421 N THR G 230 19.449 48.666 −40.282 1.00 26.96 N ATOM 7422 CA THR G 230 19.729 48.536 −41.705 1.00 26.33 C ATOM 7423 C THR G 230 20.432 49.731 −42.326 1.00 26.67 C ATOM 7424 O THR G 230 20.049 50.878 −42.097 1.00 26.83 O ATOM 7425 CB THR G 230 18.405 48.316 −42.456 1.00 27.36 C ATOM 7426 OG1 THR G 230 17.794 47.102 −41.986 1.00 27.11 O ATOM 7427 CG2 THR G 230 18.624 48.262 −43.966 1.00 26.38 C ATOM 7428 N CYS G 231 21.463 49.466 −43.120 1.00 27.19 N ATOM 7429 CA CYS G 231 22.168 50.549 −43.802 1.00 27.64 C ATOM 7430 C CYS G 231 21.734 50.506 −45.268 1.00 27.64 C ATOM 7431 O CYS G 231 21.714 49.442 −45.889 1.00 27.09 O ATOM 7432 CB CYS G 231 23.687 50.362 −43.715 1.00 29.07 C ATOM 7433 SG CYS G 231 24.273 48.894 −44.592 1.00 31.30 S ATOM 7434 N VAL G 232 21.361 51.665 −45.802 1.00 28.82 N ATOM 7435 CA VAL G 232 20.943 51.801 −47.200 1.00 29.71 C ATOM 7436 C VAL G 232 21.951 52.730 −47.897 1.00 30.46 C ATOM 7437 O VAL G 232 22.177 53.858 −47.457 1.00 29.38 O ATOM 7438 CB VAL G 232 19.520 52.421 −47.317 1.00 29.90 C ATOM 7439 CG1 VAL G 232 19.074 52.407 −48.776 1.00 29.33 C ATOM 7440 CG2 VAL G 232 18.529 51.641 −46.448 1.00 29.15 C ATOM 7441 N VAL G 233 22.557 52.247 −48.978 1.00 30.43 N ATOM 7442 CA VAL G 233 23.561 53.021 −49.695 1.00 31.82 C ATOM 7443 C VAL G 233 23.155 53.193 −51.154 1.00 32.71 C ATOM 7444 O VAL G 233 22.792 52.223 −51.819 1.00 33.76 O ATOM 7445 CB VAL G 233 24.949 52.333 −49.554 1.00 30.72 C ATOM 7446 CG1 VAL G 233 26.000 53.059 −50.359 1.00 30.29 C ATOM 7447 CG2 VAL G 233 25.353 52.328 −48.070 1.00 30.62 C ATOM 7448 N GLU G 234 23.201 54.424 −51.653 1.00 33.51 N ATOM 7449 CA GLU G 234 22.775 54.655 −53.025 1.00 35.10 C ATOM 7450 C GLU G 234 23.320 55.855 −53.796 1.00 34.23 C ATOM 7451 O GLU G 234 23.822 56.826 −53.229 1.00 34.30 O ATOM 7452 CB GLU G 234 21.246 54.698 −53.068 1.00 37.35 C ATOM 7453 CG GLU G 234 20.648 55.776 −52.190 1.00 40.83 C ATOM 7454 CD GLU G 234 19.198 55.499 −51.810 1.00 44.47 C ATOM 7455 OE1 GLU G 234 18.643 56.288 −51.012 1.00 44.70 O ATOM 7456 OE2 GLU G 234 18.616 54.496 −52.295 1.00 44.42 O ATOM 7457 N ASN G 235 23.221 55.737 −55.116 1.00 34.32 N ATOM 7458 CA ASN G 235 23.623 56.772 −56.065 1.00 34.06 C ATOM 7459 C ASN G 235 22.688 56.604 −57.264 1.00 34.55 C ATOM 7460 O ASN G 235 21.763 55.780 −57.216 1.00 33.77 O ATOM 7461 CB ASN G 235 25.116 56.656 −56.474 1.00 32.59 C ATOM 7462 CG ASN G 235 25.446 55.400 −57.288 1.00 32.92 C ATOM 7463 OD1 ASN G 235 24.578 54.736 −57.843 1.00 32.10 O ATOM 7464 ND2 ASN G 235 26.738 55.095 −57.382 1.00 32.83 N ATOM 7465 N GLU G 236 22.917 57.366 −58.330 1.00 35.00 N ATOM 7466 CA GLU G 236 22.070 57.312 −59.524 1.00 35.86 C ATOM 7467 C GLU G 236 21.952 55.943 −60.214 1.00 36.60 C ATOM 7468 O GLU G 236 20.968 55.684 −60.910 1.00 36.50 O ATOM 7469 CB GLU G 236 22.558 58.340 −60.557 1.00 35.14 C ATOM 7470 N TYR G 237 22.944 55.073 −60.028 1.00 36.16 N ATOM 7471 CA TYR G 237 22.919 53.755 −60.665 1.00 36.25 C ATOM 7472 C TYR G 237 22.503 52.583 −59.780 1.00 35.75 C ATOM 7473 O TYR G 237 22.574 51.436 −60.215 1.00 35.24 O ATOM 7474 CB TYR G 237 24.284 53.425 −61.279 1.00 36.51 C ATOM 7475 CG TYR G 237 24.811 54.520 −62.154 1.00 38.18 C ATOM 7476 CD1 TYR G 237 25.831 55.355 −61.708 1.00 38.95 C ATOM 7477 CD2 TYR G 237 24.239 54.775 −63.400 1.00 37.89 C ATOM 7478 CE1 TYR G 237 26.270 56.421 −62.478 1.00 40.57 C ATOM 7479 CE2 TYR G 237 24.661 55.836 −64.174 1.00 39.83 C ATOM 7480 CZ TYR G 237 25.680 56.663 −63.705 1.00 41.20 C ATOM 7481 OH TYR G 237 26.095 57.745 −64.450 1.00 42.74 O ATOM 7482 N GLY G 238 22.082 52.842 −58.548 1.00 34.93 N ATOM 7483 CA GLY G 238 21.677 51.723 −57.719 1.00 34.22 C ATOM 7484 C GLY G 238 21.493 51.987 −56.242 1.00 33.59 C ATOM 7485 O GLY G 238 21.898 53.026 −55.719 1.00 34.04 O ATOM 7486 N SER G 239 20.887 51.011 −55.575 1.00 32.54 N ATOM 7487 CA SER G 239 20.616 51.076 −54.146 1.00 32.28 C ATOM 7488 C SER G 239 20.735 49.675 −53.544 1.00 31.72 C ATOM 7489 O SER G 239 20.105 48.735 −54.029 1.00 31.16 O ATOM 7490 CB SER G 239 19.210 51.617 −53.908 1.00 32.19 C ATOM 7491 OG SER G 239 18.886 51.583 −52.532 1.00 34.32 O ATOM 7492 N ILE G 240 21.551 49.538 −52.498 1.00 30.28 N ATOM 7493 CA ILE G 240 21.747 48.247 −51.835 1.00 28.68 C ATOM 7494 C ILE G 240 21.654 48.410 −50.321 1.00 28.11 C ATOM 7495 O ILE G 240 21.912 49.483 −49.798 1.00 28.31 O ATOM 7496 CB ILE G 240 23.128 47.621 −52.181 1.00 27.78 C ATOM 7497 CG1 ILE G 240 24.268 48.533 −51.702 1.00 27.45 C ATOM 7498 CG2 ILE G 240 23.219 47.361 −53.663 1.00 26.24 C ATOM 7499 CD1 ILE G 240 25.679 48.024 −52.049 1.00 26.01 C ATOM 7500 N ASN G 241 21.279 47.343 −49.623 1.00 28.01 N ATOM 7501 CA ASN G 241 21.152 47.393 −48.170 1.00 27.97 C ATOM 7502 C ASN G 241 21.662 46.128 −47.474 1.00 27.84 C ATOM 7503 O ASN G 241 21.829 45.082 −48.098 1.00 27.55 O ATOM 7504 CB ASN G 241 19.693 47.622 −47.773 1.00 27.81 C ATOM 7505 CG ASN G 241 18.771 46.552 −48.317 1.00 29.79 C ATOM 7506 OD1 ASN G 241 18.122 46.736 −49.362 1.00 31.16 O ATOM 7507 ND2 ASN G 241 18.717 45.419 −47.630 1.00 28.96 N ATOM 7508 N HIS G 242 21.884 46.245 −46.167 1.00 27.95 N ATOM 7509 CA HIS G 242 22.367 45.146 −45.334 1.00 27.69 C ATOM 7510 C HIS G 242 21.748 45.312 −43.949 1.00 26.95 C ATOM 7511 O HIS G 242 21.585 46.421 −43.474 1.00 26.62 O ATOM 7512 CB HIS G 242 23.888 45.223 −45.226 1.00 28.03 C ATOM 7513 CG HIS G 242 24.485 44.178 −44.337 1.00 29.55 C ATOM 7514 ND1 HIS G 242 24.727 42.889 −44.762 1.00 29.30 N ATOM 7515 CD2 HIS G 242 24.886 44.231 −43.043 1.00 29.73 C ATOM 7516 CE1 HIS G 242 25.252 42.193 −43.769 1.00 29.52 C ATOM 7517 NE2 HIS G 242 25.359 42.983 −42.716 1.00 29.51 N ATOM 7518 N THR G 243 21.418 44.214 −43.286 1.00 27.81 N ATOM 7519 CA THR G 243 20.789 44.322 −41.983 1.00 28.78 C ATOM 7520 C THR G 243 21.498 43.589 −40.853 1.00 29.90 C ATOM 7521 O THR G 243 21.907 42.432 −40.994 1.00 29.15 O ATOM 7522 CB THR G 243 19.318 43.848 −42.051 1.00 29.58 C ATOM 7523 OG1 THR G 243 18.584 44.714 −42.931 1.00 28.66 O ATOM 7524 CG2 THR G 243 18.681 43.873 −40.670 1.00 27.96 C ATOM 7525 N TYR G 244 21.639 44.300 −39.736 1.00 30.30 N ATOM 7526 CA TYR G 244 22.269 43.789 −38.530 1.00 32.40 C ATOM 7527 C TYR G 244 21.192 43.618 −37.463 1.00 34.01 C ATOM 7528 O TYR G 244 20.216 44.379 −37.433 1.00 33.67 O ATOM 7529 CB TYR G 244 23.304 44.789 −38.004 1.00 33.37 C ATOM 7530 CG TYR G 244 24.582 44.848 −38.803 1.00 34.79 C ATOM 7531 CD1 TYR G 244 24.986 46.029 −39.422 1.00 34.97 C ATOM 7532 CD2 TYR G 244 25.396 43.719 −38.935 1.00 34.57 C ATOM 7533 CE1 TYR G 244 26.180 46.089 −40.158 1.00 35.52 C ATOM 7534 CE2 TYR G 244 26.584 43.764 −39.661 1.00 35.11 C ATOM 7535 CZ TYR G 244 26.970 44.950 −40.269 1.00 35.69 C ATOM 7536 OH TYR G 244 28.147 45.001 −40.973 1.00 35.60 O ATOM 7537 N HIS G 245 21.376 42.635 −36.590 1.00 34.92 N ATOM 7538 CA HIS G 245 20.442 42.396 −35.491 1.00 36.03 C ATOM 7539 C HIS G 245 21.217 42.634 −34.196 1.00 35.26 C ATOM 7540 O HIS G 245 22.309 42.093 −34.019 1.00 34.39 O ATOM 7541 CB HIS G 245 19.919 40.953 −35.545 1.00 38.91 C ATOM 7542 CG HIS G 245 19.299 40.594 −36.864 1.00 42.97 C ATOM 7543 ND1 HIS G 245 18.057 41.050 −37.249 1.00 45.08 N ATOM 7544 CD2 HIS G 245 19.777 39.882 −37.912 1.00 44.45 C ATOM 7545 CE1 HIS G 245 17.797 40.643 −38.483 1.00 44.93 C ATOM 7546 NE2 HIS G 245 18.831 39.935 −38.908 1.00 45.92 N ATOM 7547 N LEU G 246 20.667 43.456 −33.306 1.00 34.64 N ATOM 7548 CA LEU G 246 21.333 43.748 −32.043 1.00 34.91 C ATOM 7549 C LEU G 246 20.606 43.181 −30.825 1.00 35.69 C ATOM 7550 O LEU G 246 19.384 43.278 −30.713 1.00 35.58 O ATOM 7551 CB LEU G 246 21.494 45.260 −31.862 1.00 35.44 C ATOM 7552 CG LEU G 246 22.063 45.734 −30.517 1.00 36.47 C ATOM 7553 CD1 LEU G 246 23.469 45.183 −30.336 1.00 36.34 C ATOM 7554 CD2 LEU G 246 22.076 47.253 −30.460 1.00 35.04 C ATOM 7555 N ASP G 247 21.369 42.587 −29.913 1.00 36.18 N ATOM 7556 CA ASP G 247 20.816 42.051 −28.681 1.00 37.30 C ATOM 7557 C ASP G 247 21.720 42.476 −27.527 1.00 37.80 C ATOM 7558 O ASP G 247 22.947 42.445 −27.638 1.00 37.40 O ATOM 7559 CB ASP G 247 20.715 40.532 −28.732 1.00 39.92 C ATOM 7560 CG ASP G 247 19.307 40.044 −28.452 1.00 41.73 C ATOM 7561 OD1 ASP G 247 18.633 39.593 −29.404 1.00 42.63 O ATOM 7562 OD2 ASP G 247 18.871 40.127 −27.282 1.00 42.31 O ATOM 7563 N VAL G 248 21.111 42.891 −26.423 1.00 37.48 N ATOM 7564 CA VAL G 248 21.876 43.331 −25.268 1.00 37.97 C ATOM 7565 C VAL G 248 21.620 42.443 −24.059 1.00 38.56 C ATOM 7566 O VAL G 248 20.473 42.099 −23.762 1.00 38.74 O ATOM 7567 CB VAL G 248 21.530 44.796 −24.904 1.00 38.63 C ATOM 7568 CG1 VAL G 248 22.373 45.261 −23.724 1.00 37.78 C ATOM 7569 CG2 VAL G 248 21.775 45.695 −26.110 1.00 38.73 C ATOM 7570 N VAL G 249 22.696 42.078 −23.364 1.00 38.33 N ATOM 7571 CA VAL G 249 22.595 41.228 −22.186 1.00 38.35 C ATOM 7572 C VAL G 249 23.224 41.900 −20.964 1.00 38.07 C ATOM 7573 O VAL G 249 24.374 42.338 −21.000 1.00 37.99 O ATOM 7574 CB VAL G 249 23.286 39.868 −22.422 1.00 39.59 C ATOM 7575 CG1 VAL G 249 23.101 38.982 −21.209 1.00 40.52 C ATOM 7576 CG2 VAL G 249 22.708 39.192 −23.662 1.00 39.36 C ATOM 7577 N GLU G 250 22.462 41.991 −19.880 1.00 37.91 N ATOM 7578 CA GLU G 250 22.974 42.605 −18.665 1.00 37.55 C ATOM 7579 C GLU G 250 23.748 41.569 −17.876 1.00 37.14 C ATOM 7580 O GLU G 250 23.253 40.469 −17.621 1.00 36.70 O ATOM 7581 CB GLU G 250 21.837 43.154 −17.798 1.00 39.01 C ATOM 7582 CG GLU G 250 21.151 44.384 −18.372 1.00 41.78 C ATOM 7583 CD GLU G 250 19.883 44.749 −17.620 1.00 43.62 C ATOM 7584 OE1 GLU G 250 18.917 43.948 −17.651 1.00 44.58 O ATOM 7585 OE2 GLU G 250 19.858 45.831 −17.000 1.00 44.67 O ATOM 7586 N ARG G 251 24.972 41.916 −17.501 1.00 35.77 N ATOM 7587 CA ARG G 251 25.795 41.008 −16.730 1.00 35.07 C ATOM 7588 C ARG G 251 25.875 41.462 −15.282 1.00 35.93 C ATOM 7589 O ARG G 251 25.762 42.656 −14.981 1.00 36.05 O ATOM 7590 CB ARG G 251 27.218 40.907 −17.314 1.00 33.17 C ATOM 7591 CG ARG G 251 27.311 40.440 −18.771 1.00 30.95 C ATOM 7592 CD ARG G 251 26.466 39.204 −19.068 1.00 29.63 C ATOM 7593 NE ARG G 251 26.826 38.035 −18.268 1.00 27.31 N ATOM 7594 CZ ARG G 251 27.877 37.261 −18.507 1.00 28.64 C ATOM 7595 NH1 ARG G 251 28.683 37.530 −19.528 1.00 29.00 N ATOM 7596 NH2 ARG G 251 28.120 36.206 −17.732 1.00 28.89 N ATOM 7597 N SER G 252 26.071 40.477 −14.404 1.00 36.15 N ATOM 7598 CA SER G 252 26.204 40.717 −12.978 1.00 36.84 C ATOM 7599 C SER G 252 27.497 40.097 −12.438 1.00 37.21 C ATOM 7600 O SER G 252 27.544 38.919 −12.112 1.00 37.64 O ATOM 7601 CB SER G 252 25.020 40.122 −12.217 1.00 36.67 C ATOM 7602 OG SER G 252 25.289 40.169 −10.825 1.00 38.12 O ATOM 7603 N PRO G 253 28.562 40.897 −12.319 1.00 37.48 N ATOM 7604 CA PRO G 253 29.847 40.407 −11.816 1.00 37.21 C ATOM 7605 C PRO G 253 29.925 40.268 −10.288 1.00 37.55 C ATOM 7606 O PRO G 253 30.909 40.681 −9.678 1.00 37.38 O ATOM 7607 CB PRO G 253 30.820 41.462 −12.329 1.00 37.06 C ATOM 7608 CG PRO G 253 30.026 42.718 −12.121 1.00 37.41 C ATOM 7609 CD PRO G 253 28.639 42.336 −12.640 1.00 37.48 C ATOM 7610 N HIS G 254 28.907 39.686 −9.667 1.00 37.32 N ATOM 7611 CA HIS G 254 28.918 39.538 −8.214 1.00 37.41 C ATOM 7612 C HIS G 254 29.057 38.081 −7.782 1.00 35.91 C ATOM 7613 O HIS G 254 28.788 37.161 −8.558 1.00 34.13 O ATOM 7614 CB HIS G 254 27.624 40.098 −7.606 1.00 39.83 C ATOM 7615 CG HIS G 254 27.299 41.496 −8.033 1.00 43.05 C ATOM 7616 ND1 HIS G 254 26.937 41.818 −9.325 1.00 44.40 N ATOM 7617 CD2 HIS G 254 27.256 42.655 −7.332 1.00 44.17 C ATOM 7618 CE1 HIS G 254 26.680 43.114 −9.400 1.00 44.30 C ATOM 7619 NE2 HIS G 254 26.866 43.644 −8.205 1.00 44.52 N ATOM 7620 N ARG G 255 29.493 37.874 −6.544 1.00 34.42 N ATOM 7621 CA ARG G 255 29.588 36.515 −6.015 1.00 34.16 C ATOM 7622 C ARG G 255 28.121 36.111 −5.763 1.00 32.44 C ATOM 7623 O ARG G 255 27.234 36.966 −5.773 1.00 31.37 O ATOM 7624 CB ARG G 255 30.409 36.501 −4.717 1.00 35.31 C ATOM 7625 CG ARG G 255 29.797 37.258 −3.545 1.00 39.42 C ATOM 7626 CD ARG G 255 30.819 37.447 −2.406 1.00 43.10 C ATOM 7627 NE ARG G 255 30.168 37.650 −1.109 1.00 47.00 N ATOM 7628 CZ ARG G 255 29.348 38.659 −0.816 1.00 47.84 C ATOM 7629 NH1 ARG G 255 29.068 39.587 −1.722 1.00 48.73 N ATOM 7630 NH2 ARG G 255 28.776 38.722 −0.379 1.00 49.38 N ATOM 7631 N PRO G 256 27.844 34.815 −5.537 1.00 31.88 N ATOM 7632 CA PRO G 256 26.449 34.411 −5.304 1.00 31.34 C ATOM 7633 C PRO G 256 25.767 35.139 −4.142 1.00 30.86 C ATOM 7634 O PRO G 256 26.384 35.404 −3.113 1.00 30.32 O ATOM 7635 CB PRO G 256 26.559 32.906 −5.026 1.00 30.69 C ATOM 7636 CG PRO G 256 27.860 32.509 −5.643 1.00 30.92 C ATOM 7637 CD PRO G 256 28.749 33.677 −5.306 1.00 31.69 C ATOM 7638 N ILE G 257 24.487 35.452 −4.318 1.00 30.45 N ATOM 7639 CA ILE G 257 23.695 36.120 −3.290 1.00 31.29 C ATOM 7640 C ILE G 257 22.616 35.161 −2.753 1.00 31.09 C ATOM 7641 O ILE G 257 21.915 34.514 −3.529 1.00 30.89 O ATOM 7642 CB ILE G 257 23.023 37.378 −3.880 1.00 33.41 C ATOM 7643 CG1 ILE G 257 24.071 38.488 −4.033 1.00 34.71 C ATOM 7644 CG2 ILE G 257 21.853 37.830 −3.008 1.00 33.59 C ATOM 7645 CD1 ILE G 257 23.570 39.723 −4.772 1.00 36.23 C ATOM 7646 N LEU G 258 22.496 35.044 −1.434 1.00 30.76 N ATOM 7647 CA LEU G 258 21.473 34.171 −0.853 1.00 30.21 C ATOM 7648 C LEU G 258 20.361 34.984 −0.214 1.00 30.61 C ATOM 7649 O LEU G 258 20.577 36.106 0.249 1.00 30.83 O ATOM 7650 CB LEU G 258 22.045 33.250 0.226 1.00 29.39 C ATOM 7651 CG LEU G 258 23.313 32.433 0.000 1.00 30.50 C ATOM 7652 CD1 LEU G 258 23.439 31.416 1.128 1.00 29.89 C ATOM 7653 CD2 LEU G 258 23.274 31.740 −1.323 1.00 31.22 C ATOM 7654 N GLN G 259 19.169 34.400 −0.176 1.00 30.63 N ATOM 7655 CA GLN G 259 18.007 35.044 0.430 1.00 30.35 C ATOM 7656 C GLN G 259 18.169 35.089 1.957 1.00 29.51 C ATOM 7657 O GLN G 259 18.481 34.082 2.585 1.00 28.56 O ATOM 7658 CB GLN G 259 16.742 34.248 0.056 1.00 30.66 C ATOM 7659 CG GLN G 259 15.410 34.765 0.645 1.00 31.63 C ATOM 7660 CD GLN G 259 14.201 33.887 0.256 1.00 32.94 C ATOM 7661 OE1 GLN G 259 14.012 33.548 −0.915 1.00 30.95 O ATOM 7662 NE2 GLN G 259 13.380 33.529 1.245 1.00 32.93 N ATOM 7663 N ALA G 260 17.941 36.258 2.545 1.00 29.30 N ATOM 7664 CA ALA G 260 18.036 36.430 3.992 1.00 30.20 C ATOM 7665 C ALA G 260 17.020 35.540 4.715 1.00 30.29 C ATOM 7666 O ALA G 260 15.900 35.402 4.261 1.00 30.30 O ATOM 7667 CB ALA G 260 17.772 37.890 4.344 1.00 29.19 C ATOM 7668 N GLY G 261 17.410 34.944 5.838 1.00 30.71 N ATOM 7669 CA GLY G 261 16.485 34.103 6.580 1.00 31.64 C ATOM 7670 C GLY G 261 16.518 32.621 6.241 1.00 32.25 C ATOM 7671 O GLY G 261 15.954 31.802 6.970 1.00 32.41 O ATOM 7672 N LEU G 262 17.179 32.267 5.144 1.00 32.52 N ATOM 7673 CA LEU G 262 17.267 30.871 4.733 1.00 32.03 C ATOM 7674 C LEU G 262 18.710 30.396 4.629 1.00 32.97 C ATOM 7675 O LEU G 262 19.570 31.082 4.067 1.00 32.65 O ATOM 7676 CB LEU G 262 16.563 30.672 3.387 1.00 31.14 C ATOM 7677 CG LEU G 262 15.043 30.883 3.387 1.00 31.83 C ATOM 7678 CD1 LEU G 262 14.494 30.812 1.956 1.00 29.95 C ATOM 7679 CD2 LEU G 262 14.391 29.819 4.274 1.00 30.39 C ATOM 7680 N PRO G 263 18.996 29.203 5.159 1.00 33.16 N ATOM 7681 CA PRO G 263 18.042 28.315 5.835 1.00 34.27 C ATOM 7682 C PRO G 263 17.585 28.826 7.205 1.00 34.96 C ATOM 7683 O PRO G 263 18.212 29.698 7.802 1.00 35.11 O ATOM 7684 CB PRO G 263 18.812 26.999 5.920 1.00 33.84 C ATOM 7685 CG PRO G 263 20.232 27.461 6.068 1.00 33.03 C ATOM 7686 CD PRO G 263 20.318 28.568 5.048 1.00 33.06 C ATOM 7687 N ALA G 264 16.480 28.281 7.698 1.00 36.21 N ATOM 7688 CA ALA G 264 15.943 28.691 8.989 1.00 37.11 C ATOM 7689 C ALA G 264 16.253 27.668 10.069 1.00 37.99 C ATOM 7690 O ALA G 264 16.396 26.480 9.782 1.00 37.70 O ATOM 7691 CB ALA G 264 14.452 28.878 8.884 1.00 36.73 C ATOM 7692 N ASN G 265 16.376 28.133 11.308 1.00 38.67 N ATOM 7693 CA ASN G 265 16.628 27.231 12.420 1.00 39.92 C ATOM 7694 C ASN G 265 15.461 26.251 12.498 1.00 41.13 C ATOM 7695 O ASN G 265 14.341 26.565 12.087 1.00 40.63 O ATOM 7696 CB ASN G 265 16.722 27.992 13.745 1.00 38.98 C ATOM 7697 CG ASN G 265 17.911 28.931 13.802 1.00 39.26 C ATOM 7698 OD1 ASN G 265 19.043 28.545 13.504 1.00 37.60 O ATOM 7699 ND2 ASN G 265 17.660 30.173 14.199 1.00 39.35 N ATOM 7700 N ALA G 266 15.731 25.063 13.019 1.00 42.71 N ATOM 7701 CA ALA G 266 14.699 24.046 13.150 1.00 44.36 C ATOM 7702 C ALA G 266 14.875 23.271 14.449 1.00 45.34 C ATOM 7703 O ALA G 266 15.987 23.126 14.966 1.00 45.07 O ATOM 7704 CB ALA G 266 14.737 23.100 11.955 1.00 44.26 C ATOM 7705 N SER G 267 13.760 22.783 14.977 1.00 46.57 N ATOM 7706 CA SER G 267 13.777 22.033 16.218 1.00 47.52 C ATOM 7707 C SER G 267 12.839 20.837 16.111 1.00 47.89 C ATOM 7708 O SER G 267 11.818 20.890 15.416 1.00 47.62 O ATOM 7709 CB SER G 267 13.355 22.953 17.365 1.00 47.81 C ATOM 7710 OG SER G 267 13.657 22.380 18.623 1.00 50.08 O ATOM 7711 N THR G 268 13.187 19.766 16.815 1.00 47.83 N ATOM 7712 CA THR G 268 12.378 18.555 16.799 1.00 48.09 C ATOM 7713 C THR G 268 12.770 17.581 17.902 1.00 48.10 C ATOM 7714 O THR G 268 13.812 17.728 18.546 1.00 48.04 O ATOM 7715 CB THR G 268 12.498 17.821 15.439 1.00 48.25 C ATOM 7716 OG1 THR G 268 11.534 16.765 15.384 1.00 49.55 O ATOM 7717 CG2 THR G 268 13.892 17.228 15.264 1.00 47.43 C ATOM 7718 N VAL G 269 11.916 16.587 18.117 1.00 48.14 N ATOM 7719 CA VAL G 269 12.168 15.558 19.117 1.00 47.99 C ATOM 7720 C VAL G 269 12.913 14.430 18.408 1.00 48.08 C ATOM 7721 O VAL G 269 12.789 14.276 17.191 1.00 47.63 O ATOM 7722 CB VAL G 269 10.843 15.000 19.699 1.00 48.00 C ATOM 7723 CG1 VAL G 269 10.074 16.103 20.404 1.00 48.03 C ATOM 7724 CG2 VAL G 269 10.000 14.402 18.590 1.00 47.84 C ATOM 7725 N VAL G 270 13.692 13.658 19.160 1.00 48.46 N ATOM 7726 CA VAL G 270 14.439 12.537 18.589 1.00 49.38 C ATOM 7727 C VAL G 270 13.463 11.695 17.768 1.00 49.64 C ATOM 7728 O VAL G 270 12.339 11.449 18.205 1.00 49.06 O ATOM 7729 CB VAL G 270 15.051 11.647 19.703 1.00 49.87 C ATOM 7730 CG1 VAL G 270 15.969 10.597 19.103 1.00 50.47 C ATOM 7731 CG2 VAL G 270 15.809 12.499 20.683 1.00 50.03 C ATOM 7732 N GLY G 271 13.883 11.274 16.579 1.00 50.39 N ATOM 7733 CA GLY G 271 13.014 10.468 15.741 1.00 51.54 C ATOM 7734 C GLY G 271 12.218 11.253 14.707 1.00 52.36 C ATOM 7735 O GLY G 271 11.567 10.661 13.843 1.00 53.06 O ATOM 7736 N GLY G 272 12.269 12.582 14.781 1.00 52.39 N ATOM 7737 CA GLY G 272 11.535 13.405 13.828 1.00 52.21 C ATOM 7738 C GLY G 272 12.212 13.623 12.479 1.00 51.67 C ATOM 7739 O GLY G 272 13.307 13.113 12.227 1.00 51.44 O ATOM 7740 N ASP G 273 11.544 14.377 11.608 1.00 51.20 N ATOM 7741 CA ASP G 273 12.050 14.697 10.275 1.00 51.38 C ATOM 7742 C ASP G 273 12.204 16.219 10.132 1.00 51.14 C ATOM 7743 O ASP G 273 11.428 16.988 10.708 1.00 51.64 O ATOM 7744 CB ASP G 273 11.080 14.169 9.213 1.00 51.73 C ATOM 7745 N VAL G 274 13.193 16.658 9.357 1.00 49.98 N ATOM 7746 CA VAL G 274 13.422 18.088 9.182 1.00 48.38 C ATOM 7747 C VAL G 274 14.020 18.447 7.817 1.00 47.58 C ATOM 7748 O VAL G 274 14.531 17.584 7.098 1.00 47.16 O ATOM 7749 CB VAL G 274 14.347 18.616 10.319 1.00 48.53 C ATOM 7750 CG1 VAL G 274 15.745 18.033 10.179 1.00 47.61 C ATOM 7751 CG2 VAL G 274 14.386 20.124 10.309 1.00 49.38 C ATOM 7752 N GLU G 275 13.936 19.725 7.460 1.00 45.89 N ATOM 7753 CA GLU G 275 14.483 20.203 6.199 1.00 44.90 C ATOM 7754 C GLU G 275 15.115 21.587 6.350 1.00 43.37 C ATOM 7755 O GLU G 275 14.771 22.348 7.256 1.00 42.50 O ATOM 7756 CB GLU G 275 13.389 20.277 5.133 1.00 45.32 C ATOM 7757 CG GLU G 275 12.250 21.234 5.466 1.00 46.56 C ATOM 7758 CD GLU G 275 11.430 21.615 4.237 1.00 47.38 C ATOM 7759 OE1 GLU G 275 11.349 20.793 3.306 1.00 47.81 O ATOM 7760 OE2 GLU G 275 10.860 22.732 4.204 1.00 47.98 O ATOM 7761 N PHE G 276 16.045 21.895 5.455 1.00 41.29 N ATOM 7762 CA PHE G 276 16.721 23.183 5.436 1.00 38.87 C ATOM 7763 C PHE G 276 16.654 23.656 3.997 1.00 38.05 C ATOM 7764 O PHE G 276 17.060 22.945 3.082 1.00 36.88 O ATOM 7765 CB PHE G 276 18.174 23.038 5.889 1.00 37.78 C ATOM 7766 CG PHE G 276 18.322 22.791 7.361 1.00 37.18 C ATOM 7767 CD1 PHE G 276 17.937 23.761 8.283 1.00 36.53 C ATOM 7768 CD2 PHE G 276 18.831 21.583 7.830 1.00 37.14 C ATOM 7769 CE1 PHE G 276 18.057 23.531 9.652 1.00 36.90 C ATOM 7770 CE2 PHE G 276 18.955 21.340 9.201 1.00 36.45 C ATOM 7771 CZ PHE G 276 18.569 22.312 10.114 1.00 36.22 C ATOM 7772 N VAL G 277 16.124 24.855 3.806 1.00 36.92 N ATOM 7773 CA VAL G 277 15.967 25.413 2.482 1.00 36.11 C ATOM 7774 C VAL G 277 16.952 26.540 2.235 1.00 35.68 C ATOM 7775 O VAL G 277 17.307 27.287 3.144 1.00 36.03 O ATOM 7776 CB VAL G 277 14.533 25.961 2.300 1.00 36.01 C ATOM 7777 CG1 VAL G 277 14.322 26.425 0.861 1.00 34.54 C ATOM 7778 CG2 VAL G 277 13.526 24.890 2.684 1.00 35.65 C ATOM 7779 N CYS G 278 17.376 26.666 0.989 1.00 35.24 N ATOM 7780 CA CYS G 278 18.304 27.710 0.605 1.00 35.03 C ATOM 7781 C CYS G 278 17.871 28.279 −0.743 1.00 34.25 C ATOM 7782 O CYS G 278 17.392 27.535 −1.596 1.00 34.32 O ATOM 7783 CB CYS G 278 19.711 27.126 0.499 1.00 34.63 C ATOM 7784 SG CYS G 278 20.943 28.361 0.107 1.00 37.73 S ATOM 7785 N LYS G 279 18.032 29.585 −0.934 1.00 33.28 N ATOM 7786 CA LYS G 279 17.663 30.229 −2.199 1.00 32.54 C ATOM 7787 C LYS G 279 18.828 31.074 −2.750 1.00 31.77 C ATOM 7788 O LYS G 279 19.179 32.127 −2.198 1.00 31.51 O ATOM 7789 CB LYS G 279 16.410 31.088 −2.007 1.00 32.60 C ATOM 7790 CG LYS G 279 15.881 31.721 −3.289 1.00 32.83 C ATOM 7791 CD LYS G 279 15.501 30.677 −4.328 1.00 33.81 C ATOM 7792 CE LYS G 279 15.072 31.338 −5.656 1.00 34.37 C ATOM 7793 NZ LYS G 279 15.047 30.360 −6.799 1.00 33.91 N ATOM 7794 N VAL G 280 19.402 30.602 −3.851 1.00 30.58 N ATOM 7795 CA VAL G 280 20.551 31.229 −4.495 1.00 30.54 C ATOM 7796 C VAL G 280 20.312 31.988 −5.819 1.00 30.94 C ATOM 7797 O VAL G 280 19.504 31.573 −6.653 1.00 31.37 O ATOM 7798 CB VAL G 280 21.629 30.144 −4.764 1.00 30.35 C ATOM 7799 CG1 VAL G 280 22.840 30.753 −5.462 1.00 28.62 C ATOM 7800 CG2 VAL G 280 22.024 29.465 −3.441 1.00 28.95 C ATOM 7801 N TYR G 281 21.039 33.091 −5.994 1.00 30.49 N ATOM 7802 CA TYR G 281 20.996 33.904 −7.212 1.00 30.69 C ATOM 7803 C TYR G 281 22.451 34.164 −7.679 1.00 29.61 C ATOM 7804 O TYR G 281 23.311 34.519 −6.876 1.00 28.43 O ATOM 7805 CB TYR G 281 20.301 35.261 −6.965 1.00 32.89 C ATOM 7806 CG TYR G 281 18.838 35.163 −6.557 1.00 34.84 C ATOM 7807 CD1 TYR G 281 18.475 35.110 −5.210 1.00 34.37 C ATOM 7808 CD2 TYR G 281 17.825 35.046 −7.523 1.00 35.01 C ATOM 7809 CE1 TYR G 281 17.155 34.933 −4.823 1.00 35.59 C ATOM 7810 CE2 TYR G 281 16.485 34.863 −7.142 1.00 36.56 C ATOM 7811 CZ TYR G 281 16.164 34.806 −5.785 1.00 36.55 C ATOM 7812 OH TYR G 281 14.866 34.587 −5.379 1.00 37.46 O ATOM 7813 N SER G 282 22.717 33.977 −8.969 1.00 29.00 N ATOM 7814 CA SER G 282 24.051 34.202 −9.526 1.00 29.05 C ATOM 7815 C SER G 282 24.029 34.209 −11.056 1.00 29.48 C ATOM 7816 O SER G 282 23.231 33.512 −11.680 1.00 29.98 O ATOM 7817 CB SER G 282 25.036 33.123 −9.036 1.00 29.21 C ATOM 7818 OG SER G 282 26.365 33.368 −9.502 1.00 27.34 O ATOM 7819 N ASP G 283 24.909 35.005 −11.647 1.00 29.24 N ATOM 7820 CA ASP G 283 25.040 35.106 −13.095 1.00 29.48 C ATOM 7821 C ASP G 283 26.001 33.974 −13.493 1.00 29.82 C ATOM 7822 O ASP G 283 25.638 33.038 −14.209 1.00 30.25 O ATOM 7823 CB ASP G 283 25.625 36.484 −13.436 1.00 30.69 C ATOM 7824 CG ASP G 283 25.872 36.673 −14.918 1.00 32.09 C ATOM 7825 OD1 ASP G 283 26.122 37.829 −15.329 1.00 31.64 O ATOM 7826 OD2 ASP G 283 25.829 35.677 −15.670 1.00 32.66 O ATOM 7827 N ALA G 284 27.231 34.072 −13.011 1.00 28.90 N ATOM 7828 CA ALA G 284 28.228 33.049 −13.264 1.00 29.34 C ATOM 7829 C ALA G 284 27.691 31.796 −12.571 1.00 29.13 C ATOM 7830 O ALA G 284 27.174 31.878 −11.460 1.00 29.66 O ATOM 7831 CB ALA G 284 29.573 33.464 −12.641 1.00 29.05 C ATOM 7832 N GLN G 285 27.809 30.649 −13.224 1.00 28.43 N ATOM 7833 CA GLN G 285 27.326 29.393 −12.668 1.00 28.02 C ATOM 7834 C GLN G 285 27.783 29.198 −11.216 1.00 27.99 C ATOM 7835 O GLN G 285 28.985 29.185 −10.936 1.00 27.38 O ATOM 7836 CB GLN G 285 27.857 28.239 −13.518 1.00 27.67 C ATOM 7837 CG GLN G 285 26.911 27.072 −13.569 1.00 27.62 C ATOM 7838 CD GLN G 285 25.564 27.477 −14.144 1.00 27.85 C ATOM 7839 OE1 GLN G 285 24.538 26.853 −13.851 1.00 27.45 O ATOM 7840 NE2 GLN G 285 25.562 28.519 −14.975 1.00 25.85 N ATOM 7841 N PRO G 286 26.839 29.047 −10.270 1.00 27.55 N ATOM 7842 CA PRO G 286 27.209 28.853 −8.865 1.00 27.38 C ATOM 7843 C PRO G 286 27.281 27.368 −8.474 1.00 28.25 C ATOM 7844 O PRO G 286 26.605 26.523 −9.069 1.00 28.01 O ATOM 7845 CB PRO G 286 26.096 29.563 −8.129 1.00 27.57 C ATOM 7846 CG PRO G 286 24.902 29.135 −8.945 1.00 28.55 C ATOM 7847 CD PRO G 286 25.402 29.355 −10.382 1.00 28.43 C ATOM 7848 N HIS G 287 28.105 27.065 −7.476 1.00 28.63 N ATOM 7849 CA HIS G 287 28.255 25.700 −6.980 1.00 29.45 C ATOM 7850 C HIS G 287 27.755 25.668 −5.544 1.00 29.49 C ATOM 7851 O HIS G 287 28.299 26.330 −4.667 1.00 28.79 O ATOM 7852 CB HIS G 287 29.712 25.238 −7.034 1.00 29.44 C ATOM 7853 CG HIS G 287 29.896 23.844 −6.533 1.00 30.98 C ATOM 7854 ND1 HIS G 287 30.438 23.563 −5.299 1.00 31.86 N ATOM 7855 CD2 HIS G 287 29.527 22.652 −7.062 1.00 31.38 C ATOM 7856 CE1 HIS G 287 30.391 22.258 −5.088 1.00 32.41 C ATOM 7857 NE2 HIS G 287 29.840 21.684 −6.142 1.00 31.49 N ATOM 7858 N ILE G 288 26.711 24.881 −5.322 1.00 29.94 N ATOM 7859 CA ILE G 288 26.064 24.781 −4.029 1.00 30.32 C ATOM 7860 C ILE G 288 26.328 23.478 −3.266 1.00 31.50 C ATOM 7861 O ILE G 288 26.301 22.385 −3.843 1.00 31.99 O ATOM 7862 CB ILE G 288 24.545 24.944 −4.230 1.00 29.55 C ATOM 7863 CG1 ILE G 288 24.280 26.221 −5.043 1.00 31.03 C ATOM 7864 CG2 ILE G 288 23.845 24.967 −2.899 1.00 30.04 C ATOM 7865 CD1 ILE G 288 22.817 26.443 −5.448 1.00 30.30 C ATOM 7866 N GLN G 289 26.577 23.594 −1.967 1.00 32.07 N ATOM 7867 CA GLN G 289 26.793 22.420 −1.131 1.00 33.10 C ATOM 7868 C GLN G 289 26.274 22.691 0.276 1.00 32.96 C ATOM 7869 O GLN G 289 26.144 23.846 0.688 1.00 32.94 O ATOM 7870 CB GLN G 289 28.276 22.047 −1.079 1.00 33.70 C ATOM 7871 CG GLN G 289 29.190 23.136 −0.572 1.00 34.69 C ATOM 7872 CD GLN G 289 30.652 22.724 −0.607 1.00 35.78 C ATOM 7873 OE1 GLN G 289 31.045 21.754 0.034 1.00 36.22 O ATOM 7874 NE2 GLN G 289 31.465 23.461 −1.360 1.00 36.39 N ATOM 7875 N TRP G 290 25.951 21.618 0.993 1.00 32.34 N ATOM 7876 CA TRP G 290 25.460 21.719 2.359 1.00 32.63 C ATOM 7877 C TRP G 290 26.526 21.162 3.292 1.00 34.01 C ATOM 7878 O TRP G 290 27.037 20.062 3.073 1.00 33.74 O ATOM 7879 CB TRP G 290 24.157 20.936 2.536 1.00 29.96 C ATOM 7880 CG TRP G 290 22.947 21.591 1.917 1.00 27.97 C ATOM 7881 CD1 TRP G 290 22.447 21.367 0.673 1.00 27.32 C ATOM 7882 CD2 TRP G 290 22.077 22.554 2.533 1.00 26.53 C ATOM 7883 NE1 TRP G 290 21.313 22.122 0.470 1.00 27.22 N ATOM 7884 CE2 TRP G 290 21.064 22.862 1.596 1.00 27.22 C ATOM 7885 CE3 TRP G 290 22.053 23.185 3.783 1.00 25.74 C ATOM 7886 CZ2 TRP G 290 20.031 23.775 1.873 1.00 25.60 C ATOM 7887 CZ3 TRP G 290 21.030 24.091 4.057 1.00 26.27 C ATOM 7888 CH2 TRP G 290 20.032 24.376 3.104 1.00 24.97 C ATOM 7889 N ILE G 291 26.847 21.921 4.335 1.00 36.02 N ATOM 7890 CA ILE G 291 27.879 21.533 5.289 1.00 39.06 C ATOM 7891 C ILE G 291 27.419 21.474 6.745 1.00 40.67 C ATOM 7892 O ILE G 291 26.645 22.310 7.203 1.00 40.96 O ATOM 7893 CB ILE G 291 29.065 22.517 5.242 1.00 38.79 C ATOM 7894 CG1 ILE G 291 29.506 22.748 3.796 1.00 40.06 C ATOM 7895 CG2 ILE G 291 30.209 21.977 6.079 1.00 39.37 C ATOM 7896 CD1 ILE G 291 30.620 23.789 3.648 1.00 40.28 C ATOM 7897 N LYS G 292 27.920 20.483 7.471 1.00 42.52 N ATOM 7898 CA LYS G 292 27.612 20.323 8.890 1.00 43.88 C ATOM 7899 C LYS G 292 28.903 20.642 9.645 1.00 45.12 C ATOM 7900 O LYS G 292 29.974 20.147 9.278 1.00 44.35 O ATOM 7901 CB LYS G 292 27.197 18.881 9.184 1.00 44.16 C ATOM 7902 CG LYS G 292 26.972 18.573 10.669 1.00 44.42 C ATOM 7903 CD LYS G 292 25.542 18.855 11.097 1.00 44.52 C ATOM 7904 CE LYS G 292 25.429 19.071 12.610 1.00 44.44 C ATOM 7905 NZ LYS G 292 25.810 17.882 13.428 1.00 43.93 N ATOM 7906 N HIS G 293 28.813 21.480 10.672 1.00 46.77 N ATOM 7907 CA HIS G 293 29.994 21.830 11.452 1.00 49.11 C ATOM 7908 C HIS G 293 30.218 20.751 12.510 1.00 49.79 C ATOM 7909 O HIS G 293 29.460 20.639 13.471 1.00 50.32 O ATOM 7910 CB HIS G 293 29.826 23.207 12.112 1.00 51.00 C ATOM 7911 CG HIS G 293 29.596 24.320 11.133 1.00 52.88 C ATOM 7912 ND1 HIS G 293 30.353 25.473 11.123 1.00 53.54 N ATOM 7913 CD2 HIS G 293 28.680 24.464 10.142 1.00 53.28 C ATOM 7914 CE1 HIS G 293 29.916 26.278 10.169 1.00 54.40 C ATOM 7915 NE2 HIS G 293 28.901 25.689 9.559 1.00 54.63 N ATOM 7916 N VAL G 294 31.249 19.938 12.309 1.00 50.90 N ATOM 7917 CA VAL G 294 31.557 18.859 13.242 1.00 51.86 C ATOM 7918 C VAL G 294 32.912 19.083 13.907 1.00 52.55 C ATOM 7919 O VAL G 294 33.369 18.263 14.708 1.00 53.84 O ATOM 7920 CB VAL G 294 31.579 17.488 12.521 1.00 51.46 C ATOM 7921 CG1 VAL G 294 31.594 16.363 13.543 1.00 52.54 C ATOM 7922 CG2 VAL G 294 30.371 17.356 11.610 1.00 51.18 C ATOM 7923 N TYR G 308 36.328 22.019 11.808 1.00 56.06 N ATOM 7924 CA TYR G 308 36.049 20.672 11.322 1.00 55.65 C ATOM 7925 C TYR G 308 34.711 20.650 10.588 1.00 55.26 C ATOM 7926 O TYR G 308 33.652 20.803 11.202 1.00 55.16 O ATOM 7927 CB TYR G 308 36.013 19.686 12.491 1.00 55.81 C ATOM 7928 N LEU G 309 34.766 20.450 9.275 1.00 54.19 N ATOM 7929 CA LEU G 309 33.558 20.422 8.459 1.00 52.78 C ATOM 7930 C LEU G 309 33.294 19.063 7.829 1.00 51.35 C ATOM 7931 O LEU G 309 34.214 18.275 7.625 1.00 52.19 O ATOM 7932 CB LEU G 309 33.662 21.458 7.342 1.00 52.85 C ATOM 7933 CG LEU G 309 33.916 22.913 7.738 1.00 52.82 C ATOM 7934 CD1 LEU G 309 33.961 23.762 6.474 1.00 53.14 C ATOM 7935 CD2 LEU G 309 32.824 23.401 8.687 1.00 53.39 C ATOM 7936 N LYS G 310 32.028 18.796 7.523 1.00 49.05 N ATOM 7937 CA LYS G 310 31.633 17.547 6.880 1.00 46.61 C ATOM 7938 C LYS G 310 30.630 17.867 5.771 1.00 44.89 C ATOM 7939 O LYS G 310 29.576 18.457 6.022 1.00 43.71 O ATOM 7940 CB LYS G 310 31.003 16.589 7.893 1.00 47.16 C ATOM 7941 N VAL G 311 30.964 17.481 4.543 1.00 43.13 N ATOM 7942 CA VAL G 311 30.095 17.745 3.401 1.00 41.87 C ATOM 7943 C VAL G 311 28.961 16.736 3.304 1.00 41.16 C ATOM 7944 O VAL G 311 29.183 15.551 3.055 1.00 41.76 O ATOM 7945 CB VAL G 311 30.884 17.735 2.068 1.00 41.62 C ATOM 7946 CG1 VAL G 311 29.927 18.000 0.894 1.00 41.69 C ATOM 7947 CG2 VAL G 311 31.985 18.793 2.105 1.00 40.64 C ATOM 7948 N LEU G 312 27.739 17.217 3.488 1.00 39.89 N ATOM 7949 CA LEU G 312 26.566 16.359 3.433 1.00 39.38 C ATOM 7950 C LEU G 312 26.091 16.102 2.012 1.00 38.89 C ATOM 7951 O LEU G 312 25.671 14.994 1.675 1.00 39.49 O ATOM 7952 CB LEU G 312 25.422 16.989 4.231 1.00 38.49 C ATOM 7953 CG LEU G 312 25.760 17.379 5.669 1.00 38.22 C ATOM 7954 CD1 LEU G 312 24.515 17.907 6.351 1.00 37.54 C ATOM 7955 CD2 LEU G 312 26.313 16.166 6.419 1.00 37.98 C ATOM 7956 N LYS G 313 26.164 17.131 1.181 1.00 37.96 N ATOM 7957 CA LYS G 313 25.701 17.027 −0.192 1.00 36.96 C ATOM 7958 C LYS G 313 26.312 18.159 −1.011 1.00 35.75 C ATOM 7959 O LYS G 313 26.484 19.270 −0.509 1.00 35.15 O ATOM 7960 CB LYS G 313 24.167 17.112 −0.202 1.00 37.92 C ATOM 7961 CG LYS G 313 23.531 17.036 −1.570 1.00 39.69 C ATOM 7962 CD LYS G 313 22.017 16.829 −1.483 1.00 40.66 C ATOM 7963 CE LYS G 313 21.293 17.981 −0.808 1.00 40.96 C ATOM 7964 NZ LYS G 313 19.819 17.832 −0.980 1.00 39.90 N ATOM 7965 N ALA G 314 26.651 17.871 −2.263 1.00 34.32 N ATOM 7966 CA ALA G 314 27.245 18.873 −3.139 1.00 33.49 C ATOM 7967 C ALA G 314 26.785 18.714 −4.585 1.00 33.13 C ATOM 7968 O ALA G 314 26.636 17.594 −5.092 1.00 32.02 O ATOM 7969 CB ALA G 314 28.773 18.817 −3.057 1.00 33.39 C ATOM 7970 N ALA G 315 26.565 19.852 −5.242 1.00 32.55 N ATOM 7971 CA ALA G 315 26.100 19.882 −6.624 1.00 32.03 C ATOM 7972 C ALA G 315 27.094 19.282 −7.617 1.00 31.77 C ATOM 7973 O ALA G 315 28.311 19.307 −7.409 1.00 30.61 O ATOM 7974 CB ALA G 315 25.767 21.310 −7.026 1.00 31.94 C ATOM 7975 N GLY G 316 26.555 18.754 −8.709 1.00 32.02 N ATOM 7976 CA GLY G 316 27.384 18.159 −9.739 1.00 33.55 C ATOM 7977 C GLY G 316 26.536 17.392 −10.734 1.00 35.51 C ATOM 7978 O GLY G 316 25.302 17.438 −10.687 1.00 34.55 O ATOM 7979 N VAL G 317 27.201 16.691 −11.645 1.00 37.19 N ATOM 7980 CA VAL G 317 26.511 15.903 −12.657 1.00 39.87 C ATOM 7981 C VAL G 317 25.586 14.844 −12.050 1.00 41.07 C ATOM 7982 O VAL G 317 24.526 14.543 −12.605 1.00 41.25 O ATOM 7983 CB VAL G 317 27.521 15.211 −13.594 1.00 40.14 C ATOM 7984 CG1 VAL G 317 26.841 14.078 −14.339 1.00 41.69 C ATOM 7985 CG2 VAL G 317 28.075 16.226 −14.589 1.00 40.07 C ATOM 7986 N ASN G 318 25.981 14.296 −10.905 1.00 41.95 N ATOM 7987 CA ASN G 318 25.189 13.268 −10.248 1.00 44.07 C ATOM 7988 C ASN G 318 24.232 13.814 −9.187 1.00 44.24 C ATOM 7989 O ASN G 318 23.456 13.063 −8.608 1.00 45.18 O ATOM 7990 CB ASN G 318 26.136 12.228 −9.646 1.00 46.50 C ATOM 7991 CG ASN G 318 27.129 11.694 −10.676 1.00 48.73 C ATOM 7992 OD1 ASN G 318 28.332 11.580 −10.408 1.00 49.64 O ATOM 7993 ND2 ASN G 318 26.626 11.372 −11.866 1.00 48.81 N ATOM 7994 N THR G 319 24.290 15.119 −8.939 1.00 43.75 N ATOM 7995 CA THR G 319 23.417 15.766 −7.959 1.00 42.90 C ATOM 7996 C THR G 319 23.090 17.152 −8.532 1.00 42.35 C ATOM 7997 O THR G 319 23.662 18.163 −8.116 1.00 41.85 O ATOM 7998 CB THR G 319 24.136 15.917 −6.601 1.00 44.24 C ATOM 7999 OG1 THR G 319 24.688 14.653 −6.211 1.00 45.37 O ATOM 8000 CG2 THR G 319 23.162 16.379 −5.521 1.00 44.23 C ATOM 8001 N THR G 320 22.167 17.177 −9.493 1.00 40.79 N ATOM 8002 CA THR G 320 21.777 18.396 −10.196 1.00 40.16 C ATOM 8003 C THR G 320 21.215 19.525 −9.339 1.00 39.45 C ATOM 8004 O THR G 320 20.789 19.319 −8.200 1.00 38.71 O ATOM 8005 CB THR G 320 20.781 18.091 −11.345 1.00 40.38 C ATOM 8006 OG1 THR G 320 19.532 17.644 −10.800 1.00 40.05 O ATOM 8007 CG2 THR G 320 21.348 17.013 −12.262 1.00 40.03 C ATOM 8008 N ASP G 321 21.229 20.733 −9.905 1.00 38.20 N ATOM 8009 CA ASP G 321 20.737 21.912 −9.205 1.00 37.69 C ATOM 8010 C ASP G 321 19.228 21.894 −8.944 1.00 37.99 C ATOM 8011 O ASP G 321 18.745 22.613 −8.076 1.00 37.70 O ATOM 8012 CB ASP G 321 21.119 23.181 −9.970 1.00 36.07 C ATOM 8013 CG ASP G 321 22.612 23.470 −9.941 1.00 35.06 C ATOM 8014 OD1 ASP G 321 23.293 22.992 −9.008 1.00 32.54 O ATOM 8015 OD2 ASP G 321 23.097 24.187 −10.842 1.00 33.95 O ATOM 8016 N LYS G 322 18.486 21.072 −9.684 1.00 37.99 N ATOM 8017 CA LYS G 322 17.039 20.989 −9.514 1.00 37.74 C ATOM 8018 C LYS G 322 16.623 20.737 −8.065 1.00 37.41 C ATOM 8019 O LYS G 322 15.651 21.326 −7.578 1.00 36.98 O ATOM 8020 CB LYS G 322 16.456 19.891 −10.413 1.00 38.14 C ATOM 8021 N GLU G 323 17.363 19.880 −7.367 1.00 36.92 N ATOM 8022 CA GLU G 323 17.026 19.562 −5.981 1.00 37.04 C ATOM 8023 C GLU G 323 18.139 19.831 −4.955 1.00 37.04 C ATOM 8024 O GLU G 323 18.041 19.395 −3.804 1.00 35.73 O ATOM 8025 CB GLU G 323 16.584 18.097 −5.879 1.00 37.49 C ATOM 8026 N ILE G 324 19.175 20.564 −5.359 1.00 36.64 N ATOM 8027 CA ILE G 324 20.283 20.850 −4.457 1.00 36.36 C ATOM 8028 C ILE G 324 19.974 21.894 −3.374 1.00 36.39 C ATOM 8029 O ILE G 324 20.609 21.890 −2.325 1.00 36.32 O ATOM 8030 CB ILE G 324 21.564 21.298 −5.236 1.00 35.97 C ATOM 8031 CG1 ILE G 324 22.778 21.242 −4.304 1.00 36.15 C ATOM 8032 CG2 ILE G 324 21.418 22.724 −5.775 1.00 35.04 C ATOM 8033 CD1 ILE G 324 23.201 19.838 −3.928 1.00 35.22 C ATOM 8034 N GLU G 325 18.995 22.763 −3.610 1.00 36.24 N ATOM 8035 CA GLU G 325 18.666 23.800 −2.636 1.00 37.40 C ATOM 8036 C GLU G 325 17.861 23.396 −1.400 1.00 37.97 C ATOM 8037 O GLU G 325 17.570 24.235 −0.549 1.00 37.80 O ATOM 8038 CB GLU G 325 17.984 24.965 −3.344 1.00 37.95 C ATOM 8039 CG GLU G 325 18.949 25.748 −4.228 1.00 39.17 C ATOM 8040 CD GLU G 325 18.247 26.738 −5.131 1.00 40.30 C ATOM 8041 OE1 GLU G 325 17.453 26.298 −5.998 1.00 40.14 O ATOM 8042 OE2 GLU G 325 18.488 27.953 −4.972 1.00 40.10 O ATOM 8043 N VAL G 326 17.496 22.125 −1.292 1.00 38.24 N ATOM 8044 CA VAL G 326 16.767 21.668 −0.116 1.00 39.31 C ATOM 8045 C VAL G 326 17.461 20.438 0.460 1.00 39.67 C ATOM 8046 O VAL G 326 17.779 19.506 −0.270 1.00 39.75 O ATOM 8047 CB VAL G 326 15.279 21.339 −0.443 1.00 39.91 C ATOM 8048 CG1 VAL G 326 15.188 20.261 −1.530 1.00 40.97 C ATOM 8049 CG2 VAL G 326 14.573 20.871 0.820 1.00 39.23 C ATOM 8050 N LEU G 327 17.725 20.457 1.763 1.00 40.13 N ATOM 8051 CA LEU G 327 18.387 19.341 2.435 1.00 40.28 C ATOM 8052 C LEU G 327 17.418 18.677 3.397 1.00 41.91 C ATOM 8053 O LEU G 327 16.891 19.327 4.306 1.00 41.63 O ATOM 8054 CB LEU G 327 19.612 19.821 3.219 1.00 39.29 C ATOM 8055 CG LEU G 327 20.320 18.778 4.096 1.00 38.07 C ATOM 8056 CD1 LEU G 327 21.037 17.746 3.225 1.00 36.50 C ATOM 8057 CD2 LEU G 327 21.315 19.476 5.007 1.00 37.17 C ATOM 8058 N TYR G 328 17.190 17.382 3.196 1.00 42.74 N ATOM 8059 CA TYR G 328 16.283 16.622 4.050 1.00 43.93 C ATOM 8060 C TYR G 328 17.039 15.708 5.022 1.00 45.77 C ATOM 8061 O TYR G 328 18.049 15.097 4.664 1.00 45.73 O ATOM 8062 CB TYR G 328 15.317 15.773 3.196 1.00 41.69 C ATOM 8063 CG TYR G 328 14.348 16.574 2.342 1.00 39.94 C ATOM 8064 CD1 TYR G 328 14.572 16.760 0.976 1.00 38.82 C ATOM 8065 CD2 TYR G 328 13.224 17.176 2.910 1.00 39.08 C ATOM 8066 CE1 TYR G 328 13.695 17.531 0.192 1.00 38.26 C ATOM 8067 CE2 TYR G 328 12.345 17.953 2.144 1.00 38.56 C ATOM 8068 CZ TYR G 328 12.585 18.127 0.789 1.00 38.92 C ATOM 8069 OH TYR G 328 11.731 18.924 0.053 1.00 39.12 O ATOM 8070 N ILE G 329 16.553 15.635 6.258 1.00 47.90 N ATOM 8071 CA ILE G 329 17.151 14.768 7.272 1.00 49.82 C ATOM 8072 C ILE G 329 16.029 14.083 8.047 1.00 51.30 C ATOM 8073 O ILE G 329 15.304 14.727 8.802 1.00 51.47 O ATOM 8074 CB ILE G 329 18.032 15.547 8.242 1.00 49.44 C ATOM 8075 CG1 ILE G 329 19.170 16.205 7.472 1.00 48.78 C ATOM 8076 CG2 ILE G 329 18.581 14.607 9.308 1.00 49.28 C ATOM 8077 CD1 ILE G 329 19.913 17.229 8.276 1.00 50.09 C ATOM 8078 N ARG G 330 15.891 12.773 7.848 1.00 53.05 N ATOM 8079 CA ARG G 330 14.836 12.000 8.503 1.00 54.65 C ATOM 8080 C ARG G 330 15.320 11.157 9.683 1.00 54.87 C ATOM 8081 O ARG G 330 16.498 10.798 9.773 1.00 54.39 O ATOM 8082 CB ARG G 330 14.141 11.072 7.495 1.00 56.47 C ATOM 8083 CG ARG G 330 13.435 11.757 6.328 1.00 58.62 C ATOM 8084 CD ARG G 330 11.920 11.737 6.477 1.00 59.82 C ATOM 8085 NE ARG G 330 11.244 11.856 5.182 1.00 61.36 N ATOM 8086 CZ ARG G 330 9.944 12.094 5.022 1.00 62.24 C ATOM 8087 NH1 ARG G 330 9.162 12.243 6.078 1.00 62.98 N ATOM 8088 NH2 ARG G 330 9.424 12.167 3.803 1.00 62.21 N ATOM 8089 N ASN G 331 14.386 10.840 10.580 1.00 55.35 N ATOM 8090 CA ASN G 331 14.669 10.035 11.765 1.00 55.98 C ATOM 8091 C ASN G 331 15.949 10.543 12.431 1.00 56.14 C ATOM 8092 O ASN G 331 16.923 9.804 12.597 1.00 56.20 O ATOM 8093 CB ASN G 331 14.798 8.552 11.365 1.00 56.59 C ATOM 8094 CG ASN G 331 14.834 7.620 12.569 1.00 57.23 C ATOM 8095 OD1 ASN G 331 14.715 8.049 13.717 1.00 57.90 O ATOM 8096 ND2 ASN G 331 15.000 6.330 12.305 1.00 56.52 N ATOM 8097 N VAL G 332 15.929 11.814 12.820 1.00 56.01 N ATOM 8098 CA VAL G 332 17.085 12.451 13.442 1.00 55.69 C ATOM 8099 C VAL G 332 17.479 11.870 14.793 1.00 55.65 C ATOM 8100 O VAL G 332 16.636 11.384 15.551 1.00 55.23 O ATOM 8101 CB VAL G 332 16.853 13.966 13.631 1.00 55.69 C ATOM 8102 CG1 VAL G 332 16.411 14.596 12.318 1.00 55.96 C ATOM 8103 CG2 VAL G 332 15.820 14.201 14.709 1.00 55.79 C ATOM 8104 N THR G 333 18.777 11.927 15.078 1.00 55.48 N ATOM 8105 CA THR G 333 19.331 11.454 16.341 1.00 55.59 C ATOM 8106 C THR G 333 19.872 12.695 17.044 1.00 55.87 C ATOM 8107 O THR G 333 19.893 13.777 16.453 1.00 55.99 O ATOM 8108 CB THR G 333 20.504 10.472 16.126 1.00 55.46 C ATOM 8109 OG1 THR G 333 21.557 11.134 15.414 1.00 54.62 O ATOM 8110 CG2 THR G 333 20.050 9.250 15.338 1.00 55.51 C ATOM 8111 N PHE G 334 20.302 12.550 18.297 1.00 55.79 N ATOM 8112 CA PHE G 334 20.855 13.689 19.030 1.00 55.65 C ATOM 8113 C PHE G 334 22.155 14.123 18.356 1.00 55.18 C ATOM 8114 O PHE G 334 22.590 15.270 18.486 1.00 54.88 O ATOM 8115 CB PHE G 334 21.172 13.325 20.489 1.00 56.25 C ATOM 8116 CG PHE G 334 19.962 13.177 21.371 1.00 57.08 C ATOM 8117 CD1 PHE G 334 19.411 11.920 21.614 1.00 57.54 C ATOM 8118 CD2 PHE G 334 19.393 14.288 21.986 1.00 56.80 C ATOM 8119 CE1 PHE G 334 18.313 11.771 22.463 1.00 57.99 C ATOM 8120 CE2 PHE G 334 18.295 14.151 22.833 1.00 57.37 C ATOM 8121 CZ PHE G 334 17.754 12.891 23.075 1.00 57.64 C ATOM 8122 N GLU G 335 22.778 13.190 17.643 1.00 54.14 N ATOM 8123 CA GLU G 335 24.035 13.467 16.958 1.00 53.66 C ATOM 8124 C GLU G 335 23.856 14.452 15.796 1.00 52.54 C ATOM 8125 O GLU G 335 24.793 15.164 15.432 1.00 52.06 O ATOM 8126 CB GLU G 335 24.658 12.161 16.444 1.00 53.19 C ATOM 8127 N ASP G 336 22.654 14.497 15.227 1.00 51.27 N ATOM 8128 CA ASP G 336 22.378 15.393 14.109 1.00 50.05 C ATOM 8129 C ASP G 336 22.310 16.866 14.511 1.00 49.15 C ATOM 8130 O ASP G 336 22.448 17.747 13.665 1.00 48.99 O ATOM 8131 CB ASP G 336 21.083 14.981 13.407 1.00 49.53 C ATOM 8132 CG ASP G 336 21.184 13.617 12.754 1.00 49.48 C ATOM 8133 OD1 ASP G 336 22.212 13.353 12.092 1.00 49.51 O ATOM 8134 OD2 ASP G 336 20.236 12.813 12.893 1.00 49.11 O ATOM 8135 N ALA G 337 22.097 17.129 15.797 1.00 47.92 N ATOM 8136 CA ALA G 337 22.034 18.501 16.291 1.00 47.56 C ATOM 8137 C ALA G 337 23.294 19.263 15.878 1.00 47.01 C ATOM 8138 O ALA G 337 24.372 18.678 15.764 1.00 47.18 O ATOM 8139 CB ALA G 337 21.906 18.502 17.809 1.00 46.58 C ATOM 8140 N GLY G 338 23.161 20.566 15.653 1.00 46.08 N ATOM 8141 CA GLY G 338 24.320 21.356 15.274 1.00 44.93 C ATOM 8142 C GLY G 338 24.059 22.424 14.225 1.00 44.14 C ATOM 8143 O GLY G 338 22.911 22.675 13.842 1.00 43.26 O ATOM 8144 N GLU G 339 25.137 23.050 13.758 1.00 43.05 N ATOM 8145 CA GLU G 339 25.042 24.108 12.758 1.00 42.49 C ATOM 8146 C GLU G 339 25.165 23.588 11.332 1.00 41.35 C ATOM 8147 O GLU G 339 26.131 22.910 10.997 1.00 41.27 O ATOM 8148 CB GLU G 339 26.123 25.173 12.991 1.00 42.71 C ATOM 8149 CG GLU G 339 25.894 26.437 12.179 1.00 44.12 C ATOM 8150 CD GLU G 339 26.770 27.608 12.610 1.00 45.91 C ATOM 8151 OE1 GLU G 339 26.323 28.766 12.455 1.00 46.01 O ATOM 8152 OE2 GLU G 339 27.901 27.379 13.090 1.00 46.77 O ATOM 8153 N TYR G 340 24.172 23.910 10.505 1.00 40.08 N ATOM 8154 CA TYR G 340 24.157 23.519 9.097 1.00 38.55 C ATOM 8155 C TYR G 340 24.345 24.757 8.220 1.00 37.99 C ATOM 8156 O TYR G 340 23.751 25.817 8.470 1.00 37.78 O ATOM 8157 CB TYR G 340 22.837 22.844 8.732 1.00 39.39 C ATOM 8158 CG TYR G 340 22.666 21.468 9.332 1.00 40.42 C ATOM 8159 CD1 TYR G 340 22.521 21.298 10.711 1.00 40.04 C ATOM 8160 CD2 TYR G 340 22.636 20.336 8.518 1.00 40.28 C ATOM 8161 CE1 TYR G 340 22.346 20.031 11.268 1.00 41.01 C ATOM 8162 CE2 TYR G 340 22.464 19.067 9.058 1.00 41.27 C ATOM 8163 CZ TYR G 340 22.319 18.918 10.437 1.00 41.70 C ATOM 8164 OH TYR G 340 22.156 17.657 10.974 1.00 41.92 O ATOM 8165 N THR G 341 25.161 24.626 7.184 1.00 36.18 N ATOM 8166 CA THR G 341 25.418 25.753 6.311 1.00 35.17 C ATOM 8167 C THR G 341 25.232 25.489 4.830 1.00 34.76 C ATOM 8168 O THR G 341 25.667 24.464 4.310 1.00 35.27 O ATOM 8169 CB THR G 341 26.859 26.294 6.505 1.00 34.51 C ATOM 8170 OG1 THR G 341 26.998 26.830 7.823 1.00 34.37 O ATOM 8171 CG2 THR G 341 27.175 27.385 5.475 1.00 33.51 C ATOM 8172 N CYS G 342 24.559 26.418 4.161 1.00 33.38 N ATOM 8173 CA CYS G 342 24.403 26.331 2.721 1.00 33.42 C ATOM 8174 C CYS G 342 25.495 27.251 2.187 1.00 32.22 C ATOM 8175 O CYS G 342 25.525 28.445 2.507 1.00 31.86 O ATOM 8176 CB CYS G 342 23.043 26.838 2.255 1.00 32.91 C ATOM 8177 SG CYS G 342 23.023 27.056 0.461 1.00 36.06 S ATOM 8178 N LEU G 343 26.403 26.698 1.395 1.00 31.33 N ATOM 8179 CA LEU G 343 27.503 27.487 0.851 1.00 29.84 C ATOM 8180 C LEU G 343 27.470 27.498 −0.673 1.00 29.17 C ATOM 8181 O LEU G 343 27.415 26.442 −1.317 1.00 28.70 O ATOM 8182 CB LEU G 343 28.838 26.933 1.359 1.00 29.41 C ATOM 8183 CG LEU G 343 30.090 27.722 0.963 1.00 30.02 C ATOM 8184 CD1 LEU G 343 31.213 27.426 1.928 1.00 30.53 C ATOM 8185 CD2 LEU G 343 30.487 27.367 −0.468 1.00 31.57 C ATOM 8186 N ALA G 344 27.493 28.706 −1.234 1.00 28.06 N ATOM 8187 CA ALA G 344 27.450 28.920 −2.677 1.00 28.04 C ATOM 8188 C ALA G 344 28.666 29.689 −3.166 1.00 28.21 C ATOM 8189 O ALA G 344 28.988 30.763 −2.648 1.00 28.24 O ATOM 8190 CB ALA G 344 26.177 29.695 −3.064 1.00 24.87 C ATOM 8191 N GLY G 345 29.331 29.153 −4.182 1.00 28.21 N ATOM 8192 CA GLY G 345 30.485 29.841 −4.721 1.00 28.10 C ATOM 8193 C GLY G 345 30.563 29.818 −6.232 1.00 27.62 C ATOM 8194 O GLY G 345 30.088 28.880 −6.866 1.00 27.30 O ATOM 8195 N ASN G 346 31.136 30.875 −6.801 1.00 28.40 N ATOM 8196 CA ASN G 346 31.365 30.979 −8.238 1.00 29.46 C ATOM 8197 C ASN G 346 32.806 31.503 −8.405 1.00 29.97 C ATOM 8198 O ASN G 346 33.516 31.688 −7.411 1.00 28.93 O ATOM 8199 CB ASN G 346 30.332 31.913 −8.910 1.00 29.29 C ATOM 8200 CG ASN G 346 30.356 33.346 −8.363 1.00 31.68 C ATOM 8201 OD1 ASN G 346 31.400 33.876 −7.995 1.00 32.04 O ATOM 8202 ND2 ASN G 346 29.189 33.987 −8.347 1.00 33.14 N ATOM 8203 N SER G 347 33.232 31.737 −9.645 1.00 31.49 N ATOM 8204 CA SER G 347 34.582 32.229 −9.933 1.00 32.37 C ATOM 8205 C SER G 347 34.951 33.528 −9.197 1.00 33.15 C ATOM 8206 O SER G 347 36.117 33.755 −8.877 1.00 33.62 O ATOM 8207 CB SER G 347 34.736 32.425 −11.449 1.00 32.93 C ATOM 8208 OG SER G 347 33.785 33.349 −11.969 1.00 33.21 O ATOM 8209 N ILE G 348 33.962 34.374 −8.918 1.00 33.11 N ATOM 8210 CA ILE G 348 34.218 35.639 −8.233 1.00 33.33 C ATOM 8211 C ILE G 348 34.392 35.516 −6.717 1.00 33.98 C ATOM 8212 O ILE G 348 35.285 36.146 −6.139 1.00 34.53 O ATOM 8213 CB ILE G 348 33.097 36.656 −8.537 1.00 33.03 C ATOM 8214 CG1 ILE G 348 33.069 36.952 −10.038 1.00 32.51 C ATOM 8215 CG2 ILE G 348 33.331 37.942 −7.771 1.00 32.83 C ATOM 8216 CD1 ILE G 348 31.686 37.154 −10.592 1.00 33.67 C ATOM 8217 N GLY G 349 33.549 34.711 −6.073 1.00 33.74 N ATOM 8218 CA GLY G 349 33.651 34.554 −4.634 1.00 33.15 C ATOM 8219 C GLY G 349 32.691 33.558 −4.005 1.00 33.68 C ATOM 8220 O GLY G 349 31.941 32.868 −4.698 1.00 33.59 O ATOM 8221 N ILE G 350 32.700 33.528 −2.672 1.00 34.04 N ATOM 8222 CA ILE G 350 31.895 32.614 −1.864 1.00 33.81 C ATOM 8223 C ILE G 350 30.926 33.311 −0.907 1.00 34.33 C ATOM 8224 O ILE G 350 31.259 34.340 −0.327 1.00 34.64 O ATOM 8225 CB ILE G 350 32.828 31.741 −0.999 1.00 34.32 C ATOM 8226 CG1 ILE G 350 33.708 30.871 −1.898 1.00 34.38 C ATOM 8227 CG2 ILE G 350 32.022 30.935 0.015 1.00 34.43 C ATOM 8228 CD1 ILE G 350 34.723 30.023 −1.133 1.00 34.20 C ATOM 8229 N SER G 351 29.740 32.728 −0.736 1.00 33.67 N ATOM 8230 CA SER G 351 28.720 33.241 0.179 1.00 32.95 C ATOM 8231 C SER G 351 28.097 32.051 0.917 1.00 32.49 C ATOM 8232 O SER G 351 28.025 30.957 0.363 1.00 31.80 O ATOM 8233 CB SER G 351 27.636 34.000 −0.595 1.00 33.61 C ATOM 8234 OG SER G 351 28.168 35.162 −1.207 1.00 33.50 O ATOM 8235 N PHE G 352 27.659 32.257 2.157 1.00 31.29 N ATOM 8236 CA PHE G 352 27.060 31.177 2.930 1.00 31.63 C ATOM 8237 C PHE G 352 26.168 31.651 4.080 1.00 32.23 C ATOM 8238 O PHE G 352 26.469 32.652 4.737 1.00 32.63 O ATOM 8239 CB PHE G 352 28.167 30.260 3.476 1.00 31.01 C ATOM 8240 CG PHE G 352 29.075 30.920 4.486 1.00 31.43 C ATOM 8241 CD1 PHE G 352 28.670 31.081 5.812 1.00 31.71 C ATOM 8242 CD2 PHE G 352 30.338 31.384 4.111 1.00 31.71 C ATOM 8243 CE1 PHE G 352 29.512 31.694 6.756 1.00 32.54 C ATOM 8244 CE2 PHE G 352 31.186 32.000 5.045 1.00 31.96 C ATOM 8245 CZ PHE G 352 30.776 32.154 6.364 1.00 31.67 C ATOM 8246 N HIS G 353 25.067 30.934 4.307 1.00 32.19 N ATOM 8247 CA HIS G 353 24.131 31.235 5.400 1.00 32.95 C ATOM 8248 C HIS G 353 24.019 29.976 6.266 1.00 33.83 C ATOM 8249 O HIS G 353 23.995 28.854 5.745 1.00 33.62 O ATOM 8250 CB HIS G 353 22.725 31.590 4.887 1.00 31.45 C ATOM 8251 CG HIS G 353 22.598 32.972 4.314 1.00 31.24 C ATOM 8252 ND1 HIS G 353 21.390 33.479 3.874 1.00 28.98 N ATOM 8253 CD2 HIS G 353 23.519 33.939 4.085 1.00 31.47 C ATOM 8254 CE1 HIS G 353 21.575 34.698 3.396 1.00 29.98 C ATOM 8255 NE2 HIS G 353 22.857 35.003 3.509 1.00 29.58 N ATOM 8256 N SER G 354 23.925 30.162 7.582 1.00 34.43 N ATOM 8257 CA SER G 354 23.841 29.040 8.505 1.00 35.16 C ATOM 8258 C SER G 354 22.591 29.026 9.371 1.00 36.14 C ATOM 8259 O SER G 354 21.977 30.058 9.621 1.00 36.56 O ATOM 8260 CB SER G 354 25.070 29.035 9.407 1.00 35.17 C ATOM 8261 OG SER G 354 26.245 29.081 8.632 1.00 35.00 O ATOM 8262 N ALA G 355 22.222 27.834 9.825 1.00 37.15 N ATOM 8263 CA ALA G 355 21.054 27.658 10.676 1.00 38.86 C ATOM 8264 C ALA G 355 21.394 26.584 11.695 1.00 39.80 C ATOM 8265 O ALA G 355 22.340 25.816 11.513 1.00 39.82 O ATOM 8266 CB ALA G 355 19.846 27.235 9.843 1.00 37.20 C ATOM 8267 N TRP G 356 20.626 26.525 12.770 1.00 41.54 N ATOM 8268 CA TRP G 356 20.881 25.531 13.800 1.00 43.64 C ATOM 8269 C TRP G 356 19.751 24.523 13.935 1.00 43.65 C ATOM 8270 O TRP G 356 18.573 24.860 13.788 1.00 43.22 O ATOM 8271 CB TRP G 356 21.114 26.225 15.141 1.00 46.44 C ATOM 8272 CG TRP G 356 22.511 26.086 15.662 1.00 49.88 C ATOM 8273 CD1 TRP G 356 23.063 24.983 16.258 1.00 51.44 C ATOM 8274 CD2 TRP G 356 23.535 27.086 15.640 1.00 51.37 C ATOM 8275 NE1 TRP G 356 24.371 25.238 16.612 1.00 52.49 N ATOM 8276 CE2 TRP G 356 24.686 26.520 16.244 1.00 52.66 C ATOM 8277 CE3 TRP G 356 23.595 28.405 15.171 1.00 52.35 C ATOM 8278 CZ2 TRP G 356 25.884 27.231 16.391 1.00 53.68 C ATOM 8279 CZ3 TRP G 356 24.785 29.117 15.318 1.00 53.49 C ATOM 8280 CH2 TRP G 356 25.914 28.526 15.924 1.00 54.51 C ATOM 8281 N LEU G 357 20.123 23.276 14.191 1.00 43.63 N ATOM 8282 CA LEU G 357 19.140 22.227 14.387 1.00 44.46 C ATOM 8283 C LEU G 357 19.162 21.828 15.854 1.00 45.26 C ATOM 8284 O LEU G 357 20.201 21.426 16.381 1.00 45.00 O ATOM 8285 CB LEU G 357 19.452 21.003 13.526 1.00 43.98 C ATOM 8286 CG LEU G 357 18.610 19.760 13.838 1.00 43.52 C ATOM 8287 CD1 LEU G 357 17.133 20.042 13.592 1.00 43.52 C ATOM 8288 CD2 LEU G 357 19.076 18.604 12.980 1.00 43.08 C ATOM 8289 N THR G 358 18.017 21.963 16.516 1.00 46.65 N ATOM 8290 CA THR G 358 17.895 21.582 17.923 1.00 47.93 C ATOM 8291 C THR G 358 17.109 20.284 18.028 1.00 48.09 C ATOM 8292 O THR G 358 16.003 20.177 17.499 1.00 48.24 O ATOM 8293 CB THR G 358 17.159 22.659 18.768 1.00 48.22 C ATOM 8294 OG1 THR G 358 17.958 23.846 18.850 1.00 48.40 O ATOM 8295 CG2 THR G 358 16.902 22.140 20.183 1.00 48.34 C ATOM 8296 N VAL G 359 17.691 19.297 18.703 1.00 48.99 N ATOM 8297 CA VAL G 359 17.040 17.997 18.889 1.00 50.41 C ATOM 8298 C VAL G 359 16.756 17.800 20.378 1.00 51.86 C ATOM 8299 O VAL G 359 17.685 17.740 21.187 1.00 51.15 O ATOM 8300 CB VAL G 359 17.931 16.836 18.384 1.00 49.92 C ATOM 8301 CG1 VAL G 359 17.222 15.503 18.595 1.00 49.38 C ATOM 8302 CG2 VAL G 359 18.246 17.029 16.915 1.00 49.42 C ATOM 8303 N LEU G 360 15.480 17.688 20.741 1.00 53.56 N ATOM 8304 CA LEU G 360 15.070 17.535 22.138 1.00 54.99 C ATOM 8305 C LEU G 360 14.742 16.092 22.563 1.00 56.44 C ATOM 8306 O LEU G 360 14.593 15.216 21.713 1.00 55.74 O ATOM 8307 CB LEU G 360 13.838 18.408 22.376 1.00 54.30 C ATOM 8308 CG LEU G 360 13.939 19.838 21.853 1.00 54.34 C ATOM 8309 CD1 LEU G 360 12.560 20.487 21.838 1.00 53.64 C ATOM 8310 CD2 LEU G 360 14.903 20.630 22.725 1.00 53.91 C ATOM 8311 N PRO G 361 14.638 15.837 23.893 1.00 58.35 N ATOM 8312 CA PRO G 361 14.320 14.519 24.477 1.00 60.10 C ATOM 8313 C PRO G 361 13.075 13.925 23.790 1.00 61.58 C ATOM 8314 O PRO G 361 12.479 14.587 22.946 1.00 62.32 O ATOM 8315 CB PRO G 361 14.132 14.826 25.973 1.00 59.69 C ATOM 8316 CG PRO G 361 14.047 16.375 26.043 1.00 59.70 C ATOM 8317 CD PRO G 361 14.970 16.805 24.956 1.00 58.52 C ATOM 8318 N ALA G 362 12.644 12.721 24.119 1.00 63.49 N ATOM 8319 CA ALA G 362 11.508 12.198 23.366 1.00 65.19 C ATOM 8320 C ALA G 362 10.312 11.461 23.982 1.00 66.25 C ATOM 8321 O ALA G 362 10.011 10.348 23.530 1.00 67.02 O ATOM 8322 CB ALA G 362 12.049 11.335 22.194 1.00 64.93 C ATOM 8323 N PRO G 363 9.635 12.014 25.008 1.00 66.83 N ATOM 8324 CA PRO G 363 8.510 11.171 25.448 1.00 67.25 C ATOM 8325 C PRO G 363 7.314 11.363 24.506 1.00 67.60 C ATOM 8326 O PRO G 363 7.514 11.250 23.265 1.00 67.94 O ATOM 8327 CB PRO G 363 8.195 11.695 26.849 1.00 67.25 C ATOM 8328 CG PRO G 363 9.583 12.157 27.339 1.00 67.51 C ATOM 8329 CD PRO G 363 10.079 12.901 26.099 1.00 67.27 C TER 8330 PRO G 363 ATOM 8331 N LYS H 151 68.361 −2.336 64.009 1.00 37.79 N ATOM 8332 CA LYS H 151 66.948 −2.442 63.538 1.00 38.61 C ATOM 8333 C LYS H 151 66.342 −1.053 63.268 1.00 38.86 C ATOM 8334 O LYS H 151 66.335 −0.190 64.150 1.00 39.10 O ATOM 8335 CB LYS H 151 66.104 −3.180 64.586 1.00 38.89 C ATOM 8336 N ARG H 152 65.854 −0.836 62.047 1.00 38.23 N ATOM 8337 CA ARG H 152 65.246 0.443 61.680 1.00 37.61 C ATOM 8338 C ARG H 152 64.375 0.372 60.432 1.00 36.65 C ATOM 8339 O ARG H 152 64.543 −0.509 59.582 1.00 36.15 O ATOM 8340 CB ARG H 152 66.321 1.519 61.477 1.00 38.33 C ATOM 8341 CG ARG H 152 67.309 1.232 60.365 1.00 39.54 C ATOM 8342 CD ARG H 152 68.455 2.260 60.323 1.00 40.17 C ATOM 8343 NE ARG H 152 68.034 3.574 59.837 1.00 38.82 N ATOM 8344 CZ ARG H 152 68.873 4.573 59.563 1.00 39.74 C ATOM 8345 NH1 ARG H 152 70.179 4.406 59.727 1.00 39.28 N ATOM 8346 NH2 ARG H 152 68.414 5.739 59.121 1.00 38.90 N ATOM 8347 N ALA H 153 63.447 1.321 60.342 1.00 35.00 N ATOM 8348 CA ALA H 153 62.519 1.433 59.225 1.00 33.97 C ATOM 8349 C ALA H 153 63.284 1.736 57.935 1.00 33.19 C ATOM 8350 O ALA H 153 64.443 2.139 57.976 1.00 33.04 O ATOM 8351 CB ALA H 153 61.518 2.548 59.514 1.00 33.10 C ATOM 8352 N PRO H 154 62.635 1.561 56.771 1.00 32.28 N ATOM 8353 CA PRO H 154 63.303 1.831 55.490 1.00 32.17 C ATOM 8354 C PRO H 154 63.644 3.308 55.319 1.00 32.24 C ATOM 8355 O PRO H 154 62.956 4.181 55.849 1.00 31.70 O ATOM 8356 CB PRO H 154 62.279 1.377 54.443 1.00 31.52 C ATOM 8357 CG PRO H 154 61.340 0.453 55.213 1.00 32.11 C ATOM 8358 CD PRO H 154 61.245 1.131 56.555 1.00 32.39 C ATOM 8359 N TYR H 155 64.708 3.578 54.574 1.00 32.18 N ATOM 8360 CA TYR H 155 65.129 4.944 54.310 1.00 32.80 C ATOM 8361 C TYR H 155 65.922 5.019 53.004 1.00 32.74 C ATOM 8362 O TYR H 155 66.623 4.073 52.644 1.00 33.34 O ATOM 8363 CB TYR H 155 65.975 5.483 55.470 1.00 32.80 C ATOM 8364 CG TYR H 155 67.319 4.811 55.635 1.00 34.02 C ATOM 8365 CD1 TYR H 155 67.411 3.508 56.115 1.00 34.87 C ATOM 8366 CD2 TYR H 155 68.499 5.477 55.307 1.00 34.83 C ATOM 8367 CE1 TYR H 155 68.642 2.879 56.264 1.00 36.26 C ATOM 8368 CE2 TYR H 155 69.744 4.854 55.453 1.00 35.52 C ATOM 8369 CZ TYR H 155 69.802 3.557 55.931 1.00 36.36 C ATOM 8370 OH TYR H 155 71.014 2.927 56.083 1.00 39.04 O ATOM 8371 N TRP H 156 65.806 6.137 52.293 1.00 32.88 N ATOM 8372 CA TRP H 156 66.529 6.309 51.031 1.00 34.25 C ATOM 8373 C TRP H 156 68.018 6.515 51.302 1.00 36.20 C ATOM 8374 O TRP H 156 68.391 7.360 52.112 1.00 36.60 O ATOM 8375 CB TRP H 156 65.995 7.516 50.248 1.00 31.44 C ATOM 8376 CG TRP H 156 64.525 7.485 50.003 1.00 29.10 C ATOM 8377 CD1 TRP H 156 63.649 8.505 50.207 1.00 27.47 C ATOM 8378 CD2 TRP H 156 63.751 6.374 49.528 1.00 27.11 C ATOM 8379 NE1 TRP H 156 62.372 8.101 49.894 1.00 27.08 N ATOM 8380 CE2 TRP H 156 62.405 6.800 49.475 1.00 26.90 C ATOM 8381 CE3 TRP H 156 64.064 5.064 49.145 1.00 27.16 C ATOM 8382 CZ2 TRP H 156 61.368 5.960 49.053 1.00 26.39 C ATOM 8383 CZ3 TRP H 156 63.027 4.220 48.726 1.00 27.16 C ATOM 8384 CH2 TRP H 156 61.695 4.676 48.685 1.00 27.77 C ATOM 8385 N THR H 157 68.863 5.749 50.617 1.00 38.27 N ATOM 8386 CA THR H 157 70.312 5.860 50.803 1.00 40.64 C ATOM 8387 C THR H 157 70.982 6.820 49.834 1.00 42.78 C ATOM 8388 O THR H 157 72.187 7.048 49.929 1.00 43.27 O ATOM 8389 CB THR H 157 71.056 4.490 50.659 1.00 39.80 C ATOM 8390 OG1 THR H 157 70.746 3.889 49.395 1.00 39.61 O ATOM 8391 CG2 THR H 157 70.685 3.545 51.786 1.00 39.19 C ATOM 8392 N ASN H 158 70.214 7.382 48.906 1.00 44.33 N ATOM 8393 CA ASN H 158 70.779 8.304 47.930 1.00 46.06 C ATOM 8394 C ASN H 158 69.702 9.157 47.268 1.00 46.05 C ATOM 8395 O ASN H 158 69.271 8.871 46.157 1.00 46.11 O ATOM 8396 CB ASN H 158 71.546 7.510 46.868 1.00 47.77 C ATOM 8397 CG ASN H 158 72.210 8.405 45.838 1.00 50.73 C ATOM 8398 OD1 ASN H 158 71.537 9.123 45.091 1.00 53.07 O ATOM 8399 ND2 ASN H 158 73.540 8.374 45.798 1.00 51.21 N ATOM 8400 N THR H 159 69.278 10.212 47.957 1.00 46.64 N ATOM 8401 CA THR H 159 68.243 11.102 47.448 1.00 46.95 C ATOM 8402 C THR H 159 68.667 11.891 46.221 1.00 46.70 C ATOM 8403 O THR H 159 67.816 12.360 45.471 1.00 47.12 O ATOM 8404 CB THR H 159 67.819 12.111 48.506 1.00 47.09 C ATOM 8405 OG1 THR H 159 68.968 12.859 48.928 1.00 48.35 O ATOM 8406 CG2 THR H 159 67.202 11.403 49.689 1.00 47.23 C ATOM 8407 N GLU H 160 69.972 12.053 46.024 1.00 46.63 N ATOM 8408 CA GLU H 160 70.471 12.805 44.877 1.00 46.12 C ATOM 8409 C GLU H 160 69.952 12.202 43.575 1.00 46.04 C ATOM 8410 O GLU H 160 69.453 12.915 42.713 1.00 45.59 O ATOM 8411 CB GLU H 160 72.000 12.830 44.869 1.00 46.26 C ATOM 8412 N LYS H 161 70.054 10.882 43.450 1.00 45.79 H ATOM 8413 CA LYS H 161 69.600 10.179 42.256 1.00 45.35 C ATOM 8414 C LYS H 161 68.072 10.089 42.139 1.00 45.08 C ATOM 8415 O LYS H 161 67.561 9.494 41.192 1.00 45.43 O ATOM 8416 CB LYS H 161 70.201 8.764 42.224 1.00 45.41 C ATOM 8417 N MET H 162 67.346 10.677 43.088 1.00 44.29 N ATOM 8418 CA MET H 162 65.880 10.636 43.067 1.00 43.74 C ATOM 8419 C MET H 162 65.245 12.014 42.864 1.00 43.76 C ATOM 8420 O MET H 162 64.025 12.122 42.728 1.00 43.56 O ATOM 8421 CB MET H 162 65.344 10.032 44.377 1.00 42.48 C ATOM 8422 CG MET H 162 65.754 8.586 44.645 1.00 40.88 C ATOM 8423 SD MET H 162 65.344 8.030 46.334 1.00 40.08 S ATOM 8424 CE MET H 162 63.553 7.764 46.172 1.00 39.02 C ATOM 8425 N GLU H 163 66.064 13.062 42.842 1.00 43.95 N ATOM 8426 CA GLU H 163 65.557 14.425 42.683 1.00 44.14 C ATOM 8427 C GLU H 163 64.862 14.695 41.348 1.00 42.70 C ATOM 8428 O GLU H 163 63.919 15.476 41.292 1.00 42.78 O ATOM 8429 CB GLU H 163 66.691 15.430 42.882 1.00 46.35 C ATOM 8430 CG GLU H 163 67.440 15.228 44.188 1.00 50.14 C ATOM 8431 CD GLU H 163 68.535 16.253 44.405 1.00 51.96 C ATOM 8432 OE1 GLU H 163 69.034 16.808 43.402 1.00 53.14 O ATOM 8433 OE2 GLU H 163 68.906 16.490 45.578 1.00 53.48 O ATOM 8434 N LYS H 164 65.333 14.062 40.278 1.00 41.20 N ATOM 8435 CA LYS H 164 64.739 14.233 38.947 1.00 39.43 C ATOM 8436 C LYS H 164 63.413 13.454 38.920 1.00 38.51 C ATOM 8437 O LYS H 164 63.398 12.239 38.710 1.00 38.56 O ATOM 8438 CB LYS H 164 65.701 13.694 37.872 1.00 38.67 C ATOM 8439 CG LYS H 164 65.256 13.935 36.426 1.00 38.08 C ATOM 8440 CD LYS H 164 66.199 13.274 35.408 1.00 37.42 C ATOM 8441 CE LYS H 164 65.701 13.467 33.983 1.00 36.65 C ATOM 8442 NZ LYS H 164 66.459 12.694 32.942 1.00 35.87 N ATOM 8443 N ARG H 165 62.305 14.158 39.126 1.00 37.03 N ATOM 8444 CA ARG H 165 60.990 13.521 39.167 1.00 36.21 C ATOM 8445 C ARG H 165 60.399 13.209 37.799 1.00 35.48 C ATOM 8446 O ARG H 165 59.831 12.132 37.582 1.00 35.58 O ATOM 8447 CB ARG H 165 60.021 14.405 39.958 1.00 35.31 C ATOM 8448 N LEU H 166 60.513 14.164 36.882 1.00 34.91 N ATOM 8449 CA LEU H 166 59.999 13.991 35.536 1.00 34.26 C ATOM 8450 C LEU H 166 61.087 13.485 34.600 1.00 33.85 C ATOM 8451 O LEU H 166 62.127 14.124 34.432 1.00 34.10 O ATOM 8452 CB LEU H 166 59.427 15.308 35.011 1.00 34.41 C ATOM 8453 CG LEU H 166 59.113 15.352 33.509 1.00 36.55 C ATOM 8454 CD1 LEU H 166 58.077 14.286 33.105 1.00 34.87 C ATOM 8455 CD2 LEU H 166 58.612 16.746 33.184 1.00 37.30 C ATOM 8456 N HIS H 167 60.839 12.319 34.011 1.00 33.98 N ATOM 8457 CA HIS H 167 61.754 11.697 33.064 1.00 34.35 C ATOM 8458 C HIS H 167 61.144 11.760 31.669 1.00 34.53 C ATOM 8459 O HIS H 167 60.244 10.975 31.341 1.00 34.24 O ATOM 8460 CB HIS H 167 62.002 10.226 33.414 1.00 34.98 C ATOM 8461 CG HIS H 167 63.101 10.016 34.403 1.00 36.61 C ATOM 8462 ND1 HIS H 167 63.021 10.452 35.707 1.00 37.72 N ATOM 8463 CD2 HIS H 167 64.328 9.462 34.264 1.00 37.02 C ATOM 8464 CE1 HIS H 167 64.156 10.180 36.330 1.00 37.52 C ATOM 8465 NE2 HIS H 167 64.965 9.580 35.475 1.00 37.37 N ATOM 8466 N ALA H 168 61.611 12.699 30.854 1.00 33.25 N ATOM 8467 CA ALA H 168 61.112 12.811 29.492 1.00 32.55 C ATOM 8468 C ALA H 168 62.219 12.260 28.618 1.00 32.58 C ATOM 8469 O ALA H 168 63.343 12.762 28.648 1.00 32.79 O ATOM 8470 CB ALA H 168 60.824 14.255 29.149 1.00 32.66 C ATOM 8471 N VAL H 169 61.908 11.221 27.851 1.00 32.15 N ATOM 8472 CA VAL H 169 62.904 10.593 27.001 1.00 33.27 C ATOM 8473 C VAL H 169 62.395 10.294 25.599 1.00 33.21 C ATOM 8474 O VAL H 169 61.200 10.126 25.376 1.00 33.45 O ATOM 8475 CB VAL H 169 63.403 9.258 27.627 1.00 34.54 C ATOM 8476 CG1 VAL H 169 63.759 9.472 29.110 1.00 34.94 C ATOM 8477 CG2 VAL H 169 62.324 8.176 27.497 1.00 34.37 C ATOM 8478 N PRO H 170 63.312 10.221 24.631 1.00 32.96 N ATOM 8479 CA PRO H 170 62.909 9.930 23.258 1.00 32.75 C ATOM 8480 C PRO H 170 62.512 8.468 23.093 1.00 33.59 C ATOM 8481 O PRO H 170 63.074 7.579 23.746 1.00 33.16 O ATOM 8482 CB PRO H 170 64.139 10.317 22.447 1.00 32.54 C ATOM 8483 CG PRO H 170 65.258 10.129 23.389 1.00 33.31 C ATOM 8484 CD PRO H 170 64.724 10.627 24.698 1.00 33.12 C ATOM 8485 N ALA H 171 61.523 8.234 22.233 1.00 33.29 N ATOM 8486 CA ALA H 171 61.026 6.892 21.964 1.00 33.83 C ATOM 8487 C ALA H 171 62.169 5.976 21.563 1.00 33.64 C ATOM 8488 O ALA H 171 63.141 6.435 20.963 1.00 33.64 O ATOM 8489 CB ALA H 171 59.971 6.934 20.840 1.00 33.62 C ATOM 8490 N ALA H 172 62.049 4.694 21.920 1.00 33.14 N ATOM 8491 CA ALA H 172 63.037 3.661 21.596 1.00 33.03 C ATOM 8492 C ALA H 172 64.201 3.536 22.575 1.00 33.25 C ATOM 8493 O ALA H 172 65.023 2.628 22.458 1.00 34.34 O ATOM 8494 CB ALA H 172 63.571 3.862 20.169 1.00 31.77 C ATOM 8495 N ASN H 173 64.276 4.443 23.534 1.00 33.52 N ATOM 8496 CA ASN H 173 65.337 4.412 24.534 1.00 33.97 C ATOM 8497 C ASN H 173 64.952 3.510 25.709 1.00 33.74 C ATOM 8498 O ASN H 173 63.795 3.098 25.848 1.00 34.12 O ATOM 8499 CB ASN H 173 65.590 5.827 25.092 1.00 35.64 C ATOM 8500 CG ASN H 173 66.456 6.694 24.176 1.00 35.73 C ATOM 8501 OD1 ASN H 173 66.444 6.554 22.960 1.00 37.95 O ATOM 8502 ND2 ASN H 173 67.190 7.612 24.772 1.00 36.54 N ATOM 8503 N THR H 174 65.938 3.206 26.546 1.00 32.58 N ATOM 8504 CA THR H 174 65.715 2.413 27.752 1.00 31.55 C ATOM 8505 C THR H 174 65.553 3.405 28.910 1.00 30.88 C ATOM 8506 O THR H 174 66.265 4.407 28.976 1.00 30.12 O ATOM 8507 CB THR H 174 66.927 1.524 28.093 1.00 31.44 C ATOM 8508 OG1 THR H 174 67.034 0.468 27.137 1.00 32.92 O ATOM 8509 CG2 THR H 174 66.785 0.935 29.500 1.00 31.57 C ATOM 8510 N VAL H 175 64.620 3.130 29.814 1.00 29.88 N ATOM 8511 CA VAL H 175 64.406 3.994 30.969 1.00 29.48 C ATOM 8512 C VAL H 175 64.687 3.217 32.256 1.00 28.35 C ATOM 8513 O VAL H 175 64.333 2.042 32.373 1.00 28.18 O ATOM 8514 CB VAL H 175 62.956 4.515 31.013 1.00 29.63 C ATOM 8515 CG1 VAL H 175 62.767 5.425 32.227 1.00 29.99 C ATOM 8516 CG2 VAL H 175 62.642 5.272 29.743 1.00 30.62 C ATOM 8517 N LYS H 176 65.333 3.862 33.219 1.00 28.20 N ATOM 8518 CA LYS H 176 65.646 3.214 34.488 1.00 28.67 C ATOM 8519 C LYS H 176 65.293 4.100 35.689 1.00 29.19 C ATOM 8520 O LYS H 176 65.775 5.230 35.804 1.00 28.15 O ATOM 8521 CB LYS H 176 67.133 2.848 34.547 1.00 28.72 C ATOM 8522 N PHE H 177 64.434 3.588 36.568 1.00 28.89 N ATOM 8523 CA PHE H 177 64.042 4.322 37.765 1.00 29.43 C ATOM 8524 C PHE H 177 64.709 3.653 38.956 1.00 30.25 C ATOM 8525 O PHE H 177 64.759 2.424 39.037 1.00 29.85 O ATOM 8526 CB PHE H 177 62.515 4.304 37.952 1.00 28.61 C ATOM 8527 CG PHE H 177 61.759 5.072 36.894 1.00 27.90 C ATOM 8528 CD1 PHE H 177 62.108 6.378 36.584 1.00 27.39 C ATOM 8529 CD2 PHE H 177 60.697 4.488 36.215 1.00 27.63 C ATOM 8530 CE1 PHE H 177 61.416 7.090 35.615 1.00 27.68 C ATOM 8531 CE2 PHE H 177 59.996 5.189 35.246 1.00 26.69 C ATOM 8532 CZ PHE H 177 60.353 6.491 34.944 1.00 27.27 C ATOM 8533 N ARG H 178 65.224 4.457 39.878 1.00 31.24 N ATOM 8534 CA ARG H 178 65.885 3.907 41.052 1.00 31.69 C ATOM 8535 C ARG H 178 65.415 4.535 42.356 1.00 30.80 C ATOM 8536 O ARG H 178 65.060 5.709 42.396 1.00 29.30 O ATOM 8537 CB ARG H 178 67.404 4.075 40.930 1.00 33.79 C ATOM 8538 CG ARG H 178 68.001 3.388 39.718 1.00 38.62 C ATOM 8539 CD ARG H 178 69.510 3.228 39.866 1.00 41.50 C ATOM 8540 NE ARG H 178 69.851 2.593 41.137 1.00 45.13 N ATOM 8541 CZ ARG H 178 71.029 2.039 41.415 1.00 47.50 C ATOM 8542 NH1 ARG H 178 71.997 2.030 40.503 1.00 48.51 N ATOM 8543 NH2 ARG H 178 71.240 1.490 42.607 1.00 48.12 N ATOM 8544 N CYS H 179 65.420 3.727 43.420 1.00 30.39 N ATOM 8545 CA CYS H 179 65.042 4.166 44.756 1.00 31.12 C ATOM 8546 C CYS H 179 65.958 3.453 45.753 1.00 31.65 C ATOM 8547 O CYS H 179 65.517 2.600 46.535 1.00 29.30 O ATOM 8548 CB CYS H 179 63.582 3.810 45.039 1.00 32.01 C ATOM 8549 SG CYS H 179 62.446 4.620 43.899 1.00 33.46 S ATOM 8550 N PRO H 180 67.260 3.794 45.730 1.00 31.88 N ATOM 8551 CA PRO H 180 68.246 3.178 46.628 1.00 32.79 C ATOM 8552 C PRO H 180 67.774 3.257 48.072 1.00 32.81 C ATOM 8553 O PRO H 180 67.543 4.345 48.594 1.00 32.89 O ATOM 8554 CB PRO H 180 69.501 4.008 46.378 1.00 32.58 C ATOM 8555 CG PRO H 180 69.347 4.405 44.941 1.00 32.95 C ATOM 8556 CD PRO H 180 67.894 4.811 44.879 1.00 32.19 C ATOM 8557 N ALA H 181 67.621 2.106 48.717 1.00 33.06 N ATOM 8558 CA ALA H 181 67.143 2.102 50.094 1.00 35.06 C ATOM 8559 C ALA H 181 67.959 1.268 51.070 1.00 36.08 C ATOM 8560 O ALA H 181 68.712 0.371 50.681 1.00 35.98 O ATOM 8561 CB ALA H 181 65.681 1.646 50.138 1.00 34.31 C ATOM 8562 N GLY H 182 67.779 1.584 52.350 1.00 36.73 N ATOM 8563 CA GLY H 182 68.449 0.874 53.423 1.00 37.41 C ATOM 8564 C GLY H 182 67.396 0.466 54.438 1.00 38.30 C ATOM 8565 O GLY H 182 66.236 0.872 54.319 1.00 37.63 O ATOM 8566 N GLY H 183 67.786 −0.331 55.430 1.00 38.77 N ATOM 8567 CA GLY H 183 66.843 −0.768 56.447 1.00 39.20 C ATOM 8568 C GLY H 183 67.203 −2.112 57.061 1.00 40.18 C ATOM 8569 O GLY H 183 67.873 −2.932 56.436 1.00 40.21 O ATOM 8570 N ASN H 184 66.740 −2.347 58.284 1.00 40.96 N ATOM 8571 CA ASN H 184 67.026 −3.584 58.993 1.00 41.48 C ATOM 8572 C ASN H 184 65.809 −4.038 59.785 1.00 41.66 C ATOM 8573 O ASN H 184 65.433 −3.406 60.764 1.00 41.94 O ATOM 8574 CB ASN H 184 68.209 −3.365 59.942 1.00 41.99 C ATOM 8575 CG ASN H 184 68.613 −4.627 60.689 1.00 43.13 C ATOM 8576 OD1 ASN H 184 69.569 −4.612 61.464 1.00 43.80 O ATOM 8577 ND2 ASN H 184 67.889 −5.720 60.463 1.00 43.04 N ATOM 8578 N PRO H 185 65.207 −5.171 59.400 1.00 42.08 N ATOM 8579 CA PRO H 185 65.603 −6.036 58.287 1.00 42.78 C ATOM 8580 C PRO H 185 65.487 −5.416 56.893 1.00 43.55 C ATOM 8581 O PRO H 185 64.825 −4.387 56.701 1.00 43.80 O ATOM 8582 CB PRO H 185 64.694 −7.253 58.469 1.00 42.73 C ATOM 8583 CG PRO H 185 63.469 −6.662 59.064 1.00 42.91 C ATOM 8584 CD PRO H 185 64.032 −5.724 60.094 1.00 41.94 C ATOM 8585 N MET H 186 66.148 −6.050 55.927 1.00 43.56 N ATOM 8586 CA MET H 186 66.137 −5.585 54.547 1.00 43.87 C ATOM 8587 C MET H 186 64.720 −5.393 54.045 1.00 42.88 C ATOM 8588 O MET H 186 63.924 −6.333 54.010 1.00 42.19 O ATOM 8589 CB MET H 186 66.854 −6.582 53.638 1.00 45.83 C ATOM 8590 CG MET H 186 68.277 −6.195 53.298 1.00 48.98 C ATOM 8591 SD MET H 186 68.350 −4.713 52.263 1.00 51.20 S ATOM 8592 CE MET H 186 68.901 −3.490 53.482 1.00 51.08 C ATOM 8593 N PRO H 187 64.380 −4.163 53.653 1.00 41.92 N ATOM 8594 CA PRO H 187 63.027 −3.912 53.156 1.00 41.63 C ATOM 8595 C PRO H 187 62.761 −4.492 51.763 1.00 41.02 C ATOM 8596 O PRO H 187 63.684 −4.696 50.971 1.00 40.91 O ATOM 8597 CB PRO H 187 62.917 −2.388 53.201 1.00 41.73 C ATOM 8598 CG PRO H 187 64.321 −1.939 52.994 1.00 42.27 C ATOM 8599 CD PRO H 187 65.117 −2.902 53.846 1.00 41.98 C ATOM 8600 N THR H 188 61.492 −4.773 51.487 1.00 40.31 N ATOM 8601 CA THR H 188 61.086 −5.305 50.197 1.00 40.35 C ATOM 8602 C THR H 188 60.740 −4.127 49.291 1.00 40.63 C ATOM 8603 O THR H 188 60.550 −3.010 49.761 1.00 41.57 O ATOM 8604 CB THR H 188 59.875 −6.242 50.340 1.00 39.84 C ATOM 8605 OG1 THR H 188 58.766 −5.523 50.894 1.00 40.00 O ATOM 8606 CG2 THR H 188 60.223 −7.405 51.254 1.00 38.95 C ATOM 8607 N MET H 189 60.646 −4.390 47.997 1.00 40.93 N ATOM 8608 CA MET H 189 60.376 −3.356 47.013 1.00 41.37 C ATOM 8609 C MET H 189 59.282 −3.777 46.036 1.00 40.54 C ATOM 8610 O MET H 189 59.279 −4.906 45.551 1.00 40.87 O ATOM 8611 CB MET H 189 61.684 −3.076 46.258 1.00 43.68 C ATOM 8612 CG MET H 189 61.549 −2.518 44.858 1.00 47.65 C ATOM 8613 SD MET H 189 61.934 −0.765 44.822 1.00 53.13 S ATOM 8614 CE MET H 189 60.298 −0.119 45.325 1.00 51.14 C ATOM 8615 N ARG H 190 58.357 −2.863 45.758 1.00 39.03 N ATOM 8616 CA ARG H 190 57.272 −3.111 44.815 1.00 38.27 C ATOM 8617 C ARG H 190 57.087 −1.863 43.955 1.00 36.15 C ATOM 8618 O ARG H 190 57.212 −0.750 44.462 1.00 35.06 O ATOM 8619 CB ARG H 190 55.962 −3.388 45.551 1.00 40.41 C ATOM 8620 CG ARG H 190 56.086 −4.286 46.753 1.00 44.73 C ATOM 8621 CD ARG H 190 54.723 −4.863 47.109 1.00 47.23 C ATOM 8622 NE ARG H 190 53.677 −3.841 47.119 1.00 50.38 N ATOM 8623 CZ ARG H 190 53.563 −2.882 48.035 1.00 51.38 C ATOM 8624 NH1 ARG H 190 54.432 −2.803 49.036 1.00 52.06 N ATOM 8625 NH2 ARG H 190 52.576 −1.999 47.949 1.00 52.44 N ATOM 8626 N TRP H 191 56.790 −2.046 42.669 1.00 34.17 N ATOM 8627 CA TRP H 191 56.575 −0.912 41.770 1.00 33.18 C ATOM 8628 C TRP H 191 55.133 −0.826 41.275 1.00 32.69 C ATOM 8629 O TRP H 191 54.528 −1.831 40.913 1.00 33.43 O ATOM 8630 CB TRP H 191 57.512 −0.987 40.569 1.00 33.46 C ATOM 8631 CG TRP H 191 58.941 −0.736 40.908 1.00 33.49 C ATOM 8632 CD1 TRP H 191 59.846 −1.645 41.370 1.00 33.78 C ATOM 8633 CD2 TRP H 191 59.628 0.519 40.836 1.00 32.79 C ATOM 8634 NE1 TRP H 191 61.059 −1.034 41.589 1.00 34.46 N ATOM 8635 CE2 TRP H 191 60.955 0.293 41.271 1.00 32.88 C ATOM 8636 CE3 TRP H 191 59.252 1.811 40.450 1.00 31.84 C ATOM 8637 CZ2 TRP H 191 61.909 1.313 41.331 1.00 32.39 C ATOM 8638 CZ3 TRP H 191 60.199 2.829 40.512 1.00 31.53 C ATOM 8639 CH2 TRP H 191 61.516 2.571 40.949 1.00 32.25 C ATOM 8640 N LEU H 192 54.591 0.382 41.256 1.00 31.74 N ATOM 8641 CA LEU H 192 53.225 0.590 40.808 1.00 31.83 C ATOM 8642 C LEU H 192 53.202 1.484 39.575 1.00 31.69 C ATOM 8643 O LEU H 192 54.067 2.356 39.411 1.00 31.36 O ATOM 8644 CB LEU H 192 52.405 1.258 41.922 1.00 32.15 C ATOM 8645 CG LEU H 192 52.519 0.633 43.320 1.00 33.26 C ATOM 8646 CD1 LEU H 192 51.813 1.518 44.342 1.00 33.37 C ATOM 8647 CD2 LEU H 192 51.928 −0.774 43.308 1.00 32.33 C ATOM 8648 N LYS H 193 52.228 1.247 38.700 1.00 31.27 N ATOM 8649 CA LYS H 193 52.056 2.078 37.521 1.00 31.38 C ATOM 8650 C LYS H 193 50.704 2.745 37.724 1.00 32.24 C ATOM 8651 O LYS H 193 49.682 2.061 37.839 1.00 32.34 O ATOM 8652 CB LYS H 193 52.032 1.263 36.230 1.00 30.70 C ATOM 8653 CG LYS H 193 51.719 2.146 35.016 1.00 31.36 C ATOM 8654 CD LYS H 193 51.678 1.383 33.707 1.00 32.10 C ATOM 8655 CE LYS H 193 51.375 2.330 32.542 1.00 32.57 C ATOM 8656 NZ LYS H 193 51.390 1.655 31.212 1.00 31.31 N ATOM 8657 N ASN H 194 50.700 4.073 37.775 1.00 32.87 N ATOM 8658 CA ASN H 194 49.466 4.821 37.980 1.00 34.49 C ATOM 8659 C ASN H 194 48.725 4.323 39.225 1.00 35.42 C ATOM 8660 O ASN H 194 47.523 4.050 39.177 1.00 34.66 O ATOM 8661 CB ASN H 194 48.558 4.699 36.757 1.00 35.20 C ATOM 8662 CG ASN H 194 49.175 5.295 35.520 1.00 37.23 C ATOM 8663 OD1 ASN H 194 49.780 6.377 35.566 1.00 37.24 O ATOM 8664 ND2 ASN H 194 49.021 4.604 34.396 1.00 38.07 N ATOM 8665 N GLY H 195 49.465 4.185 40.324 1.00 35.49 N ATOM 8666 CA GLY H 195 48.894 3.755 41.588 1.00 35.87 C ATOM 8667 C GLY H 195 48.380 2.331 41.728 1.00 36.60 C ATOM 8668 O GLY H 195 47.733 2.012 42.726 1.00 37.28 O ATOM 8669 N LYS H 196 48.659 1.470 40.756 1.00 36.84 N ATOM 8670 CA LYS H 196 48.200 0.083 40.813 1.00 36.47 C ATOM 8671 C LYS H 196 49.342 −0.859 40.468 1.00 36.66 C ATOM 8672 O LYS H 196 50.306 −0.458 39.813 1.00 36.79 O ATOM 8673 CB LYS H 196 47.047 −0.144 39.826 1.00 36.59 C ATOM 8674 N GLU H 197 49.224 −2.110 40.898 1.00 36.27 N ATOM 8675 CA GLU H 197 50.250 −3.111 40.628 1.00 36.93 C ATOM 8676 C GLU H 197 50.646 −3.071 39.159 1.00 37.24 C ATOM 8677 O GLU H 197 49.788 −3.011 38.277 1.00 37.37 O ATOM 8678 CB GLU H 197 49.743 −4.513 40.978 1.00 36.22 C ATOM 8679 N PHE H 198 51.955 −3.088 38.912 1.00 37.40 N ATOM 8680 CA PHE H 198 52.519 −3.059 37.564 1.00 37.00 C ATOM 8681 C PHE H 198 52.834 −4.508 37.209 1.00 38.01 C ATOM 8682 O PHE H 198 53.680 −5.140 37.850 1.00 38.55 O ATOM 8683 CB PHE H 198 53.810 −2.225 37.557 1.00 36.91 C ATOM 8684 CG PHE H 198 54.419 −2.007 36.182 1.00 36.86 C ATOM 8685 CD1 PHE H 198 55.758 −1.631 36.062 1.00 36.29 C ATOM 8686 CD2 PHE H 198 53.660 −2.138 35.020 1.00 36.71 C ATOM 8687 CE1 PHE H 198 56.335 −1.386 34.809 1.00 36.73 C ATOM 8688 CE2 PHE H 198 54.224 −1.895 33.759 1.00 37.32 C ATOM 8689 CZ PHE H 198 55.565 −1.518 33.653 1.00 37.03 C ATOM 8690 N LYS H 199 52.152 −5.037 36.197 1.00 38.20 N ATOM 8691 CA LYS H 199 52.361 −6.417 35.775 1.00 38.43 C ATOM 8692 C LYS H 199 53.114 −6.528 34.449 1.00 38.45 C ATOM 8693 O LYS H 199 53.064 −5.622 33.615 1.00 37.89 O ATOM 8694 CB LYS H 199 51.011 −7.130 35.653 1.00 39.27 C ATOM 8695 N GLN H 200 53.808 −7.646 34.256 1.00 38.02 N ATOM 8696 CA GLN H 200 54.568 −7.875 33.032 1.00 38.31 C ATOM 8697 C GLN H 200 53.728 −7.698 31.768 1.00 39.07 C ATOM 8698 O GLN H 200 54.214 −7.170 30.765 1.00 39.42 O ATOM 8699 CB GLN H 200 55.172 −9.286 33.015 1.00 37.92 C ATOM 8700 CG GLN H 200 56.330 −9.514 33.978 1.00 37.78 C ATOM 8701 CD GLN H 200 57.578 −8.707 33.622 1.00 37.85 C ATOM 8702 OE1 GLN H 200 57.985 −8.634 32.455 1.00 37.06 O ATOM 8703 NE2 GLN H 200 58.197 −8.111 34.632 1.00 37.78 N ATOM 8704 N GLU H 201 52.473 −8.136 31.803 1.00 39.36 N ATOM 8705 CA GLU H 201 51.623 −8.020 30.621 1.00 39.62 C ATOM 8706 C GLU H 201 51.113 −6.596 30.366 1.00 39.23 C ATOM 8707 O GLU H 201 50.416 −6.350 29.381 1.00 38.74 O ATOM 8708 CB GLU H 201 50.431 −8.986 30.713 1.00 41.36 C ATOM 8709 CG GLU H 201 49.343 −8.550 31.678 1.00 44.13 C ATOM 8710 CD GLU H 201 49.234 −9.456 32.888 1.00 46.42 C ATOM 8711 OE1 GLU H 201 50.276 −9.701 33.541 1.00 47.29 O ATOM 8712 OE2 GLU H 201 48.105 −9.916 33.189 1.00 47.42 O ATOM 8713 N HIS H 202 51.465 −5.656 31.236 1.00 39.09 N ATOM 8714 CA HIS H 202 51.015 −4.281 31.060 1.00 38.39 C ATOM 8715 C HIS H 202 51.687 −3.527 29.901 1.00 37.42 C ATOM 8716 O HIS H 202 51.258 −2.427 29.541 1.00 36.70 O ATOM 8717 CB HIS H 202 51.164 −3.515 32.376 1.00 40.07 C ATOM 8718 CG HIS H 202 50.119 −3.863 33.391 1.00 42.25 C ATOM 8719 ND1 HIS H 202 48.978 −4.575 33.072 1.00 41.73 N ATOM 8720 CD2 HIS H 202 50.017 −3.563 34.709 1.00 42.67 C ATOM 8721 CE1 HIS H 202 48.222 −4.695 34.148 1.00 42.51 C ATOM 8722 NE2 HIS H 202 48.827 −4.090 35.155 1.00 43.17 N ATOM 8723 N ARG H 203 52.731 −4.120 29.315 1.00 36.47 N ATOM 8724 CA ARG H 203 53.429 −3.508 28.169 1.00 35.54 C ATOM 8725 C ARG H 203 54.157 −4.563 27.339 1.00 35.60 C ATOM 8726 O ARG H 203 54.540 −5.614 27.850 1.00 35.55 O ATOM 8727 CB ARG H 203 54.445 −2.438 28.617 1.00 34.59 C ATOM 8728 CG ARG H 203 55.832 −2.971 29.006 1.00 33.37 C ATOM 8729 CD ARG H 203 56.737 −1.854 29.562 1.00 32.84 C ATOM 8730 NE ARG H 203 57.270 −0.955 28.533 1.00 30.57 N ATOM 8731 CZ ARG H 203 58.413 −1.159 27.882 1.00 29.72 C ATOM 8732 NH1 ARG H 203 59.147 −2.234 28.150 1.00 29.07 N ATOM 8733 NH2 ARG H 203 58.829 −0.285 26.973 1.00 29.38 N ATOM 8734 N ILE H 204 54.345 −4.284 26.054 1.00 35.87 N ATOM 8735 CA ILE H 204 55.050 −5.221 25.181 1.00 37.45 C ATOM 8736 C ILE H 204 56.449 −5.450 25.769 1.00 37.69 C ATOM 8737 O ILE H 204 57.172 −4.492 26.053 1.00 37.77 O ATOM 8738 CB ILE H 204 55.232 −4.654 23.741 1.00 38.36 C ATOM 8739 CG1 ILE H 204 53.878 −4.332 23.099 1.00 39.88 C ATOM 8740 CG2 ILE H 204 55.968 −5.673 22.876 1.00 39.29 C ATOM 8741 CD1 ILE H 204 53.061 −5.548 22.712 1.00 40.07 C ATOM 8742 N GLY H 205 56.824 −6.709 25.958 1.00 37.43 N ATOM 8743 CA GLY H 205 58.138 −7.011 26.500 1.00 37.45 C ATOM 8744 C GLY H 205 58.290 −6.855 28.002 1.00 37.05 C ATOM 8745 O GLY H 205 59.377 −7.089 28.538 1.00 37.32 O ATOM 8746 N GLY H 206 57.217 −6.456 28.683 1.00 36.41 N ATOM 8747 CA GLY H 206 57.271 −6.298 30.129 1.00 35.85 C ATOM 8748 C GLY H 206 58.381 −5.406 30.661 1.00 35.30 C ATOM 8749 O GLY H 206 58.754 −4.416 30.034 1.00 34.59 O ATOM 8750 N TYR H 207 58.907 −5.757 31.830 1.00 36.01 N ATOM 8751 CA TYR H 207 59.967 −4.974 32.448 1.00 36.69 C ATOM 8752 C TYR H 207 60.936 −5.836 33.257 1.00 36.92 C ATOM 8753 O TYR H 207 60.720 −7.037 33.437 1.00 35.87 O ATOM 8754 CB TYR H 207 59.362 −3.901 33.352 1.00 37.45 C ATOM 8755 CG TYR H 207 58.487 −4.456 34.449 1.00 38.55 C ATOM 8756 CD1 TYR H 207 57.111 −4.617 34.267 1.00 38.56 C ATOM 8757 CD2 TYR H 207 59.040 −4.837 35.673 1.00 39.04 C ATOM 8758 CE1 TYR H 207 56.302 −5.144 35.289 1.00 39.03 C ATOM 8759 CE2 TYR H 207 58.253 −5.367 36.692 1.00 39.41 C ATOM 8760 CZ TYR H 207 56.886 −5.518 36.499 1.00 40.67 C ATOM 8761 OH TYR H 207 56.119 −6.041 37.523 1.00 41.90 O ATOM 8762 N LYS H 208 62.005 −5.210 33.744 1.00 36.64 N ATOM 8763 CA LYS H 208 62.998 −5.917 34.533 1.00 37.93 C ATOM 8764 C LYS H 208 63.275 −5.173 35.839 1.00 38.82 C ATOM 8765 O LYS H 208 63.281 −3.942 35.879 1.00 38.86 O ATOM 8766 CB LYS H 208 64.296 −6.076 33.729 1.00 37.63 C ATOM 8767 CG LYS H 208 64.115 −6.787 32.381 1.00 37.50 C ATOM 8768 CD LYS H 208 65.439 −6.901 31.637 1.00 35.87 C ATOM 8769 CE LYS H 208 65.296 −7.633 30.323 1.00 34.97 C ATOM 8770 NZ LYS H 208 66.601 −7.668 29.613 1.00 35.16 N ATOM 8771 N VAL H 209 63.499 −5.931 36.906 1.00 40.16 N ATOM 8772 CA VAL H 209 63.782 −5.357 38.218 1.00 42.42 C ATOM 8773 C VAL H 209 65.049 −5.964 38.793 1.00 43.29 C ATOM 8774 O VAL H 209 65.201 −7.181 38.817 1.00 44.11 O ATOM 8775 CB VAL H 209 62.623 −5.625 39.221 1.00 42.75 C ATOM 8776 CG1 VAL H 209 63.016 −5.146 40.611 1.00 43.25 C ATOM 8777 CG2 VAL H 209 61.355 −4.912 38.768 1.00 42.93 C ATOM 8778 N ARG H 210 65.960 −5.109 39.244 1.00 44.93 N ATOM 8779 CA ARG H 210 67.213 −5.556 39.851 1.00 45.95 C ATOM 8780 C ARG H 210 67.195 −5.131 41.323 1.00 46.32 C ATOM 8781 O ARG H 210 67.588 −4.016 41.656 1.00 46.91 O ATOM 8782 CB ARG H 210 68.412 −4.920 39.135 1.00 45.23 C ATOM 8783 N ASN H 211 66.722 −6.025 42.188 1.00 46.95 N ATOM 8784 CA ASN H 211 66.635 −5.771 43.626 1.00 47.41 C ATOM 8785 C ASN H 211 67.921 −5.174 44.200 1.00 47.38 C ATOM 8786 O ASN H 211 67.883 −4.252 45.015 1.00 47.66 O ATOM 8787 CB ASN H 211 66.315 −7.079 44.354 1.00 46.75 C ATOM 8788 N GLN H 212 69.056 −5.711 43.765 1.00 47.31 N ATOM 8789 CA GLN H 212 70.361 −5.251 44.226 1.00 46.65 C ATOM 8790 C GLN H 212 70.569 −3.754 43.988 1.00 45.86 C ATOM 8791 O GLN H 212 71.284 −3.095 44.744 1.00 46.53 O ATOM 8792 CB GLN H 212 71.464 −6.046 43.517 1.00 46.71 C ATOM 8793 N HIS H 213 69.947 −3.223 42.938 1.00 44.51 N ATOM 8794 CA HIS H 213 70.082 −1.804 42.617 1.00 43.04 C ATOM 8795 C HIS H 213 68.806 −0.997 42.882 1.00 39.85 C ATOM 8796 O HIS H 213 68.765 0.201 42.598 1.00 38.79 O ATOM 8797 CB HIS H 213 70.487 −1.631 41.146 1.00 46.42 C ATOM 8798 CG HIS H 213 71.713 −2.398 40.757 1.00 49.71 C ATOM 8799 ND1 HIS H 213 72.887 −2.345 41.479 1.00 51.34 N ATOM 8800 CD2 HIS H 213 71.948 −3.230 39.715 1.00 50.77 C ATOM 8801 CE1 HIS H 213 73.791 −3.115 40.899 1.00 52.07 C ATOM 8802 NE2 HIS H 213 73.247 −3.663 39.827 1.00 51.31 N ATOM 8803 N TRP H 214 67.788 −1.650 43.441 1.00 36.77 N ATOM 8804 CA TRP H 214 66.497 −1.009 43.730 1.00 34.70 C ATOM 8805 C TRP H 214 66.008 −0.263 42.493 1.00 33.04 C ATOM 8806 O TRP H 214 65.596 0.896 42.565 1.00 31.58 O ATOM 8807 CB TRP H 214 66.618 −0.032 44.906 1.00 34.83 C ATOM 8808 CG TRP H 214 67.262 −0.625 46.124 1.00 35.66 C ATOM 8809 CD1 TRP H 214 68.591 −0.632 46.420 1.00 35.53 C ATOM 8810 CD2 TRP H 214 66.610 −1.344 47.184 1.00 35.05 C ATOM 8811 NE1 TRP H 214 68.810 −1.310 47.594 1.00 36.05 N ATOM 8812 CE2 TRP H 214 67.612 −1.760 48.083 1.00 35.32 C ATOM 8813 CE3 TRP H 214 65.276 −1.677 47.457 1.00 36.06 C ATOM 8814 CZ2 TRP H 214 67.326 −2.496 49.242 1.00 35.08 C ATOM 8815 CZ3 TRP H 214 64.987 −2.412 48.610 1.00 35.94 C ATOM 8816 CH2 TRP H 214 66.012 −2.812 49.487 1.00 35.22 C ATOM 8817 N SER H 215 66.035 −0.949 41.356 1.00 32.01 N ATOM 8818 CA SER H 215 65.645 −0.330 40.100 1.00 31.21 C ATOM 8819 C SER H 215 64.560 −1.030 39.289 1.00 30.29 C ATOM 8820 O SER H 215 64.356 −2.242 39.399 1.00 30.47 O ATOM 8821 CB SER H 215 66.878 −0.211 39.218 1.00 31.16 C ATOM 8822 OG SER H 215 67.349 −1.511 38.910 1.00 31.69 O ATOM 8823 N LEU H 216 63.888 −0.240 38.455 1.00 29.28 N ATOM 8824 CA LEU H 216 62.857 −0.728 37.539 1.00 27.87 C ATOM 8825 C LEU H 216 63.351 −0.322 36.152 1.00 26.76 C ATOM 8826 O LEU H 216 63.692 0.839 35.932 1.00 26.11 O ATOM 8827 CB LEU H 216 61.499 −0.066 37.800 1.00 28.18 C ATOM 8828 CG LEU H 216 60.431 −0.226 36.700 1.00 27.88 C ATOM 8829 CD1 LEU H 216 59.966 −1.669 36.632 1.00 27.76 C ATOM 8830 CD2 LEU H 216 59.244 0.672 36.992 1.00 27.10 C ATOM 8831 N ILE H 217 63.382 −1.276 35.224 1.00 26.12 N ATOM 8832 CA ILE H 217 63.859 −1.009 33.867 1.00 26.88 C ATOM 8833 C ILE H 217 62.852 −1.336 32.761 1.00 27.40 C ATOM 8834 O ILE H 217 62.284 −2.434 32.718 1.00 26.58 O ATOM 8835 CB ILE H 217 65.145 −1.806 33.572 1.00 27.88 C ATOM 8836 CG1 ILE H 217 66.264 −1.355 34.505 1.00 28.58 C ATOM 8837 CG2 ILE H 217 65.553 −1.626 32.120 1.00 27.63 C ATOM 8838 CD1 ILE H 217 67.515 −2.173 34.340 1.00 30.18 C ATOM 8839 N MET H 218 62.642 −0.374 31.866 1.00 27.21 N ATOM 8840 CA MET H 218 61.744 −0.548 30.729 1.00 28.46 C ATOM 8841 C MET H 218 62.535 −0.223 29.462 1.00 29.47 C ATOM 8842 O MET H 218 63.041 0.890 29.300 1.00 29.05 O ATOM 8843 CB MET H 218 60.512 0.362 30.838 1.00 28.18 C ATOM 8844 CG MET H 218 59.474 −0.101 31.867 1.00 29.87 C ATOM 8845 SD MET H 218 58.118 1.083 32.139 1.00 31.17 S ATOM 8846 CE MET H 218 58.975 2.346 33.116 1.00 32.28 C ATOM 8847 N GLU H 219 62.646 −1.213 28.580 1.00 29.76 N ATOM 8848 CA GLU H 219 63.386 −1.085 27.329 1.00 30.45 C ATOM 8849 C GLU H 219 62.485 −0.672 26.166 1.00 31.67 C ATOM 8850 O GLU H 219 61.289 −0.983 26.157 1.00 31.77 O ATOM 8851 CB GLU H 219 64.067 −2.427 27.017 1.00 30.73 C ATOM 8852 CG GLU H 219 64.930 −2.941 28.176 1.00 30.88 C ATOM 8853 CD GLU H 219 65.103 −4.453 28.183 1.00 32.39 C ATOM 8854 OE1 GLU H 219 64.093 −5.162 27.990 1.00 32.44 O ATOM 8855 OE2 GLU H 219 66.240 −4.937 28.404 1.00 32.35 O ATOM 8856 N SER H 220 63.068 0.040 25.198 1.00 31.54 N ATOM 8857 CA SER H 220 62.367 0.504 24.001 1.00 32.05 C ATOM 8858 C SER H 220 61.024 1.162 24.283 1.00 32.14 C ATOM 8859 O SER H 220 59.996 0.720 23.764 1.00 32.54 O ATOM 8860 CB SER H 220 62.153 −0.668 23.057 1.00 33.03 C ATOM 8861 OG SER H 220 63.347 −1.411 22.927 1.00 35.98 O ATOM 8862 N VAL H 221 61.035 2.227 25.080 1.00 31.04 N ATOM 8863 CA VAL H 221 59.801 2.909 25.443 1.00 31.01 C ATOM 8864 C VAL H 221 59.039 3.497 24.254 1.00 31.75 C ATOM 8865 O VAL H 221 59.632 3.864 23.229 1.00 31.26 O ATOM 8866 CB VAL H 221 60.058 4.033 26.481 1.00 28.69 C ATOM 8867 CG1 VAL H 221 60.706 3.452 27.714 1.00 29.39 C ATOM 8868 CG2 VAL H 221 60.936 5.115 25.883 1.00 30.09 C ATOM 8869 N VAL H 222 57.718 3.587 24.418 1.00 31.66 N ATOM 8870 CA VAL H 222 56.827 4.121 23.398 1.00 32.31 C ATOM 8871 C VAL H 222 55.855 5.081 24.067 1.00 33.19 C ATOM 8872 O VAL H 222 55.736 5.102 25.294 1.00 33.57 O ATOM 8873 CB VAL H 222 56.028 2.987 22.702 1.00 32.00 C ATOM 8874 CG1 VAL H 222 56.954 2.170 21.815 1.00 32.20 C ATOM 8875 CG2 VAL H 222 55.384 2.081 23.739 1.00 30.79 C ATOM 8876 N PRO H 223 55.151 5.895 23.271 1.00 34.18 N ATOM 8877 CA PRO H 223 54.185 6.863 23.800 1.00 34.61 C ATOM 8878 C PRO H 223 53.232 6.316 24.859 1.00 34.84 C ATOM 8879 O PRO H 223 52.960 6.988 25.848 1.00 35.37 O ATOM 8880 CB PRO H 223 53.461 7.341 22.544 1.00 34.95 C ATOM 8881 CG PRO H 223 54.580 7.344 21.527 1.00 34.86 C ATOM 8882 CD PRO H 223 55.285 6.029 21.804 1.00 34.68 C ATOM 8883 N SER H 224 52.734 5.096 24.667 1.00 35.09 N ATOM 8884 CA SER H 224 51.811 4.509 25.637 1.00 34.94 C ATOM 8885 C SER H 224 52.397 4.247 27.039 1.00 34.92 C ATOM 8886 O SER H 224 51.646 3.985 27.977 1.00 34.65 O ATOM 8887 CB SER H 224 51.206 3.215 25.077 1.00 35.60 C ATOM 8888 OG SER H 224 52.203 2.360 24.545 1.00 37.29 O ATOM 8889 N ASP H 225 53.723 4.322 27.186 1.00 34.37 N ATOM 8890 CA ASP H 225 54.361 4.107 28.491 1.00 33.89 C ATOM 8891 C ASP H 225 54.233 5.318 29.422 1.00 33.37 C ATOM 8892 O ASP H 225 54.572 5.252 30.604 1.00 33.39 O ATOM 8893 CB ASP H 225 55.844 3.754 28.318 1.00 34.24 C ATOM 8894 CG ASP H 225 56.045 2.352 27.793 1.00 35.08 C ATOM 8895 OD1 ASP H 225 55.378 1.430 28.311 1.00 34.26 O ATOM 8896 OD2 ASP H 225 56.871 2.164 26.876 1.00 35.90 O ATOM 8897 N LYS H 226 53.758 6.430 28.875 1.00 33.82 N ATOM 8898 CA LYS H 226 53.559 7.653 29.648 1.00 33.74 C ATOM 8899 C LYS H 226 52.706 7.352 30.881 1.00 32.86 C ATOM 8900 O LYS H 226 51.705 6.643 30.783 1.00 33.43 O ATOM 8901 CB LYS H 226 52.846 8.679 28.772 1.00 35.12 C ATOM 8902 CG LYS H 226 52.420 9.954 29.475 1.00 36.96 C ATOM 8903 CD LYS H 226 51.656 10.846 28.506 1.00 38.84 C ATOM 8904 CE LYS H 226 51.319 12.178 29.139 1.00 41.97 C ATOM 8905 NZ LYS H 226 52.566 12.900 29.517 1.00 43.84 N ATOM 8906 N GLY H 227 53.102 7.882 32.035 1.00 32.12 N ATOM 8907 CA GLY H 227 52.342 7.664 33.256 1.00 31.37 C ATOM 8908 C GLY H 227 53.187 7.849 34.509 1.00 31.81 C ATOM 8909 O GLY H 227 54.310 8.355 34.435 1.00 31.79 O ATOM 8910 N ASN H 228 52.646 7.447 35.655 1.00 31.03 N ATOM 8911 CA ASN H 226 53.354 7.550 36.921 1.00 30.85 C ATOM 8912 C ASN H 228 53.845 6.187 37.376 1.00 29.72 C ATOM 8913 O ASN H 228 53.123 5.191 37.279 1.00 30.39 O ATOM 8914 CB ASN H 228 52.454 8.138 38.002 1.00 32.32 C ATOM 8915 CG ASN H 228 52.044 9.561 37.700 1.00 34.94 C ATOM 8916 OD1 ASN H 228 52.877 10.394 37.331 1.00 35.94 O ATOM 8917 ND2 ASN H 228 50.757 9.853 37.855 1.00 35.31 N ATOM 8918 N TYR H 229 55.080 6.155 37.866 1.00 27.72 N ATOM 8919 CA TYR H 229 55.689 4.928 38.362 1.00 27.25 C ATOM 8920 C TYR H 229 56.153 5.166 39.799 1.00 27.25 C ATOM 8921 O TYR H 229 57.006 6.020 40.061 1.00 26.34 O ATOM 8922 CB TYR H 229 56.846 4.512 37.447 1.00 26.74 C ATOM 8923 CG TYR H 229 56.372 4.151 36.054 1.00 26.75 C ATOM 8924 CD1 TYR H 229 56.148 5.131 35.081 1.00 26.36 C ATOM 8925 CD2 TYR H 229 56.083 2.830 35.725 1.00 26.67 C ATOM 8926 CE1 TYR H 229 55.645 4.793 33.817 1.00 25.79 C ATOM 8927 CE2 TYR H 229 55.584 2.488 34.474 1.00 25.91 C ATOM 8928 CZ TYR H 229 55.368 3.464 33.528 1.00 26.33 C ATOM 8929 OH TYR H 229 54.882 3.082 32.287 1.00 27.87 O ATOM 8930 N THR H 230 55.568 4.405 40.722 1.00 26.69 N ATOM 8931 CA THR H 230 55.852 4.537 42.145 1.00 26.63 C ATOM 8932 C THR H 230 56.543 3.338 42.766 1.00 26.70 C ATOM 8933 O THR H 230 56.150 2.194 42.548 1.00 26.96 O ATOM 8934 CB THR H 230 54.550 4.774 42.930 1.00 27.14 C ATOM 8935 OG1 THR H 230 53.916 5.970 42.454 1.00 28.26 O ATOM 8936 CG2 THR H 230 54.834 4.896 44.425 1.00 27.42 C ATOM 8937 N CYS H 231 57.568 3.611 43.562 1.00 27.11 N ATOM 8938 CA CYS H 231 58.291 2.547 44.247 1.00 27.77 C ATOM 8939 C CYS H 231 57.852 2.567 45.713 1.00 27.56 C ATOM 8940 O CYS H 231 57.845 3.617 46.344 1.00 26.94 O ATOM 8941 CB CYS H 231 59.803 2.791 44.160 1.00 28.81 C ATOM 8942 SG CYS H 231 60.369 4.264 45.054 1.00 29.74 S ATOM 8943 N VAL H 232 57.464 1.405 46.234 1.00 29.02 N ATOM 8944 CA VAL H 232 57.048 1.257 47.632 1.00 30.32 C ATOM 8945 C VAL H 232 58.065 0.337 48.328 1.00 31.10 C ATOM 8946 O VAL H 232 58.294 −0.792 47.888 1.00 30.52 O ATOM 8947 CB VAL H 232 55.634 0.617 47.747 1.00 30.65 C ATOM 8948 CG1 VAL H 232 55.164 0.652 49.189 1.00 29.14 C ATOM 8949 CG2 VAL H 232 54.644 1.368 46.855 1.00 30.28 C ATOM 8950 N VAL H 233 58.664 0.822 49.415 1.00 31.38 N ATOM 8951 CA VAL H 233 59.678 0.057 50.131 1.00 32.74 C ATOM 8952 C VAL H 233 59.271 −0.123 51.583 1.00 33.12 C ATOM 8953 O VAL H 233 58.919 0.846 52.253 1.00 34.28 O ATOM 8954 CB VAL H 233 61.044 0.775 50.016 1.00 32.49 C ATOM 8955 CG1 VAL H 233 62.095 0.072 50.830 1.00 33.55 C ATOM 8956 CG2 VAL H 233 61.462 0.815 48.550 1.00 32.77 C ATOM 8957 N GLU H 234 59.322 −1.354 52.082 1.00 33.62 N ATOM 8958 CA GLU H 234 58.884 −1.588 53.453 1.00 34.62 C ATOM 8959 C GLU H 234 59.435 −2.781 54.233 1.00 33.75 C ATOM 8960 O GLU H 234 59.942 −3.754 53.671 1.00 33.82 O ATOM 8961 CB GLU H 234 57.358 −1.656 53.465 1.00 36.46 C ATOM 8962 CG GLU H 234 56.794 −2.727 52.553 1.00 39.69 C ATOM 8963 CD GLU H 234 55.327 −2.489 52.180 1.00 43.48 C ATOM 8964 OE1 GLU H 234 54.753 −3.359 51.485 1.00 43.83 O ATOM 8965 OE2 GLU H 234 54.751 −1.436 52.564 1.00 43.30 O ATOM 8966 N ASN H 235 59.337 −2.660 55.554 1.00 33.27 N ATOM 8967 CA ASN H 235 59.739 −3.701 56.500 1.00 33.61 C ATOM 8968 C ASN H 235 58.806 −3.533 57.700 1.00 33.99 C ATOM 8969 O ASN H 235 57.882 −2.713 57.655 1.00 33.48 O ATOM 8970 CB ASN H 235 61.225 −3.584 56.917 1.00 32.09 C ATOM 8971 CG ASN H 235 61.535 −2.342 57.754 1.00 31.97 C ATOM 8972 OD1 ASN H 235 60.664 −1.759 58.388 1.00 31.33 O ATOM 8973 ND2 ASN H 235 62.807 −1.961 57.780 1.00 31.28 N ATOM 8974 N GLU H 236 59.039 −4.293 58.764 1.00 34.43 N ATOM 8975 CA GLU H 236 58.196 −4.242 59.961 1.00 35.26 C ATOM 8976 C GLU H 236 58.071 −2.876 60.657 1.00 35.71 C ATOM 8977 O GLU H 236 57.095 −2.626 61.367 1.00 35.11 O ATOM 8978 CB GLU H 236 58.695 −5.275 60.983 1.00 34.81 C ATOM 8979 N TYR H 237 59.051 −1.998 60.462 1.00 35.47 N ATOM 8980 CA TYR H 237 59.024 −0.684 61.103 1.00 35.87 C ATOM 8981 C TYR H 237 58.606 0.489 60.216 1.00 35.74 C ATOM 8982 O TYR H 237 58.679 1.636 60.645 1.00 35.72 O ATOM 8983 CB TYR H 237 60.391 −0.351 61.703 1.00 36.51 C ATOM 8984 CG TYR H 237 60.972 −1.460 62.527 1.00 38.57 C ATOM 8985 CD1 TYR H 237 62.116 −2.128 62.105 1.00 39.34 C ATOM 8986 CD2 TYR H 237 60.372 −1.857 63.723 1.00 38.70 C ATOM 8987 CE1 TYR H 237 62.655 −3.164 62.854 1.00 41.42 C ATOM 8988 CE2 TYR H 237 60.895 −2.889 64.475 1.00 40.61 C ATOM 8989 CZ TYR H 237 62.043 −3.540 64.036 1.00 41.94 C ATOM 8990 OH TYR H 237 62.593 −4.558 64.780 1.00 44.10 O ATOM 8991 N GLY H 238 58.187 0.230 58.985 1.00 34.67 N ATOM 8992 CA GLY H 238 57.784 1.352 58.160 1.00 34.62 C ATOM 8993 C GLY H 238 57.605 1.088 56.682 1.00 34.06 C ATOM 8994 O GLY H 238 58.008 0.046 56.163 1.00 34.41 O ATOM 8995 N SER H 239 56.997 2.062 56.010 1.00 33.16 N ATOM 8996 CA SER H 239 56.734 1.997 54.579 1.00 32.94 C ATOM 8997 C SER H 239 56.846 3.394 53.977 1.00 32.43 C ATOM 8998 O SER H 239 56.203 4.333 54.451 1.00 32.53 O ATOM 8999 CB SER H 239 55.336 1.443 54.330 1.00 33.10 C ATOM 9000 OG SER H 239 55.033 1.451 52.946 1.00 35.89 O ATOM 9001 N ILE H 240 57.670 3.533 52.940 1.00 30.73 N ATOM 9002 CA ILE H 240 57.865 4.823 52.277 1.00 29.58 C ATOM 9003 C ILE H 240 57.766 4.656 50.764 1.00 28.89 C ATOM 9004 O ILE H 240 58.017 3.574 50.248 1.00 28.79 O ATOM 9005 CB ILE H 240 59.259 5.443 52.611 1.00 28.35 C ATOM 9006 CG1 ILE H 240 60.386 4.527 52.114 1.00 28.29 C ATOM 9007 CG2 ILE H 240 59.378 5.683 54.109 1.00 27.34 C ATOM 9008 CD1 ILE H 240 61.810 5.006 52.476 1.00 27.28 C ATOM 9009 N ASN H 241 57.402 5.726 50.060 1.00 28.56 N ATOM 9010 CA ASN H 241 57.281 5.676 48.604 1.00 28.26 C ATOM 9011 C ASN H 241 57.780 6.944 47.911 1.00 28.17 C ATOM 9012 O ASN H 241 57.936 7.995 48.534 1.00 28.13 O ATOM 9013 CB ASN H 241 55.830 5.428 48.199 1.00 28.67 C ATOM 9014 CG ASN H 241 54.884 6.490 48.733 1.00 30.86 C ATOM 9015 OD1 ASN H 241 54.186 6.281 49.737 1.00 32.41 O ATOM 9016 ND2 ASN H 241 54.864 7.639 48.078 1.00 30.28 N ATOM 9017 N HIS H 242 58.008 6.829 46.605 1.00 27.60 N ATOM 9018 CA HIS H 242 58.491 7.932 45.774 1.00 27.16 C ATOM 9019 C HIS H 242 57.861 7.760 44.386 1.00 26.91 C ATOM 9020 O HIS H 242 57.694 6.648 43.916 1.00 26.35 O ATOM 9021 CB HIS H 242 60.019 7.852 45.658 1.00 26.94 C ATOM 9022 CG HIS H 242 60.628 8.925 44.811 1.00 27.19 C ATOM 9023 ND1 HIS H 242 60.842 10.206 45.269 1.00 27.39 N ATOM 9024 CD2 HIS H 242 61.083 8.903 43.533 1.00 28.28 C ATOM 9025 CE1 HIS H 242 61.404 10.927 44.316 1.00 27.31 C ATOM 9026 NE2 HIS H 242 61.561 10.162 43.252 1.00 27.69 N ATOM 9027 N THR H 243 57.526 8.859 43.725 1.00 27.18 N ATOM 9028 CA THR H 243 56.894 8.755 42.423 1.00 28.17 C ATOM 9029 C THR H 243 57.613 9.480 41.300 1.00 29.37 C ATOM 9030 O THR H 243 58.041 10.629 41.452 1.00 28.73 O ATOM 9031 CB THR H 243 55.421 9.242 42.492 1.00 28.46 C ATOM 9032 OG1 THR H 243 54.657 8.327 43.295 1.00 26.48 O ATOM 9033 CG2 THR H 243 54.814 9.327 41.091 1.00 27.09 C ATOM 9034 N TYR H 244 57.744 8.773 40.179 1.00 29.94 N ATOM 9035 CA TYR H 244 58.381 9.285 38.973 1.00 32.10 C ATOM 9036 C TYR H 244 57.305 9.454 37.901 1.00 33.21 C ATOM 9037 O TYR H 244 56.330 8.698 37.869 1.00 33.58 O ATOM 9038 CB TYR H 244 59.422 8.283 38.448 1.00 32.60 C ATOM 9039 CG TYR H 244 60.686 8.203 39.265 1.00 33.86 C ATOM 9040 CD1 TYR H 244 61.081 7.005 39.862 1.00 34.01 C ATOM 9041 CD2 TYR H 244 61.504 9.323 39.424 1.00 33.69 C ATOM 9042 CE1 TYR H 244 62.274 6.922 40.601 1.00 34.99 C ATOM 9043 CE2 TYR H 244 62.691 9.254 40.153 1.00 34.59 C ATOM 9044 CZ TYR H 244 63.068 8.053 40.737 1.00 35.17 C ATOM 9045 OH TYR H 244 64.233 7.992 41.452 1.00 34.83 O ATOM 9046 N HIS H 245 57.485 10.436 37.025 1.00 33.44 N ATOM 9047 CA HIS H 245 56.551 10.656 35.920 1.00 33.62 C ATOM 9048 C HIS H 245 57.334 10.420 34.634 1.00 33.53 C ATOM 9049 O HIS H 245 58.431 10.961 34.463 1.00 33.32 O ATOM 9050 CB HIS H 245 56.005 12.087 35.939 1.00 33.59 C ATOM 9051 N LEU H 246 56.783 9.605 33.741 1.00 33.25 N ATOM 9052 CA LEU H 246 57.442 9.303 32.478 1.00 33.94 C ATOM 9053 C LEU H 246 56.714 9.881 31.265 1.00 34.90 C ATOM 9054 O LEU H 246 55.488 9.787 31.156 1.00 35.11 O ATOM 9055 CB LEU H 246 57.581 7.786 32.301 1.00 33.54 C ATOM 9056 CG LEU H 246 58.149 7.294 30.961 1.00 34.43 C ATOM 9057 CD1 LEU H 246 59.585 7.792 30.785 1.00 33.01 C ATOM 9058 CD2 LEU H 246 58.089 5.777 30.910 1.00 32.50 C ATOM 9059 N ASP H 247 57.482 10.465 30.353 1.00 35.61 N ATOM 9060 CA ASP H 247 56.944 11.033 29.127 1.00 37.11 C ATOM 9061 C ASP H 247 57.832 10.602 27.964 1.00 37.48 C ATOM 9062 O ASP H 247 59.058 10.634 28.066 1.00 37.54 O ATOM 9063 CB ASP H 247 56.912 12.550 29.224 1.00 39.91 C ATOM 9064 CG ASP H 247 55.542 13.115 28.940 1.00 42.18 C ATOM 9065 OD1 ASP H 247 55.139 14.058 29.651 1.00 44.55 O ATOM 9066 OD2 ASP H 247 54.875 12.622 28.004 1.00 43.69 O ATOM 9067 N VAL H 248 57.219 10.188 26.861 1.00 37.77 N ATOM 9068 CA VAL H 248 57.981 9.745 25.701 1.00 38.35 C ATOM 9069 C VAL H 248 57.724 10.631 24.490 1.00 38.52 C ATOM 9070 O VAL H 248 56.577 10.963 24.189 1.00 38.82 O ATOM 9071 CB VAL H 248 57.628 8.281 25.332 1.00 39.24 C ATOM 9072 CG1 VAL H 248 58.433 7.835 24.126 1.00 38.91 C ATOM 9073 CG2 VAL H 248 57.909 7.366 26.516 1.00 39.39 C ATOM 9074 N VAL H 249 58.797 11.010 23.797 1.00 38.34 N ATOM 9075 CA VAL H 249 58.692 11.855 22.616 1.00 38.12 C ATOM 9076 C VAL H 249 59.333 11.186 21.406 1.00 37.91 C ATOM 9077 O VAL H 249 60.488 10.757 21.447 1.00 37.97 O ATOM 9078 CB VAL H 249 59.370 13.225 22.835 1.00 39.72 C ATOM 9079 CG1 VAL H 249 59.227 14.079 21.589 1.00 40.27 C ATOM 9080 CG2 VAL H 249 58.741 13.936 24.022 1.00 39.98 C ATOM 9081 N GLU H 250 58.574 11.092 20.323 1.00 37.93 N ATOM 9082 CA GLU H 250 59.083 10.475 19.110 1.00 37.74 C ATOM 9083 C GLU H 250 59.862 11.506 18.317 1.00 37.23 C ATOM 9084 O GLU H 250 59.373 12.608 18.060 1.00 37.25 O ATOM 9085 CB GLU H 250 57.934 9.925 18.259 1.00 39.21 C ATOM 9086 CG GLU H 250 57.283 8.677 18.835 1.00 41.78 C ATOM 9087 CD GLU H 250 55.943 8.362 18.197 1.00 43.45 C ATOM 9088 OE1 GLU H 250 55.029 9.217 18.283 1.00 43.91 O ATOM 9089 OE2 GLU H 250 55.803 7.261 17.621 1.00 44.35 O ATOM 9090 N ARG H 251 61.084 11.157 17.943 1.00 36.00 N ATOM 9091 CA ARG H 251 61.907 12.065 17.173 1.00 35.19 C ATOM 9092 C ARG H 251 61.992 11.611 15.725 1.00 35.81 C ATOM 9093 O ARG H 251 61.891 10.416 15.422 1.00 36.37 O ATOM 9094 CB ARG H 251 63.329 12.170 17.760 1.00 33.44 C ATOM 9095 CG ARG H 251 63.431 12.648 19.220 1.00 30.61 C ATOM 9096 CD ARG H 251 62.608 13.895 19.515 1.00 29.36 C ATOM 9097 NE ARG H 251 62.964 15.055 18.698 1.00 26.84 N ATOM 9098 CZ ARG H 251 64.011 15.844 18.926 1.00 26.71 C ATOM 9099 NH1 ARG H 251 64.819 15.599 19.953 1.00 27.05 N ATOM 9100 NH2 ARG H 251 64.237 16.895 18.145 1.00 25.96 N ATOM 9101 N SER H 252 62.181 12.595 14.848 1.00 36.27 N ATOM 9102 CA SER H 252 62.311 12.341 13.425 1.00 36.60 C ATOM 9103 C SER H 252 63.600 12.969 12.887 1.00 36.76 C ATOM 9104 O SER H 252 63.639 14.146 12.563 1.00 36.31 O ATOM 9105 CB SER H 252 61.112 12.915 12.673 1.00 36.51 C ATOM 9106 OG SER H 252 61.353 12.873 11.278 1.00 37.79 O ATOM 9107 N PRO H 253 64.669 12.170 12.764 1.00 37.26 N ATOM 9108 CA PRO H 253 65.954 12.668 12.263 1.00 37.69 C ATOM 9109 C PRO H 253 66.035 12.810 10.735 1.00 37.97 C ATOM 9110 O PRO H 253 67.026 12.412 10.128 1.00 38.17 O ATOM 9111 CB PRO H 253 66.931 11.618 12.781 1.00 37.61 C ATOM 9112 CG PRO H 253 66.150 10.361 12.554 1.00 37.62 C ATOM 9113 CD PRO H 253 64.749 10.726 13.053 1.00 37.15 C ATOM 9114 N HIS H 254 65.010 13.375 10.107 1.00 37.79 N ATOM 9115 CA HIS H 254 65.036 13.527 8.654 1.00 37.61 C ATOM 9116 C HIS H 254 65.157 14.984 8.220 1.00 36.26 C ATOM 9117 O HIS H 254 64.863 15.904 8.987 1.00 35.10 O ATOM 9118 CB HIS H 254 63.768 12.945 8.013 1.00 39.78 C ATOM 9119 CG HIS H 254 63.513 11.506 8.348 1.00 43.24 C ATOM 9120 ND1 HIS H 254 62.942 11.106 9.539 1.00 44.40 N ATOM 9121 CD2 HIS H 254 63.732 10.373 7.638 1.00 44.25 C ATOM 9122 CE1 HIS H 254 62.814 9.790 9.547 1.00 44.51 C ATOM 9123 NE2 HIS H 254 63.286 9.320 8.405 1.00 45.34 N ATOM 9124 N ARG H 255 65.602 15.190 6.986 1.00 34.70 N ATOM 9125 CA ARG H 255 65.697 16.543 6.450 1.00 34.66 C ATOM 9126 C ARG H 255 64.234 16.947 6.199 1.00 32.87 C ATOM 9127 O ARG H 255 63.348 16.094 6.220 1.00 31.68 O ATOM 9128 CB ARG H 255 66.516 16.545 5.147 1.00 36.11 C ATOM 9129 CG ARG H 255 65.923 15.740 3.992 1.00 39.33 C ATOM 9130 CD ARG H 255 66.925 15.610 2.830 1.00 43.41 C ATOM 9131 NE ARG H 255 66.255 15.594 1.526 1.00 47.20 N ATOM 9132 CZ ARG H 255 65.493 14.602 1.065 1.00 48.68 C ATOM 9133 NH1 ARG H 255 65.293 13.509 1.790 1.00 49.44 N ATOM 9134 NH2 ARG H 255 64.897 14.719 −0.117 1.00 50.48 N ATOM 9135 N PRO H 256 63.956 18.238 5.962 1.00 32.44 N ATOM 9136 CA PRO H 256 62.562 18.655 5.727 1.00 31.90 C ATOM 9137 C PRO H 256 61.879 17.921 4.567 1.00 31.51 C ATOM 9138 O PRO H 256 62.496 17.656 3.541 1.00 31.23 O ATOM 9139 CB PRO H 256 62.681 20.160 5.437 1.00 31.84 C ATOM 9140 CG PRO H 256 63.959 20.555 6.105 1.00 32.24 C ATOM 9141 CD PRO H 256 64.870 19.381 5.788 1.00 31.98 C ATOM 9142 N ILE H 257 60.603 17.601 4.745 1.00 30.89 N ATOM 9143 CA ILE H 257 59.809 16.922 3.727 1.00 31.20 C ATOM 9144 C ILE H 257 58.727 17.884 3.195 1.00 30.90 C ATOM 9145 O ILE H 257 58.043 18.540 3.977 1.00 30.53 O ATOM 9146 CB ILE H 257 59.143 15.659 4.338 1.00 32.99 C ATOM 9147 CG1 ILE H 257 60.180 14.530 4.439 1.00 33.63 C ATOM 9148 CG2 ILE H 257 57.922 15.231 3.521 1.00 33.41 C ATOM 9149 CD1 ILE H 257 59.668 13.271 5.144 1.00 34.78 C ATOM 9150 N LEU H 258 58.594 17.992 1.872 1.00 29.84 N ATOM 9151 CA LEU H 258 57.578 18.870 1.293 1.00 29.28 C ATOM 9152 C LEU H 258 56.468 18.062 0.652 1.00 29.66 C ATOM 9153 O LEU H 258 56.679 16.938 0.197 1.00 29.28 O ATOM 9154 CB LEU H 258 58.157 19.789 0.222 1.00 27.98 C ATOM 9155 CG LEU H 258 59.413 20.606 0.512 1.00 29.09 C ATOM 9156 CD1 LEU H 258 59.627 21.596 −0.628 1.00 28.96 C ATOM 9157 CD2 LEU H 258 59.287 21.334 1.808 1.00 29.25 C ATOM 9158 ND GLN H 259 55.280 18.656 0.607 1.00 30.32 N ATOM 9159 CA GLN H 259 54.109 18.021 0.003 1.00 30.43 C ATOM 9160 C GLN H 259 54.277 17.965 −1.518 1.00 29.17 C ATOM 9161 O GLN H 259 54.605 18.967 −2.147 1.00 28.86 O ATOM 9162 CB GLN H 259 52.846 18.834 0.363 1.00 31.05 C ATOM 9163 CG GLN H 259 51.519 18.315 −0.222 1.00 31.55 C ATOM 9164 CD GLN H 259 50.304 19.180 0.162 1.00 32.40 C ATOM 9165 OE1 GLN H 259 50.084 19.480 1.336 1.00 31.59 O ATOM 9166 NE2 GLN H 259 49.510 19.569 −0.835 1.00 32.80 N ATOM 9167 N ALA H 260 54.050 16.795 −2.102 1.00 28.89 N ATOM 9168 CA ALA H 260 54.155 16.627 −3.549 1.00 29.45 C ATOM 9169 C ALA H 260 53.130 17.505 −4.268 1.00 29.81 C ATOM 9170 O ALA H 260 52.011 17.648 −3.801 1.00 29.56 O ATOM 9171 CB ALA H 260 53.922 15.174 −3.905 1.00 28.68 C ATOM 9172 N GLY H 261 53.514 18.093 −5.397 1.00 30.77 N ATOM 9173 CA GLY H 261 52.595 18.934 −6.148 1.00 31.72 C ATOM 9174 C GLY H 261 52.630 20.414 −5.805 1.00 32.63 C ATOM 9175 O GLY H 261 52.069 21.230 −6.535 1.00 32.86 O ATOM 9176 N LEU H 262 53.279 20.769 −4.699 1.00 33.34 N ATOM 9177 CA LEU H 262 53.364 22.169 −4.294 1.00 33.16 C ATOM 9178 C LEU H 262 54.810 22.636 −4.198 1.00 33.78 C ATOM 9179 O LEU H 262 55.663 21.937 −3.653 1.00 34.08 O ATOM 9180 CB LEU H 262 52.654 22.372 −2.949 1.00 32.41 C ATOM 9181 CG LEU H 262 51.125 22.199 −2.974 1.00 32.91 C ATOM 9182 CD1 LEU H 262 50.548 22.321 −1.561 1.00 31.68 C ATOM 9183 CD2 LEU H 262 50.515 23.261 −3.897 1.00 32.35 C ATOM 9184 N PRO H 263 55.106 23.828 −4.730 1.00 33.86 N ATOM 9185 CA PRO H 263 54.162 24.731 −5.398 1.00 34.62 C ATOM 9186 C PRO H 263 53.692 24.210 −6.762 1.00 35.16 C ATOM 9187 O PRO H 263 54.308 23.324 −7.353 1.00 35.17 O ATOM 9188 CB PRO H 263 54.965 26.022 −5.514 1.00 34.70 C ATOM 9189 CG PRO H 263 56.368 25.509 −5.724 1.00 34.09 C ATOM 9190 CD PRO H 263 56.456 24.412 −4.689 1.00 33.37 C ATOM 9191 N ALA H 264 52.593 24.767 −7.257 1.00 35.96 N ATOM 9192 CA ALA H 264 52.052 24.354 −8.547 1.00 37.08 C ATOM 9193 C ALA H 264 52.357 25.379 −9.637 1.00 37.85 C ATOM 9194 O ALA H 264 52.493 26.572 −9.361 1.00 37.83 O ATOM 9195 CB ALA H 264 50.559 24.159 −8.435 1.00 36.46 C ATOM 9196 N ASN H 265 52.484 24.907 −10.872 1.00 38.58 N ATOM 9197 CA ASN H 265 52.730 25.800 −11.995 1.00 39.78 C ATOM 9198 C ASN H 265 51.564 26.790 −12.067 1.00 41.26 C ATOM 9199 O ASN H 265 50.443 26.486 −11.653 1.00 40.55 O ATOM 9200 CB ASN H 265 52.808 25.025 −13.317 1.00 38.66 C ATOM 9201 CG ASN H 265 54.022 24.103 −13.399 1.00 38.73 C ATOM 9202 OD1 ASN H 265 55.143 24.494 −13.074 1.00 36.98 O ATOM 9203 ND2 ASN H 265 53.799 22.877 −13.856 1.00 38.25 N ATOM 9204 N ALA H 266 51.836 27.975 −12.595 1.00 42.81 N ATOM 9205 CA ALA H 266 50.817 29.005 −12.714 1.00 44.32 C ATOM 9206 C ALA H 266 50.978 29.762 −14.022 1.00 45.43 C ATOM 9207 O ALA H 266 52.088 29.900 −14.547 1.00 44.88 O ATOM 9208 CB ALA H 266 50.921 29.970 −11.545 1.00 44.47 C ATOM 9209 N SER H 267 49.861 30.253 −14.544 1.00 46.44 N ATOM 9210 CA SER H 267 49.873 31.010 −15.784 1.00 47.36 C ATOM 9211 C SER H 267 48.937 32.207 −15.656 1.00 47.83 C ATOM 9212 O SER H 267 47.907 32.136 −14.976 1.00 47.58 O ATOM 9213 CB SER H 267 49.441 30.110 −16.939 1.00 47.43 C ATOM 9214 OG SER H 267 49.592 30.777 −18.179 1.00 49.15 O ATOM 9215 N THR H 268 49.295 33.304 −16.313 1.00 47.79 N ATOM 9216 CA THR H 268 48.477 34.512 −16.264 1.00 48.27 C ATOM 9217 C THR H 268 48.836 35.504 −17.371 1.00 48.78 C ATOM 9218 O THR H 268 49.878 35.383 −18.021 1.00 48.83 O ATOM 9219 CB THR H 268 48.627 35.225 −14.899 1.00 47.98 C ATOM 9220 OG1 THR H 268 47.774 36.374 −14.866 1.00 48.48 O ATOM 9221 CG2 THR H 268 50.065 35.663 −14.677 1.00 47.38 C ATOM 9222 N VAL H 269 47.961 36.481 −17.588 1.00 48.82 N ATOM 9223 CA VAL H 269 48.196 37.507 −18.596 1.00 48.68 C ATOM 9224 C VAL H 269 48.993 38.625 −17.919 1.00 48.43 C ATOM 9225 O VAL H 269 48.927 38.781 −16.698 1.00 47.74 O ATOM 9226 CB VAL H 269 46.858 38.082 −19.132 1.00 48.31 C ATOM 9227 N VAL H 270 49.759 39.381 −18.699 1.00 48.71 N ATOM 9228 CA VAL H 270 50.541 40.484 −18.142 1.00 49.74 C ATOM 9229 C VAL H 270 49.587 41.324 −17.294 1.00 50.18 C ATOM 9230 O VAL H 270 48.443 41.548 −17.689 1.00 50.16 O ATOM 9231 CB VAL H 270 51.152 41.381 −19.264 1.00 49.84 C ATOM 9232 CG1 VAL H 270 51.888 42.557 −18.654 1.00 50.08 C ATOM 9233 CG2 VAL H 270 52.109 40.574 −20.128 1.00 49.80 C ATOM 9234 N GLY H 271 50.044 41.764 −16.124 1.00 51.04 N ATOM 9235 CA GLY H 271 49.195 42.573 −15.265 1.00 52.18 C ATOM 9236 C GLY H 271 48.353 41.793 −14.266 1.00 53.14 C ATOM 9237 O GLY H 271 47.632 42.386 −13.459 1.00 53.93 O ATOM 9238 N GLY H 272 48.439 40.467 −14.305 1.00 53.00 N ATOM 9239 CA GLY H 272 47.662 39.658 −13.379 1.00 53.12 C ATOM 9240 C GLY H 272 48.330 39.423 −12.034 1.00 52.85 C ATOM 9241 O GLY H 272 49.427 39.919 −11.770 1.00 52.78 O ATOM 9242 N ASP H 273 47.653 38.665 −11.178 1.00 52.73 N ATOM 9243 CA ASP H 273 48.156 38.333 −9.850 1.00 53.33 C ATOM 9244 C ASP H 273 48.303 36.815 −9.706 1.00 52.50 C ATOM 9245 O ASP H 273 47.527 36.050 −10.287 1.00 52.84 O ATOM 9246 CB ASP H 273 47.191 38.870 −8.792 1.00 55.38 C ATOM 9247 CG ASP H 273 47.200 40.384 −8.719 1.00 57.47 C ATOM 9248 OD1 ASP H 273 47.256 41.024 −9.793 1.00 58.51 O ATOM 9249 OD2 ASP H 273 47.144 40.934 −7.597 1.00 59.33 O ATOM 9250 N VAL H 274 49.285 36.377 −8.923 1.00 50.85 N ATOM 9251 CA VAL H 274 49.512 34.953 −8.746 1.00 48.93 C ATOM 9252 C VAL H 274 50.120 34.592 −7.386 1.00 47.83 C ATOM 9253 O VAL H 274 50.644 35.450 −6.674 1.00 47.74 O ATOM 9254 CB VAL H 274 50.413 34.433 −9.893 1.00 49.11 C ATOM 9255 CG1 VAL H 274 51.810 35.040 −9.781 1.00 48.48 C ATOM 9256 CG2 VAL H 274 50.456 32.929 −9.879 1.00 49.90 C ATOM 9257 N GLU H 275 50.029 33.318 −7.022 1.00 46.20 N ATOM 9258 CA GLU H 275 50.580 32.847 −5.763 1.00 45.12 C ATOM 9259 C GLU H 275 51.209 31.461 −5.912 1.00 43.67 C ATOM 9260 O GLU H 275 50.865 30.702 −6.817 1.00 43.08 O ATOM 9261 CB GLU H 275 49.491 32.791 −4.683 1.00 45.59 C ATOM 9262 CG GLU H 275 48.336 31.821 −4.962 1.00 46.75 C ATOM 9263 CD GLU H 275 47.542 31.474 −3.696 1.00 47.38 C ATOM 9264 OE1 GLU H 275 47.397 32.353 −2.829 1.00 48.10 O ATOM 9265 OE2 GLU H 275 47.056 30.328 −3.563 1.00 48.30 O ATOM 9266 N PHE H 276 52.141 31.150 −5.019 1.00 41.69 N ATOM 9267 CA PHE H 276 52.808 29.857 −5.003 1.00 39.52 C ATOM 9268 C PHE H 276 52.755 29.386 −3.564 1.00 39.03 C ATOM 9269 O PHE H 276 53.170 30.100 −2.648 1.00 38.10 O ATOM 9270 CB PHE H 276 54.249 29.988 −5.481 1.00 38.65 C ATOM 9271 CG PHE H 276 54.369 30.243 −6.951 1.00 38.48 C ATOM 9272 CD1 PHE H 276 54.031 29.256 −7.872 1.00 38.27 C ATOM 9273 CD2 PHE H 276 54.800 31.476 −7.421 1.00 38.58 C ATOM 9274 CE1 PHE H 276 54.121 29.495 −9.243 1.00 38.00 C ATOM 9275 CE2 PHE H 276 54.894 31.724 −8.790 1.00 38.36 C ATOM 9276 CZ PHE H 276 54.554 30.732 −9.702 1.00 37.74 C ATOM 9277 N VAL H 277 52.224 28.185 −3.368 1.00 37.80 N ATOM 9278 CA VAL H 277 52.069 27.633 −2.037 1.00 37.39 C ATOM 9279 C VAL H 277 53.056 26.509 −1.791 1.00 36.85 C ATOM 9280 O VAL H 277 53.412 25.765 −2.700 1.00 37.31 O ATOM 9281 CB VAL H 277 50.638 27.071 −1.835 1.00 37.65 C ATOM 9282 CG1 VAL H 277 50.423 26.681 −0.379 1.00 36.24 C ATOM 9283 CG2 VAL H 277 49.608 28.097 −2.299 1.00 38.51 C ATOM 9284 N CYS H 278 53.483 26.386 −0.544 1.00 36.31 N ATOM 9285 CA CYS H 278 54.421 25.348 −0.161 1.00 35.95 C ATOM 9286 C CYS H 278 53.983 24.777 1.183 1.00 34.83 C ATOM 9287 O CYS H 278 53.500 25.519 2.034 1.00 34.27 O ATOM 9288 GB CYS H 278 55.818 25.945 −0.043 1.00 35.67 C ATOM 9289 SG CYS H 278 57.046 24.702 0.310 1.00 39.57 S ATOM 9290 N LYS H 279 54.155 23.471 1.370 1.00 33.39 N ATOM 9291 CA LYS H 279 53.774 22.810 2.619 1.00 33.07 C ATOM 9292 C LYS H 279 54.944 21.983 3.186 1.00 32.16 C ATOM 9293 O LYS H 279 55.314 20.936 2.635 1.00 31.95 O ATOM 9294 CB LYS H 279 52.564 21.911 2.367 1.00 34.19 C ATOM 9295 CG LYS H 279 51.451 22.094 3.369 1.00 36.03 C ATOM 9296 CD LYS H 279 51.912 21.792 4.767 1.00 36.39 C ATOM 9297 CE LYS H 279 50.854 22.200 5.779 1.00 36.81 C ATOM 9298 NZ LYS H 279 51.292 21.982 7.178 1.00 36.20 N ATOM 9299 N VAL H 280 55.495 22.450 4.301 1.00 31.18 N ATOM 9300 CA VAL H 280 56.648 21.825 4.946 1.00 31.20 C ATOM 9301 C VAL H 280 56.417 21.072 6.264 1.00 31.10 C ATOM 9302 O VAL H 280 55.619 21.489 7.094 1.00 31.08 O ATOM 9303 CB VAL H 280 57.727 22.903 5.221 1.00 30.51 C ATOM 9304 CG1 VAL H 280 58.967 22.269 5.838 1.00 30.03 C ATOM 9305 CG2 VAL H 280 58.068 23.632 3.926 1.00 30.17 C ATOM 9306 N TYR H 281 57.150 19.971 6.442 1.00 31.13 N ATOM 9307 CA TYR H 281 57.110 19.165 7.666 1.00 31.35 C ATOM 9308 C TYR H 281 58.557 18.911 8.126 1.00 30.45 C ATOM 9309 O TYR H 281 59.417 18.558 7.317 1.00 29.54 O ATOM 9310 CB TYR H 281 56.426 17.805 7.433 1.00 34.05 C ATOM 9311 CG TYR H 281 54.983 17.892 6.985 1.00 35.89 C ATOM 9312 CD1 TYR H 281 54.661 17.969 5.632 1.00 36.41 C ATOM 9313 CD2 TYR H 281 53.945 17.962 7.919 1.00 36.66 C ATOM 9314 CE1 TYR H 281 53.347 18.123 5.208 1.00 37.37 C ATOM 9315 CE2 TYR H 281 52.615 18.118 7.509 1.00 37.92 C ATOM 9316 CZ TYR H 281 52.327 18.201 6.147 1.00 38.00 C ATOM 9317 OH TYR H 281 51.033 18.403 5.726 1.00 38.37 O ATOM 9318 N SER H 282 58.821 19.090 9.417 1.00 29.51 N ATOM 9319 CA SER H 282 60.159 18.875 9.962 1.00 29.67 C ATOM 9320 C SER H 282 60.142 18.858 11.497 1.00 29.90 C ATOM 9321 O SER H 282 59.332 19.538 12.126 1.00 30.45 O ATOM 9322 CB SER H 282 61.110 19.977 9.456 1.00 29.57 C ATOM 9323 OG SER H 282 62.438 19.767 9.908 1.00 29.13 O ATOM 9324 N ASP H 283 61.024 18.065 12.091 1.00 29.63 N ATOM 9325 CA ASP H 283 61.143 17.975 13.549 1.00 30.15 C ATOM 9326 C ASP H 283 62.118 19.096 13.941 1.00 30.23 C ATOM 9327 O ASP H 283 61.775 20.029 14.665 1.00 31.19 O ATOM 9328 CB ASP H 283 61.704 16.594 13.929 1.00 31.41 C ATOM 9329 CG ASP H 283 61.957 16.438 15.422 1.00 32.47 C ATOM 9330 OD1 ASP H 283 62.102 15.275 15.869 1.00 31.49 O ATOM 9331 OD2 ASP H 283 62.022 17.460 16.145 1.00 32.81 O ATOM 9332 N ALA H 284 63.342 18.985 13.451 1.00 29.34 N ATOM 9333 CA ALA H 284 64.356 19.997 13.683 1.00 29.14 C ATOM 9334 C ALA H 284 63.812 21.267 13.005 1.00 28.51 C ATOM 9335 O ALA H 284 63.304 21.194 11.897 1.00 28.63 O ATOM 9336 CB ALA H 284 65.669 19.559 13.014 1.00 27.52 C ATOM 9337 N GLN H 285 63.917 22.414 13.663 1.00 28.67 N ATOM 9338 CA GLN H 285 63.416 23.671 13.111 1.00 28.52 C ATOM 9339 C GLN H 285 63.883 23.876 11.662 1.00 28.22 C ATOM 9340 O GLN H 285 65.083 23.898 11.391 1.00 28.44 O ATOM 9341 CB GLN H 285 63.912 24.822 13.984 1.00 29.12 C ATOM 9342 CG GLN H 285 62.896 25.925 14.200 1.00 28.42 C ATOM 9343 CD GLN H 285 61.558 25.395 14.677 1.00 28.46 C ATOM 9344 OE1 GLN H 285 61.491 24.469 15.496 1.00 28.03 O ATOM 9345 NE2 GLN H 285 60.482 25.991 14.177 1.00 26.08 N ATOM 9346 N PRO H 286 62.946 24.020 10.712 1.00 27.62 N ATOM 9347 CA PRO H 286 63.296 24.219 9.299 1.00 27.16 C ATOM 9348 C PRO H 286 63.381 25.703 8.907 1.00 28.07 C ATOM 9349 O PRO H 286 62.701 26.545 9.496 1.00 28.41 O ATOM 9350 CB PRO H 286 62.155 23.533 8.577 1.00 27.57 C ATOM 9351 CG PRO H 286 60.981 23.969 9.420 1.00 27.78 C ATOM 9352 CD PRO H 286 61.502 23.752 10.851 1.00 28.09 C ATOM 9353 N HIS H 287 64.212 26.012 7.915 1.00 27.90 N ATOM 9354 CA HIS H 287 64.355 27.382 7.425 1.00 28.46 C ATOM 9355 C HIS H 287 63.843 27.395 5.989 1.00 28.05 C ATOM 9356 O HIS H 287 64.366 26.710 5.122 1.00 27.07 O ATOM 9357 CB HIS H 287 65.817 27.854 7.471 1.00 27.74 C ATOM 9358 CG HIS H 287 65.993 29.265 7.010 1.00 29.87 C ATOM 9359 ND1 HIS H 287 66.529 29.587 5.782 1.00 31.80 N ATOM 9360 CD2 HIS H 287 65.626 30.441 7.579 1.00 30.30 C ATOM 9361 CE1 HIS H 287 66.479 30.898 5.611 1.00 31.47 C ATOM 9362 NE2 HIS H 287 65.934 31.440 6.687 1.00 30.23 N ATOM 9363 N ILE H 288 62.806 28.185 5.753 1.00 29.18 N ATOM 9364 CA ILE H 288 62.169 28.263 4.448 1.00 29.25 C ATOM 9365 C ILE H 288 62.433 29.573 3.689 1.00 30.96 C ATOM 9366 O ILE H 288 62.399 30.664 4.266 1.00 31.51 O ATOM 9367 CB ILE H 288 60.642 28.082 4.621 1.00 28.49 C ATOM 9368 CG1 ILE H 288 60.373 26.832 5.481 1.00 29.99 C ATOM 9369 CG2 ILE H 288 59.969 27.980 3.269 1.00 28.50 C ATOM 9370 CD1 ILE H 288 58.884 26.559 5.795 1.00 28.45 C ATOM 9371 N GLN H 289 62.696 29.460 2.390 1.00 31.82 N ATOM 9372 CA GLN H 289 62.923 30.631 1.552 1.00 32.69 C ATOM 9373 C GLN H 289 62.388 30.368 0.156 1.00 32.57 C ATOM 9374 O GLN H 289 62.260 29.212 −0.254 1.00 32.41 O ATOM 9375 CB GLN H 289 64.414 30.963 1.458 1.00 33.25 C ATOM 9376 CG GLN H 289 65.269 29.878 0.859 1.00 33.75 C ATOM 9377 CD GLN H 289 66.744 30.258 0.825 1.00 35.50 C ATOM 9378 OE1 GLN H 289 67.139 31.179 0.112 1.00 36.06 O ATOM 9379 NE2 GLN H 289 67.564 29.547 1.602 1.00 34.39 N ATOM 9380 N TRP H 290 62.060 31.440 −0.559 1.00 31.53 N ATOM 9381 CA TRP H 290 61.570 31.333 −1.922 1.00 32.53 C ATOM 9382 C TRP H 290 62.642 31.893 −2.848 1.00 33.98 C ATOM 9383 O TRP H 290 63.164 32.985 −2.617 1.00 33.48 O ATOM 9384 CB TRP H 290 60.265 32.108 −2.102 1.00 30.04 C ATOM 9385 CG TRP H 290 59.055 31.426 −1.495 1.00 28.03 C ATOM 9386 CD1 TRP H 290 58.547 31.625 −0.250 1.00 27.08 C ATOM 9387 CD2 TRP H 290 58.199 30.459 −2.128 1.00 26.37 C ATOM 9388 NE1 TRP H 290 57.422 30.852 −0.064 1.00 26.17 N ATOM 9389 CE2 TRP H 290 57.186 30.126 −1.201 1.00 26.79 C ATOM 9390 CE3 TRP H 290 58.186 29.850 −3.390 1.00 25.93 C ATOM 9391 CZ2 TRP H 290 56.159 29.205 −1.498 1.00 25.61 C ATOM 9392 CZ3 TRP H 290 57.170 28.937 −3.685 1.00 26.82 C ATOM 9393 CH2 TRP H 290 56.166 28.627 −2.737 1.00 25.68 C ATOM 9394 N ILE H 291 62.955 31.138 −3.896 1.00 35.66 N ATOM 9395 CA ILE H 291 63.989 31.515 −4.844 1.00 39.09 C ATOM 9396 C ILE H 291 63.525 31.573 −6.304 1.00 40.97 C ATOM 9397 O ILE H 291 62.742 30.736 −6.759 1.00 41.16 O ATOM 9398 CB ILE H 291 65.171 30.518 −4.771 1.00 38.90 C ATOM 9399 CG1 ILE H 291 65.583 30.296 −3.311 1.00 40.33 C ATOM 9400 CG2 ILE H 291 66.337 31.044 −5.587 1.00 39.19 C ATOM 9401 CD1 ILE H 291 66.613 29.197 −3.115 1.00 40.21 C ATOM 9402 N LYS H 292 64.030 32.561 −7.034 1.00 42.59 N ATOM 9403 CA LYS H 292 63.716 32.732 −8.449 1.00 44.15 C ATOM 9404 C LYS H 292 65.004 32.417 −9.215 1.00 44.86 C ATOM 9405 O LYS H 292 66.073 32.920 −8.859 1.00 44.43 O ATOM 9406 CB LYS H 292 63.294 34.179 −8.708 1.00 44.79 C ATOM 9407 CG LYS H 292 62.216 34.374 −9.782 1.00 46.10 C ATOM 9408 CD LYS H 292 62.752 34.216 −11.188 1.00 46.60 C ATOM 9409 CE LYS H 292 61.676 34.580 −12.217 1.00 46.77 C ATOM 9410 NZ LYS H 292 62.245 34.792 −13.575 1.00 46.44 N ATOM 9411 N HIS H 293 64.916 31.571 −10.239 1.00 46.05 N ATOM 9412 CA HIS H 293 66.097 31.225 −11.031 1.00 47.50 C ATOM 9413 C HIS H 293 66.315 32.299 −12.092 1.00 48.23 C ATOM 9414 O HIS H 293 65.552 32.398 −13.044 1.00 49.00 O ATOM 9415 CB HIS H 293 65.919 29.857 −11.699 1.00 47.52 C ATOM 9416 N VAL H 294 67.349 33.114 −11.925 1.00 49.24 N ATOM 9417 CA VAL H 294 67.626 34.182 −12.886 1.00 49.93 C ATOM 9418 C VAL H 294 68.978 33.999 −13.575 1.00 50.69 C ATOM 9419 O VAL H 294 69.468 34.901 −14.265 1.00 52.03 O ATOM 9420 CB VAL H 294 67.604 35.562 −12.196 1.00 49.74 C ATOM 9421 CG1 VAL H 294 66.247 35.806 −11.558 1.00 49.61 C ATOM 9422 CG2 VAL H 294 68.700 35.631 −11.142 1.00 50.11 C ATOM 9423 N PRO H 307 74.376 28.181 −11.083 1.00 60.18 N ATOM 9424 CA PRO H 307 73.015 28.699 −11.266 1.00 59.57 C ATOM 9425 C PRO H 307 72.797 30.049 −10.589 1.00 58.87 C ATOM 9426 O PRO H 307 72.977 30.187 −9.378 1.00 58.70 O ATOM 9427 CB PRO H 307 72.141 27.600 −10.661 1.00 59.86 C ATOM 9428 CG PRO H 307 73.005 27.068 −9.555 1.00 60.24 C ATOM 9429 CD PRO H 307 74.370 26.983 −10.222 1.00 60.69 C ATOM 9430 N TYR H 308 72.419 31.045 −11.387 1.00 57.90 N ATOM 9431 CA TYR H 308 72.163 32.385 −10.878 1.00 56.75 C ATOM 9432 C TYR H 308 70.820 32.403 −10.157 1.00 56.02 C ATOM 9433 O TYR H 308 69.766 32.244 −10.780 1.00 55.98 O ATOM 9434 CB TYR H 308 72.148 33.398 −12.025 1.00 57.22 C ATOM 9435 N LEU H 309 70.865 32.605 −8.843 1.00 54.51 N ATOM 9436 CA LEU H 309 69.653 32.631 −8.034 1.00 52.98 C ATOM 9437 C LEU H 309 69.388 33.991 −7.398 1.00 51.39 C ATOM 9438 O LEU H 309 70.307 34.780 −7.194 1.00 52.19 O ATOM 9439 CB LEU H 309 69.738 31.569 −6.936 1.00 53.03 C ATOM 9440 CG LEU H 309 69.988 30.127 −7.391 1.00 53.20 C ATOM 9441 CD1 LEU H 309 70.038 29.221 −6.170 1.00 53.52 C ATOM 9442 CD2 LEU H 309 68.886 29.679 −8.349 1.00 53.46 C ATOM 9443 N LYS H 310 68.122 34.256 −7.095 1.00 48.98 N ATOM 9444 CA LYS H 310 67.719 35.502 −6.453 1.00 46.80 C ATOM 9445 C LYS H 310 66.721 35.182 −5.341 1.00 45.04 C ATOM 9446 O LYS H 310 65.668 34.594 −5.592 1.00 43.73 O ATOM 9447 CB LYS H 310 67.071 36.446 −7.470 1.00 47.70 C ATOM 9448 N VAL H 311 67.060 35.568 −4.114 1.00 43.31 N ATOM 9449 CA VAL H 311 66.203 35.317 −2.961 1.00 41.81 C ATOM 9450 C VAL H 311 65.068 36.326 −2.870 1.00 41.18 C ATOM 9451 O VAL H 311 65.292 37.513 −2.631 1.00 41.93 O ATOM 9452 CB VAL H 311 67.014 35.361 −1.641 1.00 41.66 C ATOM 9453 CG1 VAL H 311 66.072 35.199 −0.438 1.00 41.45 C ATOM 9454 CG2 VAL H 311 68.075 34.265 −1.649 1.00 40.22 C ATOM 9455 N LEU H 312 63.846 35.846 −3.047 1.00 39.47 N ATOM 9456 CA LEU H 312 62.678 36.712 −2.997 1.00 39.06 C ATOM 9457 C LEU H 312 62.191 36.958 −1.580 1.00 38.82 C ATOM 9458 O LEU H 312 61.750 38.059 −1.246 1.00 39.00 O ATOM 9459 CB LEU H 312 61.530 36.093 −3.795 1.00 38.04 C ATOM 9460 CG LEU H 312 61.868 35.589 −5.194 1.00 38.09 C ATOM 9461 CD1 LEU H 312 60.606 35.046 −5.840 1.00 37.34 C ATOM 9462 CD2 LEU H 312 62.478 36.724 −6.030 1.00 38.16 C ATOM 9463 N LYS H 313 62.294 35.935 −0.741 1.00 38.00 N ATOM 9464 CA LYS H 313 61.788 36.022 0.615 1.00 36.74 C ATOM 9465 C LYS H 313 62.424 34.902 1.447 1.00 35.97 C ATOM 9466 O LYS H 313 62.619 33.790 0.949 1.00 35.18 O ATOM 9467 CB LYS H 313 60.271 35.853 0.496 1.00 36.72 C ATOM 9468 CG LYS H 313 59.418 35.909 1.718 1.00 37.50 C ATOM 9469 CD LYS H 313 57.995 35.679 1.221 1.00 37.93 C ATOM 9470 CE LYS H 313 56.951 35.675 2.312 1.00 38.60 C ATOM 9471 NZ LYS H 313 55.667 35.265 1.685 1.00 37.65 N ATOM 9472 N ALA H 314 62.751 35.196 2.703 1.00 34.47 N ATOM 9473 CA ALA H 314 63.368 34.208 3.583 1.00 33.45 C ATOM 9474 C ALA H 314 62.896 34.356 5.021 1.00 32.58 C ATOM 9475 O ALA H 314 62.744 35.470 5.532 1.00 31.18 O ATOM 9476 CB ALA H 314 64.905 34.312 3.519 1.00 33.76 C ATOM 9477 N ALA H 315 62.679 33.213 5.670 1.00 31.78 N ATOM 9478 CA ALA H 315 62.209 33.164 7.051 1.00 31.19 C ATOM 9479 C ALA H 315 63.200 33.782 8.041 1.00 31.17 C ATOM 9480 O ALA H 315 64.415 33.771 7.825 1.00 29.04 O ATOM 9481 CB ALA H 315 61.929 31.722 7.444 1.00 31.28 C ATOM 9482 N GLY H 316 62.659 34.308 9.133 1.00 31.15 N ATOM 9483 CA GLY H 316 63.481 34.920 10.158 1.00 33.15 C ATOM 9484 C GLY H 316 62.631 35.677 11.161 1.00 35.11 C ATOM 9485 O GLY H 316 61.394 35.625 11.113 1.00 34.36 O ATOM 9486 N VAL H 317 63.292 36.379 12.075 1.00 36.85 N ATOM 9487 CA VAL H 317 62.585 37.151 13.091 1.00 39.38 C ATOM 9488 C VAL H 317 61.681 38.230 12.482 1.00 40.23 C ATOM 9489 O VAL H 317 60.631 38.547 13.039 1.00 40.13 O ATOM 9490 CB VAL H 317 63.575 37.798 14.081 1.00 39.91 C ATOM 9491 CG1 VAL H 317 62.938 39.022 14.731 1.00 41.41 C ATOM 9492 CG2 VAL H 317 63.956 36.784 15.158 1.00 39.67 C ATOM 9493 N ASN H 318 62.081 38.777 11.335 1.00 41.18 N ATOM 9494 CA ASN H 318 61.285 39.805 10.676 1.00 42.85 C ATOM 9495 C ASN H 318 60.330 39.246 9.621 1.00 43.52 C ATOM 9496 O ASN H 318 59.555 39.994 9.038 1.00 45.16 O ATOM 9497 CB ASN H 318 62.203 40.852 10.031 1.00 43.45 C ATOM 9498 N THR H 319 60.393 37.940 9.372 1.00 43.55 N ATOM 9499 CA THR H 319 59.522 37.289 8.390 1.00 42.98 C ATOM 9500 C THR H 319 59.194 35.906 8.959 1.00 42.78 C ATOM 9501 O THR H 319 59.766 34.895 8.550 1.00 42.38 O ATOM 9502 CB THR H 319 60.234 37.120 7.028 1.00 43.83 C ATOM 9503 OG1 THR H 319 60.967 38.310 6.712 1.00 44.68 O ATOM 9504 CG2 THR H 319 59.213 36.859 5.921 1.00 42.87 C ATOM 9505 N THR H 320 58.271 35.892 9.914 1.00 42.01 N ATOM 9506 CA THR H 320 57.839 34.694 10.628 1.00 42.17 C ATOM 9507 C THR H 320 57.305 33.541 9.773 1.00 40.98 C ATOM 9508 O THR H 320 56.901 33.738 8.627 1.00 40.68 O ATOM 9509 CB THR H 320 56.792 35.101 11.700 1.00 43.14 C ATOM 9510 OG1 THR H 320 57.448 35.887 12.702 1.00 45.22 O ATOM 9511 CG2 THR H 320 56.151 33.889 12.360 1.00 45.06 C ATOM 9512 N ASP H 321 57.318 32.333 10.342 1.00 39.70 N ATOM 9513 CA ASP H 321 56.835 31.149 9.639 1.00 38.81 C ATOM 9514 C ASP H 321 55.326 31.172 9.375 1.00 38.85 C ATOM 9515 O ASP H 321 54.837 30.461 8.507 1.00 38.89 O ATOM 9516 CB ASP H 321 57.197 29.874 10.411 1.00 37.34 C ATOM 9517 CG ASP H 321 58.693 29.589 10.407 1.00 36.21 C ATOM 9518 OD1 ASP H 321 59.383 30.100 9.500 1.00 35.02 O ATOM 9519 OD2 ASP H 321 59.166 28.843 11.296 1.00 33.81 O ATOM 9520 N LYS H 322 54.590 31.993 10.120 1.00 38.99 N ATOM 9521 CA LYS H 322 53.143 32.083 9.953 1.00 38.60 C ATOM 9522 C LYS H 322 52.720 32.329 8.499 1.00 37.91 C ATOM 9523 O LYS H 322 51.747 31.742 8.015 1.00 36.72 O ATOM 9524 CB LYS H 322 52.580 33.199 10.846 1.00 38.53 C ATOM 9525 N GLU H 323 53.458 33.182 7.797 1.00 37.47 N ATOM 9526 CA GLU H 323 53.112 33.495 6.419 1.00 37.78 C ATOM 9527 C GLU H 323 54.225 33.234 5.394 1.00 37.88 C ATOM 9528 O GLU H 323 54.135 33.667 4.244 1.00 37.65 O ATOM 9529 CB GLU H 323 52.645 34.953 6.336 1.00 37.67 C ATOM 9530 N ILE H 324 55.257 32.502 5.801 1.00 37.50 N ATOM 9531 CA ILE H 324 56.370 32.225 4.904 1.00 37.08 C ATOM 9532 C ILE H 324 56.077 31.163 3.821 1.00 36.29 C ATOM 9533 O ILE H 324 56.713 31.166 2.773 1.00 35.74 O ATOM 9534 CB ILE H 324 57.631 31.849 5.737 1.00 37.12 C ATOM 9535 CG1 ILE H 324 58.866 32.552 5.159 1.00 38.18 C ATOM 9536 CG2 ILE H 324 57.798 30.336 5.816 1.00 36.42 C ATOM 9537 CD1 ILE H 324 59.214 32.162 3.758 1.00 38.53 C ATOM 9538 N GLU H 325 55.097 30.291 4.048 1.00 35.93 N ATOM 9539 CA GLU H 325 54.785 29.252 3.069 1.00 36.88 C ATOM 9540 C GLU H 325 53.963 29.653 1.841 1.00 37.34 C ATOM 9541 O GLU H 325 53.660 28.815 0.996 1.00 36.84 O ATOM 9542 CB GLU H 325 54.137 28.064 3.769 1.00 37.33 C ATOM 9543 CG GLU H 325 55.112 27.279 4.649 1.00 38.42 C ATOM 9544 CD GLU H 325 54.409 26.228 5.498 1.00 39.29 C ATOM 9545 OE1 GLU H 325 53.518 26.613 6.291 1.00 39.31 O ATOM 9546 OE2 GLU H 325 54.742 25.029 5.368 1.00 37.77 O ATOM 9547 N VAL H 326 53.603 30.925 1.728 1.00 37.78 N ATOM 9548 CA VAL H 326 52.862 31.373 0.556 1.00 39.52 C ATOM 9549 C VAL H 326 53.555 32.610 −0.020 1.00 39.99 C ATOM 9550 O VAL H 326 53.880 33.536 0.714 1.00 40.78 O ATOM 9551 CB VAL H 326 51.375 31.676 0.903 1.00 40.06 C ATOM 9552 CG1 VAL H 326 51.289 32.735 2.006 1.00 41.95 C ATOM 9553 CG2 VAL H 326 50.638 32.143 −0.342 1.00 39.31 C ATOM 9554 N LEU H 327 53.817 32.597 −1.326 1.00 40.27 N ATOM 9555 CA LEU H 327 54.478 33.712 −2.006 1.00 40.64 C ATOM 9556 C LEU H 327 53.508 34.372 −2.970 1.00 42.00 C ATOM 9557 O LEU H 327 52.989 33.720 −3.882 1.00 41.64 O ATOM 9558 CB LEU H 327 55.700 33.238 −2.803 1.00 38.86 C ATOM 9559 CG LEU H 327 56.432 34.300 −3.636 1.00 37.79 C ATOM 9560 CD1 LEU H 327 57.253 35.215 −2.718 1.00 36.93 C ATOM 9561 CD2 LEU H 327 57.346 33.624 −4.645 1.00 36.04 C ATOM 9562 N TYR H 328 53.277 35.666 −2.769 1.00 42.93 N ATOM 9563 CA TYR H 328 52.371 36.427 −3.624 1.00 44.15 C ATOM 9564 C TYR H 328 53.129 37.341 −4.591 1.00 45.79 C ATOM 9565 O TYR H 328 54.136 37.956 −4.226 1.00 45.90 O ATOM 9566 CB TYR H 328 51.400 37.278 −2.770 1.00 42.30 C ATOM 9567 CG TYR H 328 50.434 36.476 −1.911 1.00 41.07 C ATOM 9568 CD1 TYR H 328 50.642 36.331 −0.532 1.00 40.43 C ATOM 9569 CD2 TYR H 328 49.340 35.820 −2.484 1.00 40.34 C ATOM 9570 CE1 TYR H 328 49.784 35.548 0.254 1.00 39.51 C ATOM 9571 CE2 TYR H 328 48.483 35.031 −1.714 1.00 39.61 C ATOM 9572 CZ TYR H 328 48.712 34.897 −0.349 1.00 40.54 C ATOM 9573 OH TYR H 328 47.891 34.077 0.398 1.00 41.41 O ATOM 9574 N ILE H 329 52.649 37.407 −5.832 1.00 47.90 N ATOM 9575 CA ILE H 329 53.243 38.277 −6.849 1.00 49.69 C ATOM 9576 C ILE H 329 52.121 38.962 −7.620 1.00 51.11 C ATOM 9577 O ILE H 329 51.392 38.317 −8.372 1.00 50.96 O ATOM 9578 CB ILE H 329 54.107 37.512 −7.844 1.00 49.40 C ATOM 9579 CG1 ILE H 329 55.273 36.854 −7.113 1.00 49.02 C ATOM 9580 CG2 ILE H 329 54.619 38.469 −8.911 1.00 48.86 C ATOM 9581 CD1 ILE H 329 56.103 35.964 −7.994 1.00 49.85 C ATOM 9582 N ARG H 330 51.987 40.270 −7.425 1.00 52.65 N ATOM 9583 CA ARG H 330 50.937 41.026 −8.092 1.00 54.33 C ATOM 9584 C ARG H 330 51.419 41.888 −9.254 1.00 54.53 C ATOM 9585 O ARG H 330 52.595 42.253 −9.340 1.00 53.97 O ATOM 9586 CB ARG H 330 50.177 41.898 −7.084 1.00 56.10 C ATOM 9587 CG ARG H 330 49.459 41.108 −5.994 1.00 58.20 C ATOM 9588 CD ARG H 330 48.308 41.898 −5.396 1.00 59.84 C ATOM 9589 NE ARG H 330 47.443 41.061 −4.564 1.00 62.08 N ATOM 9590 CZ ARG H 330 46.223 41.403 −4.156 1.00 62.89 C ATOM 9591 NH1 ARG H 330 45.706 42.574 −4.498 1.00 63.06 N ATOM 9592 NH2 ARG H 330 45.515 40.569 −3.406 1.00 63.25 N ATOM 9593 N ASN H 331 50.489 42.193 −10.158 1.00 55.19 N ATOM 9594 CA ASN H 331 50.777 43.016 −11.326 1.00 55.80 C ATOM 9595 C ASN H 331 52.050 42.499 −12.001 1.00 56.05 C ATOM 9596 O ASN H 331 53.023 43.237 −12.177 1.00 55.89 O ATOM 9597 CB ASN H 331 50.937 44.480 −10.877 1.00 56.20 C ATOM 9598 CG ASN H 331 50.917 45.455 −12.038 1.00 56.60 C ATOM 9599 OD1 ASN H 331 50.701 45.075 −13.187 1.00 57.12 O ATOM 9600 ND2 ASN H 331 51.137 46.730 −11.737 1.00 55.92 N ATOM 9601 N VAL H 332 52.029 41.224 −12.387 1.00 56.09 N ATOM 9602 CA VAL H 332 53.188 40.593 −13.014 1.00 55.89 C ATOM 9603 C VAL H 332 53.578 41.172 −14.367 1.00 55.80 C ATOM 9604 O VAL H 332 52.735 41.652 −15.127 1.00 55.56 O ATOM 9605 CB VAL H 332 52.988 39.067 −13.197 1.00 55.93 C ATOM 9606 CG1 VAL H 332 52.608 38.419 −11.872 1.00 56.01 C ATOM 9607 CG2 VAL H 332 51.930 38.803 −14.240 1.00 56.49 C ATOM 9608 N THR H 333 54.876 41.117 −14.648 1.00 55.86 N ATOM 9609 CA THR H 333 55.437 41.591 −15.905 1.00 55.84 C ATOM 9610 C THR H 333 55.973 40.347 −16.606 1.00 55.98 C ATOM 9611 O THR H 333 55.989 39.265 −16.015 1.00 55.70 O ATOM 9612 CB THR H 333 56.610 42.576 −15.667 1.00 56.00 C ATOM 9613 OG1 THR H 333 57.707 41.887 −15.053 1.00 55.64 O ATOM 9614 CG2 THR H 333 56.171 43.716 −14.757 1.00 56.17 C ATOM 9615 N PHE H 334 56.402 40.489 −17.856 1.00 55.64 N ATOM 9616 CA PHE H 334 56.943 39.354 −18.595 1.00 55.14 C ATOM 9617 C PHE H 334 58.255 38.924 −17.935 1.00 54.70 C ATOM 9618 O PHE H 334 58.697 37.778 −18.072 1.00 54.50 O ATOM 9619 CB PHE H 334 57.188 39.744 −20.059 1.00 54.92 C ATOM 9620 N GLU H 335 58.867 39.853 −17.209 1.00 53.71 N ATOM 9621 CA GLU H 335 60.128 39.585 −16.529 1.00 53.18 C ATOM 9622 C GLU H 335 59.956 38.597 −15.372 1.00 52.08 C ATOM 9623 O GLU H 335 60.894 37.889 −15.010 1.00 51.65 O ATOM 9624 CB GLU H 335 60.734 40.896 −16.009 1.00 52.71 C ATOM 9625 N ASP H 336 58.753 38.550 −14.802 1.00 50.89 N ATOM 9626 CA ASP H 336 58.477 37.653 −13.685 1.00 49.91 C ATOM 9627 C ASP H 336 58.419 36.179 −14.084 1.00 49.25 C ATOM 9628 O ASP H 336 58.576 35.301 −13.238 1.00 48.81 O ATOM 9629 CB ASP H 336 57.177 38.060 −12.991 1.00 49.37 C ATOM 9630 CG ASP H 336 57.285 39.410 −12.313 1.00 49.80 C ATOM 9631 OD1 ASP H 336 58.295 39.634 −11.609 1.00 50.47 O ATOM 9632 OD2 ASP H 336 56.364 40.243 −12.470 1.00 49.20 O ATOM 9633 N ALA H 337 58.197 35.913 −15.369 1.00 48.17 N ATOM 9634 CA ALA H 337 58.143 34.539 −15.865 1.00 47.58 C ATOM 9635 C ALA H 337 59.401 33.780 −15.447 1.00 46.88 C ATOM 9636 O ALA H 337 60.477 34.365 −15.339 1.00 46.85 O ATOM 9637 CB ALA H 337 58.025 34.533 −17.390 1.00 47.07 C ATOM 9638 N GLY H 338 59.268 32.479 −15.216 1.00 45.84 N ATOM 9639 CA GLY H 338 60.428 31.694 −14.837 1.00 44.74 C ATOM 9640 C GLY H 338 60.166 30.625 −13.791 1.00 44.03 C ATOM 9641 O GLY H 338 59.018 30.370 −13.408 1.00 43.61 O ATOM 9642 N GLU H 339 61.245 30.004 −13.323 1.00 42.77 N ATOM 9643 CA GLU H 339 61.152 28.942 −12.324 1.00 42.35 C ATOM 9644 C GLU H 339 61.277 29.461 −10.895 1.00 40.94 C ATOM 9645 O GLU H 339 62.246 30.136 −10.558 1.00 40.42 O ATOM 9646 CB GLU H 339 62.233 27.880 −12.572 1.00 42.79 C ATOM 9647 CG GLU H 339 62.137 26.664 −11.645 1.00 44.52 C ATOM 9648 CD GLU H 339 63.097 25.539 −12.030 1.00 46.13 C ATOM 9649 OE1 GLU H 339 64.315 25.798 −12.120 1.00 47.18 O ATOM 9650 OE2 GLU H 339 62.636 24.394 −12.237 1.00 46.84 O ATOM 9651 N TYR H 340 60.280 29.146 −10.072 1.00 39.59 N ATOM 9652 CA TYR H 340 60.259 29.531 −8.664 1.00 38.28 C ATOM 9653 C TYR H 340 60.448 28.290 −7.784 1.00 37.55 C ATOM 9654 O TYR H 340 59.855 27.229 −8.034 1.00 37.22 O ATOM 9655 CB TYR H 340 58.940 30.212 −8.305 1.00 38.61 C ATOM 9656 CG TYR H 340 58.797 31.603 −8.884 1.00 39.74 C ATOM 9657 CD1 TYR H 340 58.677 31.799 −10.262 1.00 39.98 C ATOM 9658 CD2 TYR H 340 58.775 32.724 −8.054 1.00 39.49 C ATOM 9659 CE1 TYR H 340 58.536 33.077 −10.800 1.00 40.79 C ATOM 9660 CE2 TYR H 340 58.637 34.002 −8.578 1.00 40.34 C ATOM 9661 CZ TYR H 340 58.517 34.176 −9.952 1.00 41.35 C ATOM 9662 OH TYR H 340 58.382 35.445 −10.475 1.00 42.00 O ATOM 9663 N THR H 341 61.266 28.425 −6.748 1.00 35.65 N ATOM 9664 CA THR H 341 61.536 27.301 −5.872 1.00 34.71 C ATOM 9665 C THR H 341 61.341 27.567 −4.387 1.00 34.35 C ATOM 9666 O THR H 341 61.777 28.592 −3.864 1.00 33.93 O ATOM 9667 CB THR H 341 62.985 26.800 −6.053 1.00 33.92 C ATOM 9668 OG1 THR H 341 63.166 26.323 −7.388 1.00 34.09 O ATOM 9669 CG2 THR H 341 63.306 25.687 −5.053 1.00 33.25 C ATOM 9670 N CYS H 342 60.667 26.638 −3.720 1.00 33.12 N ATOM 9671 CA CYS H 342 60.506 26.724 −2.278 1.00 33.28 C ATOM 9672 C CYS H 342 61.601 25.807 −1.741 1.00 32.46 C ATOM 9673 O CYS H 342 61.624 24.608 −2.048 1.00 32.40 O ATOM 9674 CB CYS H 342 59.148 26.204 −1.818 1.00 33.42 C ATOM 9675 SG CYS H 342 59.108 26.023 −0.019 1.00 36.87 S ATOM 9676 N LEU H 343 62.514 26.366 −0.958 1.00 31.35 N ATOM 9677 CA LEU H 343 63.617 25.586 −0.408 1.00 30.39 C ATOM 9678 C LEU H 343 63.578 25.559 1.117 1.00 29.88 C ATOM 9679 O LEU H 343 63.520 26.605 1.768 1.00 29.41 O ATOM 9680 CB LEU H 343 64.946 26.166 −0.890 1.00 31.72 C ATOM 9681 CG LEU H 343 66.223 25.422 −0.480 1.00 33.14 C ATOM 9682 CD1 LEU H 343 67.337 25.785 −1.432 1.00 34.29 C ATOM 9683 CD2 LEU H 343 66.600 25.767 0.962 1.00 34.27 C ATOM 9684 N ALA H 344 63.606 24.351 1.678 1.00 28.52 N ATOM 9685 CA ALA H 344 63.565 24.152 3.119 1.00 28.66 C ATOM 9686 C ALA H 344 64.776 23.376 3.607 1.00 28.75 C ATOM 9687 O ALA H 344 65.087 22.298 3.091 1.00 28.52 O ATOM 9688 CB ALA H 344 62.290 23.402 3.519 1.00 26.24 C ATOM 9689 N GLY H 345 65.451 23.917 4.616 1.00 28.93 N ATOM 9690 CA GLY H 345 66.605 23.230 5.158 1.00 28.63 C ATOM 9691 C GLY H 345 66.671 23.246 6.672 1.00 28.33 C ATOM 9692 O GLY H 345 66.179 24.181 7.305 1.00 27.94 O ATOM 9693 N ASN H 346 67.244 22.183 7.238 1.00 28.29 N ATOM 9694 CA ASN H 346 67.470 22.061 8.677 1.00 29.80 C ATOM 9695 C ASN H 346 68.912 21.547 8.843 1.00 30.24 C ATOM 9696 O ASN H 346 69.619 21.360 7.849 1.00 28.99 O ATOM 9697 CB ASN H 346 66.455 21.099 9.340 1.00 29.39 C ATOM 9698 CG ASN H 346 66.493 19.675 8.768 1.00 31.32 C ATOM 9699 OD1 ASN H 346 67.527 19.196 8.307 1.00 30.86 O ATOM 9700 ND2 ASN H 346 65.354 18.985 8.829 1.00 32.58 N ATOM 9701 N SER H 347 69.339 21.323 10.084 1.00 32.25 N ATOM 9702 CA SER H 347 70.694 20.839 10.374 1.00 33.21 C ATOM 9703 C SER H 347 71.072 19.546 9.641 1.00 33.84 C ATOM 9704 O SER H 347 72.235 19.323 9.328 1.00 34.09 O ATOM 9705 CB SER H 347 70.844 20.629 11.887 1.00 34.51 C ATOM 9706 OG SER H 347 69.870 19.718 12.394 1.00 34.95 O ATOM 9707 N ILE H 348 70.084 18.699 9.367 1.00 34.13 N ATOM 9708 CA ILE H 348 70.318 17.434 8.686 1.00 33.98 C ATOM 9709 C ILE H 348 70.498 17.551 7.167 1.00 34.47 C ATOM 9710 O ILE H 348 71.387 16.911 6.591 1.00 34.96 O ATOM 9711 CB ILE H 348 69.168 16.454 9.014 1.00 34.31 C ATOM 9712 CG1 ILE H 348 69.134 16.207 10.525 1.00 33.70 C ATOM 9713 CG2 ILE H 348 69.363 15.145 8.273 1.00 35.12 C ATOM 9714 CD1 ILE H 348 67.761 15.971 11.081 1.00 35.74 C ATOM 9715 N GLY H 349 69.667 18.364 6.520 1.00 34.17 N ATOM 9716 CA GLY H 349 69.769 18.514 5.081 1.00 33.60 C ATOM 9717 C GLY H 349 68.802 19.506 4.452 1.00 34.04 C ATOM 9718 O GLY H 349 68.050 20.191 5.147 1.00 33.36 O ATOM 9719 N ILE H 350 68.813 19.540 3.119 1.00 34.41 N ATOM 9720 CA ILE H 350 68.006 20.452 2.308 1.00 34.58 C ATOM 9721 C ILE H 350 67.033 19.750 1.354 1.00 35.06 C ATOM 9722 O ILE H 350 67.360 18.715 0.780 1.00 35.43 O ATOM 9723 CB ILE H 350 68.947 21.326 1.442 1.00 34.97 C ATOM 9724 CG1 ILE H 350 69.814 22.211 2.342 1.00 35.77 C ATOM 9725 CG2 ILE H 350 68.148 22.131 0.424 1.00 34.94 C ATOM 9726 CD1 ILE H 350 70.890 23.018 1.587 1.00 36.05 C ATOM 9727 N SER H 351 65.850 20.336 1.180 1.00 34.68 N ATOM 9728 CA SER H 351 64.824 19.816 0.269 1.00 33.71 C ATOM 9729 C SER H 351 64.217 21.007 −0.467 1.00 33.16 C ATOM 9730 O SER H 351 64.169 22.107 0.087 1.00 32.26 O ATOM 9731 CB SER H 351 63.719 19.081 1.046 1.00 33.92 C ATOM 9732 OG SER H 351 64.195 17.873 1.612 1.00 33.92 O ATOM 9733 N PHE H 352 63.762 20.796 −1.703 1.00 32.29 N ATOM 9734 CA PHE H 352 63.168 21.878 −2.483 1.00 32.43 C ATOM 9735 C PHE H 352 62.276 21.395 −3.633 1.00 32.72 C ATOM 9736 O PHE H 352 62.574 20.387 −4.281 1.00 31.63 O ATOM 9737 CB PHE H 352 64.277 22.793 −3.031 1.00 33.11 C ATOM 9738 CG PHE H 352 65.161 22.141 −4.067 1.00 34.50 C ATOM 9739 CD1 PHE H 352 64.707 21.946 −5.376 1.00 35.60 C ATOM 9740 CD2 PHE H 352 66.445 21.710 −3.735 1.00 35.05 C ATOM 9741 CE1 PHE H 352 65.517 21.330 −6.341 1.00 35.94 C ATOM 9742 CE2 PHE H 352 67.267 21.090 −4.690 1.00 35.60 C ATOM 9743 CZ PHE H 352 66.804 20.900 −5.992 1.00 35.75 C ATOM 9744 N HIS H 353 61.183 22.124 −3.870 1.00 32.24 N ATOM 9745 CA HIS H 353 60.230 21.828 −4.947 1.00 32.60 C ATOM 9746 C HIS H 353 60.123 23.081 −5.818 1.00 33.51 C ATOM 9747 O HIS H 353 60.099 24.204 −5.297 1.00 33.35 O ATOM 9748 CB HIS H 353 58.831 21.511 −4.398 1.00 30.97 C ATOM 9749 CG HIS H 353 58.667 20.116 −3.881 1.00 29.85 C ATOM 9750 ND1 HIS H 353 57.445 19.623 −3.469 1.00 28.49 N ATOM 9751 CD2 HIS H 353 59.563 19.121 −3.673 1.00 30.21 C ATOM 9752 CE1 HIS H 353 57.597 18.387 −3.028 1.00 28.83 C ATOM 9753 NE2 HIS H 353 58.872 18.056 −3.139 1.00 27.96 N ATOM 9754 N SER H 354 60.033 22.892 −7.133 1.00 33.84 N ATOM 9755 CA SER H 354 59.951 24.011 −8.064 1.00 34.71 C ATOM 9756 C SER H 354 58.698 24.018 −8.927 1.00 35.83 C ATOM 9757 O SER H 354 58.082 22.982 −9.173 1.00 36.45 O ATOM 9758 CB SER H 354 61.177 24.014 −8.979 1.00 33.91 C ATOM 9759 OG SER H 354 62.365 24.081 −8.222 1.00 32.77 O ATOM 9760 N ALA H 355 58.333 25.205 −9.387 1.00 36.67 N ATOM 9761 CA ALA H 355 57.164 25.382 −10.236 1.00 38.27 C ATOM 9762 C ALA H 355 57.507 26.462 −11.256 1.00 39.56 C ATOM 9763 O ALA H 355 58.456 27.231 −11.068 1.00 38.77 O ATOM 9764 CB ALA H 355 55.963 25.804 −9.398 1.00 36.50 C ATOM 9765 N TRP H 356 56.741 26.518 −12.335 1.00 41.08 N ATOM 9766 CA TRP H 356 56.986 27.507 −13.370 1.00 43.37 C ATOM 9767 C TRP H 356 55.856 28.520 −13.500 1.00 43.51 C ATOM 9768 O TRP H 356 54.678 28.181 −13.360 1.00 42.74 O ATOM 9769 CB TRP H 356 57.195 26.809 −14.713 1.00 46.21 C ATOM 9770 CG TRP H 356 58.585 26.940 −15.259 1.00 49.86 C ATOM 9771 CD1 TRP H 356 59.119 28.023 −15.910 1.00 51.19 C ATOM 9772 CD2 TRP H 356 59.622 25.955 −15.199 1.00 51.39 C ATOM 9773 NE1 TRP H 356 60.428 27.770 −16.259 1.00 52.44 N ATOM 9774 CE2 TRP H 356 60.761 26.508 −15.834 1.00 52.70 C ATOM 9775 CE3 TRP H 356 59.700 24.659 −14.670 1.00 52.30 C ATOM 9776 CZ2 TRP H 356 61.967 25.805 −15.956 1.00 53.75 C ATOM 9777 CZ3 TRP H 356 60.899 23.957 −14.790 1.00 53.65 C ATOM 9778 CH2 TRP H 356 62.016 24.533 −15.430 1.00 54.68 C ATOM 9779 N LEU H 357 56.228 29.771 −13.749 1.00 43.57 N ATOM 9780 CA LEU H 357 55.241 30.821 −13.948 1.00 44.37 C ATOM 9781 C LEU H 357 55.264 31.210 −15.419 1.00 44.97 C ATOM 9782 O LEU H 357 56.306 31.606 −15.943 1.00 44.95 O ATOM 9783 CB LEU H 357 55.553 32.063 −13.102 1.00 43.75 C ATOM 9784 CG LEU H 357 54.647 33.275 −13.395 1.00 43.33 C ATOM 9785 CD1 LEU H 357 53.199 32.930 −13.065 1.00 42.94 C ATOM 9786 CD2 LEU H 357 55.097 34.483 −12.592 1.00 42.64 C ATOM 9787 N THR H 358 54.125 31.072 −16.088 1.00 46.14 N ATOM 9788 CA THR H 358 54.021 31.455 −17.494 1.00 47.09 C ATOM 9789 C THR H 358 53.217 32.748 −17.602 1.00 47.54 C ATOM 9790 O THR H 358 52.111 32.851 −17.070 1.00 47.65 O ATOM 9791 CB THR H 358 53.347 30.355 −18.357 1.00 47.36 C ATOM 9792 OG1 THR H 358 54.224 29.223 −18.454 1.00 46.99 O ATOM 9793 CG2 THR H 358 53.059 30.880 −19.769 1.00 47.09 C ATOM 9794 N VAL H 359 53.798 33.739 −18.273 1.00 48.63 N ATOM 9795 CA VAL H 359 53.150 35.035 −18.462 1.00 50.08 C ATOM 9796 C VAL H 359 52.862 35.241 −19.946 1.00 51.19 C ATOM 9797 O VAL H 359 53.779 35.297 −20.764 1.00 50.62 O ATOM 9798 CB VAL H 359 54.040 36.198 −17.960 1.00 49.65 C ATOM 9799 N LEU H 360 51.576 35.351 −20.280 1.00 52.47 N ATOM 9800 CA LEU H 360 51.122 35.539 −21.659 1.00 53.75 C ATOM 9801 C LEU H 360 50.855 37.013 −21.990 1.00 54.89 C ATOM 9802 O LEU H 360 50.672 37.836 −21.086 1.00 54.42 O ATOM 9803 CB LEU H 360 49.859 34.711 −21.882 1.00 52.68 C ATOM 9804 CG LEU H 360 50.030 33.232 −21.527 1.00 52.35 C ATOM 9805 CD1 LEU H 360 48.682 32.530 −21.579 1.00 51.71 C ATOM 9806 CD2 LEU H 360 51.018 32.582 −22.494 1.00 51.91 C ATOM 9807 N PRO H 361 50.829 37.360 −23.292 1.00 56.57 N ATOM 9808 CA PRO H 361 50.587 38.734 −23.759 1.00 57.88 C ATOM 9809 C PRO H 361 49.152 39.223 −23.536 1.00 59.14 C ATOM 9810 O PRO H 361 48.215 38.421 −23.432 1.00 58.75 O ATOM 9811 CB PRO H 361 50.945 38.653 −25.241 1.00 57.63 C ATOM 9812 CG PRO H 361 50.519 37.252 −25.605 1.00 57.72 C ATOM 9813 CD PRO H 361 51.068 36.459 −24.436 1.00 56.77 C ATOM 9814 N ALA H 362 48.988 40.540 −23.458 1.00 60.86 N ATOM 9815 CA ALA H 362 47.671 41.137 −23.245 1.00 62.45 C ATOM 9816 C ALA H 362 47.003 41.386 −24.592 1.00 63.55 C ATOM 9817 O ALA H 362 47.664 41.329 −25.630 1.00 63.78 O ATOM 9818 CB ALA H 362 47.810 42.457 −22.470 1.00 62.08 C ATOM 9819 N PRO H 363 45.687 41.657 −24.605 1.00 64.64 N ATOM 9820 CA PRO H 363 44.919 41.923 −25.837 1.00 65.06 C ATOM 9821 C PRO H 363 44.966 43.393 −26.248 1.00 65.26 C ATOM 9822 O PRO H 363 45.828 43.746 −27.072 1.00 65.96 O ATOM 9823 CB PRO H 363 43.491 41.523 −25.462 1.00 65.00 C ATOM 9824 CG PRO H 363 43.656 40.661 −24.196 1.00 65.12 C ATOM 9825 CD PRO H 363 44.777 41.349 −23.490 1.00 64.84 C HETATM 9927 S SO4 9001 46.360 43.651 14.525 1.00 80.11 S HETATM 9828 O1 SO4 9001 45.130 42.976 14.081 1.00 80.85 O HETATM 9829 O2 SO4 9001 46.043 45.024 14.953 1.00 79.61 O HETATM 9830 O3 SO4 9001 46.944 42.914 15.659 1.00 80.93 O HETATM 9831 O4 SO4 9001 47.320 43.674 13.407 1.00 79.94 O HETATM 9832 S SO4 9002 39.893 32.643 −36.234 1.00 57.87 S NETATM 9833 O1 SO4 9002 40.848 33.615 −36.811 1.00 58.67 O HETATM 9834 O2 SO4 9002 40.300 31.273 −36.580 1.00 58.27 O HETATM 9835 O3 SO4 9002 39.894 32.781 −34.766 1.00 57.83 O HETATM 9836 O4 SO4 9002 38.548 32.894 −36.778 1.00 57.44 O HETATM 9837 S SO4 9003 76.012 20.398 36.658 1.00 64.33 S HETATM 9838 O1 SO4 9003 76.273 20.228 35.214 1.00 64.38 O HETATM 9839 O2 SO4 9003 76.984 19.588 37.421 1.00 65.03 O HETATM 9840 O3 SO4 9003 76.155 21.819 37.013 1.00 64.70 O HETATM 9841 O4 SO4 9003 74.644 19.964 36.986 1.00 63.96 O HETATM 9842 S SO4 9004 82.383 9.280 −14.072 1.00 88.97 S HETATM 9843 O1 SO4 9004 82.503 10.218 −15.201 1.00 89.47 O HETATM 9844 O2 SO4 9004 83.325 8.161 −14.260 1.00 88.96 O HETATM 9845 O3 SO4 9004 82.686 9.986 −12.808 1.00 88.61 O HETATM 9846 O4 SO4 9004 81.009 8.751 −14.037 1.00 89.30 O HETATM 9847 O HOH 8001 30.583 19.182 −20.544 1.00 21.98 O HETATM 9848 O HOH 8002 76.423 −6.864 9.843 1.00 23.00 O HETATM 9849 O HOH 8003 19.265 31.410 1.209 1.00 22.84 O HETATM 9850 O HOH 8004 61.744 −4.031 28.962 1.00 22.37 O HETATM 9851 O HOH 8005 66.826 33.841 20.938 1.00 23.18 O HETATM 9852 O HOH 8006 18.482 37.390 8.210 1.00 23.45 O HETATM 9853 O HOH 8007 54.625 15.653 −7.780 1.00 22.48 O HETATM 9854 O HOH 8008 59.923 9.805 49.344 1.00 26.25 O HETATM 9855 O HOH 8009 72.094 23.144 24.607 1.00 19.78 O HETATM 9856 O HOH 8010 14.982 26.494 6.291 1.00 21.68 O HETATM 9857 O HOH 8011 40.246 59.911 −9.530 1.00 24.78 O HETATM 9858 O HOH 8012 15.805 46.501 5.661 1.00 29.73 O HETATM 9859 O HOH 8013 55.380 21.613 −0.817 1.00 23.35 O HETATM 9860 O HOH 8014 16.573 46.338 9.812 1.00 24.34 O HETATM 9861 O HOH 8015 51.751 6.536 −5.223 1.00 27.38 O HETATM 9862 O HOH 8016 36.033 29.962 −24.110 1.00 23.25 O HETATM 9863 O HOH 8017 25.606 57.088 −28.459 1.00 22.89 O HETATM 9864 O HOH 8018 73.859 −2.056 4.603 1.00 19.45 O HETATM 9865 O HOH 8019 51.125 26.594 −5.604 1.00 24.70 O HETATM 9866 O HOH 8020 66.880 25.381 9.858 1.00 28.68 O HETATM 9867 O HOH 8021 38.023 25.055 −28.614 1.00 22.96 O HETATM 9868 O HOH 8022 26.996 30.474 −16.396 1.00 23.98 O HETATM 9869 O HOH 8023 25.809 19.877 −17.801 1.00 24.38 O HETATM 9870 O HOH 8024 45.339 47.075 −3.217 1.00 24.47 O HETATM 9871 O HOH 8025 58.457 26.484 18.703 1.00 28.38 O HETATM 9872 O HOH 8026 37.737 55.122 −4.166 1.00 21.76 O HETATM 9873 O HOH 8027 62.668 37.972 3.726 1.00 37.90 O HETATM 9874 O HOH 8028 76.437 −7.756 13.648 1.00 21.50 O HETATM 9875 O HOH 8029 52.710 6.639 −9.379 1.00 25.02 O HETATM 9876 O HOH 8030 81.344 5.935 3.580 1.00 25.92 O HETATM 9877 O HOH 8031 23.909 43.293 −49.084 1.00 22.88 O HETATM 9878 O HOH 8032 24.078 33.069 8.400 1.00 30.55 O HETATM 9879 O HOH 8033 49.020 60.054 −0.925 1.00 30.74 O HETATM 9880 O HOH 8034 74.099 28.029 29.070 1.00 28.15 O HETATM 9881 O HOH 8035 65.801 0.287 24.875 1.00 34.23 O HETATM 9882 O HOH 8036 58.785 1.057 −24.404 1.00 24.39 O HETATM 9883 O HOH 8037 28.568 14.884 −9.616 1.00 34.53 O HETATM 9884 O HOH 8038 54.116 2.380 −18.860 1.00 29.41 O HETATM 9885 O HOH 8039 30.881 27.679 −9.394 1.00 27.68 O HETATM 9886 O HOH 8040 65.552 4.439 59.031 1.00 25.86 O HETATM 9887 O HOH 8041 65.513 10.326 −17.439 1.00 30.59 O HETATM 9888 O HOH 8042 17.929 50.681 19.191 1.00 28.19 O HETATM 9889 O HOH 8043 68.778 6.931 16.604 1.00 39.86 O HETATM 9890 O HOH 8044 67.164 12.773 5.516 1.00 33.07 O HETATM 9891 O HOH 8045 55.249 8.894 45.955 1.00 29.25 O HETATM 9892 O HOH 8046 22.665 51.933 24.883 1.00 28.14 O HETATM 9893 O HOH 8047 37.888 61.108 −2.570 1.00 31.13 O HETATM 9894 O HOH 8048 49.282 61.990 −14.155 1.00 36.20 O HETATM 9895 O HOH 8049 79.384 −12.820 −6.839 1.00 37.30 O HETATM 9896 O HOH 8050 26.570 15.111 −3.236 1.00 37.60 O HETATM 9897 O HOH 8051 19.038 44.180 −45.467 1.00 26.94 O HETATM 9898 O HOH 8052 60.388 25.333 28.267 1.00 27.06 O HETATM 9899 O HOH 8053 23.414 15.233 9.873 1.00 34.15 O HETATM 9900 O HOH 8054 66.392 27.654 3.426 1.00 31.42 O HETATM 9901 O HOH 8055 62.016 33.264 18.060 1.00 33.13 O HETATM 9902 O HOH 8056 43.462 65.933 7.208 1.00 44.73 O HETATM 9903 O HOH 8057 69.239 2.254 10.867 1.00 38.73 O HETATM 9904 O HOH 8058 14.577 44.517 4.008 1.00 33.29 O HETATM 9905 O HOH 8059 85.110 −7.051 1.368 1.00 35.88 O HETATM 9906 O HOH 8060 45.130 48.451 2.474 1.00 30.78 O HETATM 9907 O HOH 8061 63.059 22.563 16.774 1.00 23.95 O HETATM 9908 O HOH 8062 73.904 −8.163 3.078 1.00 36.65 O HETATM 9909 O HOH 8063 53.387 0.804 26.358 1.00 32.68 O HETATM 9910 O HOH 8064 13.296 34.466 4.116 1.00 29.56 O HETATM 9911 O HOH 8065 29.710 52.865 −24.449 1.00 30.83 O HETATM 9912 O HOH 8066 67.684 22.717 12.581 1.00 28.39 O HETATM 9913 O HOH 8067 18.064 52.076 −30.370 1.00 32.76 O HETATM 9914 O HOH 8068 85.007 −9.066 15.009 1.00 43.17 O HETATM 9915 O HOH 8069 15.569 35.041 9.972 1.00 31.63 O HETATM 9916 O HOH 8070 17.191 52.234 −25.947 1.00 35.07 O HETATM 9917 O HOH 8071 30.314 25.533 −3.007 1.00 32.66 O HETATM 9918 O HOH 8072 47.442 66.967 −17.665 1.00 31.12 O HETATM 9919 O HOH 8073 34.258 51.896 −24.228 1.00 34.62 O HETATM 9920 O HOH 8074 66.403 −0.525 21.596 1.00 30.11 O HETATM 9921 O HOH 8075 17.325 49.223 0.994 1.00 37.88 O HETATM 9922 O HOH 8076 59.434 37.817 −9.613 1.00 27.94 O HETATM 9923 O HOH 8077 27.027 41.793 38.232 1.00 37.52 O HETATM 9924 O HOH 8078 40.302 60.801 −13.194 1.00 22.94 O HETATM 9925 O HOH 8079 81.263 −10.005 4.030 1.00 29.81 O HETATM 9926 O HOH 8080 27.556 33.013 −16.634 1.00 31.61 O HETATM 9927 O HOH 8081 53.479 3.973 −0.763 1.00 40.24 O HETATM 9928 O HOH 8082 29.612 42.889 17.699 1.00 34.12 O HETATM 9929 O HOH 8083 31.582 30.335 −12.062 1.00 31.47 O HETATM 9930 O HOH 8084 69.184 6.616 −7.967 1.00 37.68 O HETATM 9931 O HOH 8085 56.292 20.021 11.107 1.00 29.89 O HETATM 9932 O HOH 8086 25.472 24.891 −11.314 1.00 30.53 O HETATM 9933 O HOH 8087 81.124 4.621 −1.975 1.00 28.02 O HETATM 9934 O HOH 8088 78.096 −1.640 12.197 1.00 29.00 O HETATM 9935 O HOH 8089 13.865 47.316 7.506 1.00 32.89 O HETATM 9936 O HOH 8090 61.310 28.601 8.211 1.00 24.59 O HETATM 9937 O HOH 8091 17.421 23.402 −6.076 1.00 34.31 O HETATM 9938 O HOH 8092 57.812 10.445 0.414 1.00 28.37 O HETATM 9939 O HOH 8093 58.384 32.757 14.907 1.00 33.51 O HETATM 9940 O HOH 8094 24.207 27.604 −27.914 1.00 28.18 O HETATM 9941 O HOH 8095 63.100 11.384 −37.852 1.00 39.50 O HETATM 9942 O HOH 8096 71.145 17.722 1.891 1.00 42.96 O HETATM 9943 O HOH 8097 29.409 48.671 −58.806 1.00 28.48 O HETATM 9944 O HOH 8098 26.815 49.289 28.620 1.00 27.67 O HETATM 9945 O HOH 8099 63.739 20.042 17.105 1.00 29.92 O HETATM 9946 O HOH 8100 16.197 48.146 −40.012 1.00 36.11 O HETATM 9947 O HOH 8101 28.797 19.484 −13.783 1.00 30.27 O HETATM 9948 O HOH 8102 74.942 −5.515 −6.685 1.00 32.65 O HETATM 9949 O HOH 8103 25.351 24.480 −7.993 1.00 26.19 O HETATM 9950 O HOH 8104 74.186 34.192 19.566 1.00 29.84 O HETATM 9951 O HOH 8105 83.633 −13.959 18.198 1.00 32.48 O HETATM 9952 O HOH 8106 52.144 19.807 −15.029 1.00 47.82 O HETATM 9953 O HOH 8107 79.030 −3.693 18.591 1.00 37.03 O HETATM 9954 O HOH 8108 15.025 52.871 −28.124 1.00 35.88 O HETATM 9955 O HOH 8109 55.203 14.515 1.204 1.00 26.74 O HETATM 9956 O HOH 8110 50.909 12.754 −20.344 1.00 35.29 O HETATM 9957 O HOH 8111 48.196 16.287 −16.372 1.00 36.40 O HETATM 9958 O HOH 8112 45.057 63.127 −3.521 1.00 28.95 O HETATM 9959 O HOH 8113 66.876 9.858 −36.882 1.00 29.60 O HETATM 9960 O HOH 8114 51.733 17.941 −9.585 1.00 32.25 O HETATM 9961 O HOH 8115 14.959 24.873 8.383 1.00 31.68 O HETATM 9962 O HOH 8116 54.406 3.719 51.786 1.00 34.52 O HETATM 9963 O HOH 8117 47.786 29.136 −13.190 1.00 43.19 O HETATM 9964 O HOH 8118 16.528 42.222 4.279 1.00 29.03 O HETATM 9965 O HOH 8119 22.165 20.253 −14.491 1.00 32.49 O HETATM 9966 O HOH 8120 38.018 18.783 −19.030 1.00 29.87 O HETATM 9967 O HOH 8121 12.676 52.034 13.008 1.00 33.57 O HETATM 9968 O HOH 8122 30.241 53.649 −21.241 1.00 31.91 O HETATM 9969 O HOH 8123 40.855 50.843 −9.251 1.00 36.33 O HETATM 9970 O HOH 8124 16.414 33.295 15.556 1.00 39.62 O HETATM 9971 O HOH 8125 18.353 48.759 30.683 1.00 35.44 O HETATM 9972 O HOH 8126 27.919 64.251 −31.560 1.00 39.39 O HETATM 9973 O HOH 8127 54.074 11.927 −1.836 1.00 20.42 O HETATM 9974 O HOH 8128 67.489 10.620 −5.827 1.00 24.90 O HETATM 9975 O HOH 8129 56.468 32.717 −20.169 1.00 34.22 O HETATM 9976 O HOH 8130 37.565 9.799 −16.847 1.00 39.96 O HETATM 9977 O HOH 8131 76.829 1.988 9.827 1.00 41.86 O HETATM 9978 O HOH 8132 43.003 56.760 −18.029 1.00 32.10 O HETATM 9979 O HOH 8133 33.394 50.852 −10.344 1.00 45.63 O HETATM 9980 O HOH 8134 57.923 33.762 28.761 1.00 35.78 O HETATM 9981 O HOH 8135 63.084 −8.959 36.290 1.00 42.92 O HETATM 9982 O HOH 8136 21.708 42.750 0.109 1.00 32.64 O HETATM 9983 O HOH 8137 48.251 −2.260 29.824 1.00 47.66 O HETATM 9984 O HOH 8138 64.982 33.645 14.162 1.00 32.84 O HETATM 9985 O HOH 8139 37.774 30.276 −18.377 1.00 25.37 O HETATM 9986 O HOH 8140 20.175 20.176 20.621 1.00 40.03 O HETATM 9987 O HOH 8141 15.210 32.340 9.751 1.00 30.63 O HETATM 9988 O HOH 8142 53.556 29.620 6.545 1.00 35.87 O HETATM 9989 O HOH 8143 52.402 5.039 40.375 1.00 36.45 O HETATM 9990 O HOH 8144 41.944 54.575 −11.736 1.00 25.88 O HETATM 9991 O HOH 8145 14.808 40.343 20.475 1.00 36.26 O HETATM 9992 O HOH 8146 36.235 53.078 −4.162 1.00 24.78 O HETATM 9993 O HOH 8147 51.322 20.699 −9.253 1.00 34.49 O HETATM 9994 O HOH 8148 44.258 30.807 −17.555 1.00 46.92 O HETATM 9995 O HOH 8149 11.904 21.107 9.147 1.00 41.29 O HETATM 9996 O HOH 8150 72.373 −0.009 4.822 1.00 28.51 O HETATM 9997 O HOH 8151 20.170 33.123 −10.615 1.00 28.26 O HETATM 9998 O HOH 8152 60.563 −6.573 58.339 1.00 43.96 O HETATM 9999 O HOH 8153 57.895 28.648 13.774 1.00 30.15 O HETATM 10000 O HON 8154 53.947 23.638 7.544 1.00 41.95 O HETATM 10001 O HOH 8155 13.166 53.396 −31.308 1.00 44.46 O HETATM 10002 O HOH 8156 38.690 58.693 7.177 1.00 27.24 O HETATM 10003 O HOH 8157 51.253 0.008 28.416 1.00 35.72 O HETATM 10004 O HOH 8158 18.004 41.137 2.217 1.00 20.61 O HETATM 10005 O HOH 8159 54.755 37.212 −0.604 1.00 29.83 O HETATM 10006 O HOH 8160 18.580 15.949 0.946 1.00 34.15 O HETATM 10007 O HOH 8161 57.339 −4.703 41.534 1.00 33.68 O HETATM 10008 O HOH 8162 68.790 10.518 33.158 1.00 44.07 O HETATM 10009 O HOH 8163 48.266 4.423 −10.271 1.00 23.22 O HETATM 10010 O HOH 8164 32.688 42.614 −32.515 1.00 43.90 O HETATM 10011 O HOH 8165 64.899 38.193 10.025 1.00 34.17 O HETATM 10012 O HOH 8166 19.100 38.573 −0.767 1.00 25.16 O HETATM 10013 O HOH 8167 64.226 8.781 −37.188 1.00 26.93 O HETATM 10014 O HOH 8168 29.180 37.941 4.587 1.00 30.90 O HETATM 10015 O HOH 8169 63.251 7.981 −34.694 1.00 20.84 O HETATM 10016 O HOH 8170 32.539 48.870 −25.937 1.00 40.48 O HETATM 10017 O HOH 8171 55.576 29.806 14.321 1.00 25.66 O HETATM 10018 O HOH 8172 21.748 19.472 −28.189 1.00 30.89 O HETATM 10019 O HOH 8173 48.653 0.885 −12.564 1.00 33.10 O HETATM 10020 O HOH 8174 50.731 8.561 −3.840 1.00 26.40 O HETATM 10021 O HOH 8175 67.331 8.027 58.226 1.00 26.20 O HETATM 10022 O HOH 8176 64.354 3.045 −26.220 1.00 32.54 O HETATM 10023 O HOH 8177 39.113 62.755 −7.021 1.00 27.10 O HETATM 10024 O HOH 8178 46.583 45.195 −4.701 1.00 30.19 O HETATM 10025 O HOH 8179 31.224 45.086 −57.745 1.00 26.44 O HETATM 10026 O HOH 8180 67.620 7.867 −17.944 1.00 33.64 O HETATM 10027 O HOH 8181 68.440 4.360 25.981 1.00 38.96 O HETATM 10028 O HOH 8182 24.285 56.988 −21.046 1.00 34.78 O HETATM 10029 O HOH 8183 60.110 20.079 −7.760 1.00 31.63 O HETATM 10030 O HOH 8184 21.199 57.796 −41.110 1.00 37.92 O HETATM 10031 O HOH 8185 59.503 24.146 17.040 1.00 28.08 O HETATM 10032 O HOH 8186 60.538 −3.909 21.754 1.00 33.98 O HETATM 10033 O HOH 8187 50.010 5.646 −7.056 1.00 28.66 O HETATM 10034 O HOH 8188 86.579 2.282 −6.040 1.00 38.85 O HETATM 10035 O HOH 8189 35.299 34.821 −1.319 1.00 36.49 O HETATM 10036 O HOH 8190 83.307 −8.029 7.975 1.00 29.74 O HETATM 10037 O HOH 8191 44.187 65.659 −4.506 1.00 31.35 O HETATM 10038 O HOH 8192 30.932 40.093 −5.050 1.00 33.10 O HETATM 10039 O HOH 8193 56.018 31.976 28.056 1.00 33.87 O HETATM 10040 O HOH 8194 27.127 45.046 35.049 1.00 24.02 O HETATM 10041 O HOH 8195 73.921 22.935 18.943 1.00 29.41 O HETATM 10042 O HOH 8196 18.153 50.887 32.927 1.00 43.89 O HETATM 10043 O HOH 8197 64.984 6.884 58.308 1.00 27.06 O HETATM 10044 O HOH 8198 23.014 13.926 7.613 1.00 40.19 O HETATM 10045 O HOH 8199 48.401 26.009 −5.169 1.00 30.24 O HETATM 10046 O HOH 8200 66.865 −7.653 21.825 1.00 30.37 O HETATM 10047 O HOH 8201 45.045 48.534 −8.439 1.00 34.67 O HETATM 10048 O HOH 8202 17.155 51.924 0.154 1.00 41.46 O HETATM 10049 O HOH 8203 43.366 53.992 −17.926 1.00 35.60 O HETATM 10050 O HOH 8204 17.215 35.488 26.426 1.00 45.03 O HETATM 10051 O HOH 8205 61.642 28.204 11.796 1.00 29.48 O HETATM 10052 O HOH 8206 60.187 42.226 22.209 1.00 40.71 O HETATM 10053 O HOH 8207 77.953 27.539 35.830 1.00 34.42 O HETATM 10054 O HOH 8208 25.995 34.365 7.024 1.00 28.38 O HETATM 10055 O HOH 8209 15.844 31.108 11.675 1.00 33.02 O HETATM 10056 O HOH 8210 12.732 15.752 6.140 1.00 40.56 O HETATM 10057 O HOH 8211 62.907 2.915 62.753 1.00 30.92 O HETATM 10058 O HOH 8212 24.044 10.937 −21.880 1.00 42.40 O HETATM 10059 O HOH 8213 79.343 −1.121 18.453 1.00 33.07 O HETATM 10060 O HOH 8214 68.004 33.744 5.930 1.00 33.70 O HETATM 10061 O HOH 8215 76.210 17.950 33.459 1.00 38.92 O HETATM 10062 O HOH 8216 41.987 23.581 −37.300 1.00 44.75 O HETATM 10063 O HOH 8217 80.531 11.139 −10.855 1.00 40.75 O HETATM 10064 O HOH 8218 61.409 0.815 −24.031 1.00 29.53 O HETATM 10065 O HOH 8219 65.745 12.430 −11.075 1.00 34.48 O HETATM 10066 O HOH 8220 17.792 29.223 −7.156 1.00 34.49 O HETATM 10067 O HOH 8221 50.809 25.767 6.138 1.00 33.13 O HETATM 10068 O HOH 8222 16.549 52.909 10.612 1.00 32.50 O HETATM 10069 O HOH 8223 47.243 61.049 −7.633 1.00 29.91 O HETATM 10070 O HOH 8224 28.774 46.253 −57.672 1.00 27.24 O HETATM 10071 O HOH 8225 12.249 27.080 5.705 1.00 33.04 O HETATM 10072 O HOH 8226 46.668 57.243 −23.318 1.00 40.27 O HETATM 10073 O HOH 8227 82.077 −14.452 5.876 1.00 36.27 O HETATM 10074 O HOH 8228 40.389 30.876 −17.266 1.00 30.97 O HETATM 10075 O HOH 8229 49.327 18.630 −3.627 1.00 27.94 O HETATM 10076 O HOH 8230 30.848 43.282 37.200 1.00 29.75 O HETATM 10077 O HOH 8231 27.538 34.519 36.719 1.00 43.67 O HETATM 10078 O HOH 8232 14.545 35.316 −2.739 1.00 36.62 O HETATM 10079 O HOH 8233 34.553 42.907 −11.613 1.00 38.00 O HETATM 10080 O HOH 8234 50.214 50.520 6.739 1.00 38.64 O HETATM 10081 O HOH 8235 19.251 23.087 −13.713 1.00 28.03 O HETATM 10082 O HOH 8236 30.812 60.706 −21.436 1.00 28.95 O HETATM 10083 O HOH 8237 66.757 11.655 −26.300 1.00 39.69 O HETATM 10084 O HOH 8238 35.046 35.455 −12.734 1.00 39.15 O HETATM 10085 O HOH 8239 23.172 32.494 −15.018 1.00 36.10 O HETATM 10086 O HOH 8240 12.204 48.652 10.766 1.00 31.97 O HETATM 10087 O HOH 8241 32.636 46.110 −16.084 1.00 33.67 O HETATM 10088 O HOH 8242 23.375 28.819 −16.529 1.00 28.89 O HETATM 10089 O HOH 8243 33.092 46.467 8.373 1.00 34.92 O HETATM 10090 O HOH 8244 75.191 −15.210 1.700 1.00 34.77 O HETATM 10091 O HOH 8245 51.102 7.512 −30.877 1.00 39.35 O HETATM 10092 O HOH 8246 29.649 40.776 11.607 1.00 36.74 O HETATM 10093 O HOH 8247 64.241 −11.167 31.991 1.00 36.77 O HETATM 10094 O HOH 8248 35.807 52.227 −37.837 1.00 42.89 O HETATM 10095 O HOH 8249 21.004 47.633 −18.472 1.00 43.58 O HETATM 10096 O HOH 8250 20.104 21.077 −27.523 1.00 37.70 O HETATM 10097 O HOH 8251 82.131 −14.102 −15.373 1.00 46.38 O HETATM 10098 O HOH 8252 52.596 0.316 −10.214 1.00 33.07 O HETATM 10099 O HOH 8253 54.192 1.046 30.601 1.00 35.61 O HETATM 10100 O HOH 8254 28.240 44.984 −53.215 1.00 30.80 O HETATM 10101 O HOH 8255 64.550 −3.466 −2.475 1.00 37.95 O HETATM 10102 O HOH 8256 16.260 21.918 −28.169 1.00 42.28 O HETATM 10103 O HOH 8257 31.591 44.914 17.918 1.00 30.56 O HETATM 10104 O HOH 8258 63.725 18.485 −36.455 1.00 41.83 O HETATM 10105 O HOH 8259 54.594 4.317 −30.127 1.00 36.36 O HETATM 10106 O HOH 8260 12.031 48.610 15.939 1.00 34.32 O HETATM 10107 O HOH 8261 62.047 0.039 1.306 1.00 40.89 O HETATM 10108 O HOH 8262 63.743 26.826 40.506 1.00 38.51 O HETATM 10109 O HOH 8263 80.317 −12.708 5.435 1.00 35.75 O CONECT 4172 4569 CONECT 4569 4172 CONECT 4893 5256 CONECT 5256 4893 CONECT 5615 6015 CONECT 6015 5615 CONECT 6356 6708 CONECT 6708 6356 CONECT 7044 7433 CONECT 7433 7044 CONECT 7784 8177 CONECT 8177 7784 CONECT 8549 8942 CONECT 8942 8549 CONECT 9289 9675 CONECT 9675 9289 CONECT 9827 9828 9829 9830 9831 CONECT 9828 9827 CONECT 9829 9827 CONECT 9830 9827 CONECT 9831 9827 CONECT 9832 9833 9834 9835 9836 CONECT 9833 9832 CONECT 9834 9832 CONECT 9835 9832 CONECT 9836 9832 CONECT 9837 9838 9839 9840 9841 CONECT 9838 9837 CONECT 9839 9837 CONECT 9840 9837 CONECT 9841 9837 CONECT 9842 9843 9844 9845 9846 CONECT 9843 9842 CONECT 9844 9842 CONECT 9845 9842 CONECT 9846 9842 MASTER  540 0 4 24 123 0 0 610101 8 36 112

TABLE 4 Stem Cell Factor Dimer HEADER HORMONE/GROWTH FACTOR 05-MAY-00 1EXZ TITLE STRUCTURE OF STEM CELL FACTOR COMPND MOL_ID: 1; COMPND  2 MOLECULE: STEM CELL FACTOR; COMPND  3 CHAIN: A, B, C, D; COMPND  4 FRAGMENT: 26–166; COMPND  5 SYNONYM: SCF; COMPND  6 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE  2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE  3 ORGANISM_COMMON: HUMAN; SOURCE  4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE  5 EXPRESSION_SYSTEM_COMMON: BACTERIA KEYWDS SCF EXPDTA X-RAY DIFFRACTION AUTHOR Z.ZHANG,R.ZHANG,A.JOACHIMIAK,J.SCHLESSINGER,X.KONG REVDAT  1 06-JUL-00 1EXZ  0 JRNL AUTH Z.ZHANG,R.ZHANG,A.JOACHIMIAK,J.SCHLESSINGER,X.KONG JRNL TITL CRYSTAL STRUCTURE OF HUMAN STEM CELL FACTOR: JRNL TITL 2 IMPLICATION FOR STEM CELL FACTOR RECEPTOR JRNL TITL 3 DIMERIZATION AND ACTIVATION. JRNL REF PROC.NAT.ACAD.SCI.USA    V.  97 7732 2000 JRNL REFN ASTM PNASA6 US ISSN 0027-8424 REMARK  1 REMARK  2 REMARK  2 RESOLUTION. 2.30 ANGSTROMS. REMARK  3 REMARK  3 REFINEMENT. REMARK  3 PROGRAM : CNS REMARK  3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- REMARK  3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU, REMARK  3 : READ,RICE,SIMONSON,WARREN REMARK  3 REMARK  3 REFINEMENT TARGET : MLF REMARK  3 REMARK  3 DATA USED IN REFINEMENT. REMARK  3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK  3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00 REMARK  3 DATA CUTOFF (SIGMA(F)) : 2.000 REMARK  3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL REMARK  3 COMPLETENESS (WORKING+TEST) (%) : 10.0 REMARK  3 NUMBER OF REFLECTIONS : 21494 REMARK  3 REMARK  3 REMARK  3 FIT TO DATA USED IN REFINEMENT. REMARK  3 CROSS-VALIDATION METHOD : NULL REMARK  3 FREE R VALUE TEST SET SELECTION : RANDOMLY SELECTED 10% REMARK  3  OF REFLECTIONS REMARK  3 R VALUE (WORKING SET) : 0.223 REMARK  3 FREE R VALUE : 0.294 REMARK  3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK  3 FREE R VALUE TEST SET COUNT : 2133 REMARK  3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK  3 REMARK  3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK  3 TOTAL NUMBER OF BINS USED : NULL REMARK  3 BIN RESOLUTION RANGE HIGH (A) : NULL REMARK  3 BIN RESOLUTION RANGE LOW (A) : NULL REMARK  3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK  3 REFLECTIONS IN BIN (WORKING SET) : NULL REMARK  3 BIN R VALUE (WORKING SET) : NULL REMARK  3 BIN FREE R VALUE : NULL REMARK  3 BIN FREE R VALUE TEST SET SIZE (%) : NULL REMARK  3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK  3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK  3 REMARK  3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK  3 PROTEIN ATOMS : 4090 REMARK  3 NUCLEIC ACID ATOMS : 0 REMARK  3 HETEROGEN ATOMS : 14 REMARK  3 SOLVENT ATOMS : 132 REMARK  3 REMARK  3 B VALUES. REMARK  3 FROM WILSON PLOT (A**2) : 45.00 REMARK  3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK  3 OVERALL ANISOTROPIC B VALUE. REMARK  3 B11 (A**2) : NULL REMARK  3 B22 (A**2) : NULL REMARK  3 B33 (A**2) : NULL REMARK  3 B12 (A**2) : NULL REMARK  3 B13 (A**2) : NULL REMARK  3 B23 (A**2) : NULL REMARK  3 REMARK  3 ESTIMATED COORDINATE ERROR. REMARK  3 ESD FROM LUZZATI PLOT (A) : NULL REMARK  3 ESD FROM SIGMAA (A) : NULL REMARK  3 LOW RESOLUTION CUTOFF (A) : NULL REMARK  3 REMARK  3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR. REMARK  3 ESD FROM C-V LUZZATI PLOT (A) : NULL REMARK  3 ESD FROM C-V SIGMAA (A) : NULL REMARK  3 REMARK  3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK  3 BOND LENGTHS (A) : 0.007 REMARK  3 BOND ANGLES (DEGREES) : 1.22 REMARK  3 DIHEDRAL ANGLES (DEGREES) : NULL REMARK  3 IMPROPER ANGLES (DEGREES) : NULL REMARK  3 REMARK  3 ISOTROPIC THERMAL MODEL : NULL REMARK  3 REMARK  3 ISOTROPIC THERMAL FACTOR RESTRAINTS.     RMS  SIGMA REMARK  3 MAIN-CHAIN BOND (A**2) : NULL ; NULL REMARK  3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL REMARK  3 SIDE-CHAIN BOND (A**2) : NULL ; NULL REMARK  3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL REMARK  3 REMARK  3 REMARK  3 BULK SOLVENT MODELING. REMARK  3 METHOD USED : NULL REMARK  3 KSOL : NULL REMARK  3 BSOL : NULL REMARK  3 REMARK  3 NCS MODEL : NULL REMARK  3 REMARK  3 NCS RESTRAINTS.     RMS  SIGMA/WEIGHT REMARK  3 GROUP 1 POSITIONAL (A) : NULL ; NULL REMARK  3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL REMARK  3 REMARK  3 PARAMETER FILE 1 : NULL REMARK  3 TOPOLOGY FILE 1 : NULL REMARK  3 REMARK  3 OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD TARGET USING REMARK  3 AMPLITUDES REMARK  4 REMARK  4 1EXZ COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-2000. REMARK 100 THE RCSB ID CODE IS RCSB011008. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 26-NOV-1999 REMARK 200 TEMPERATURE (KELVIN) : 100.0 REMARK 200 PH : 7.00 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y; Y REMARK 200 RADIATION SOURCE : APS ; APS REMARK 200 BEAMLINE : 19ID; 19ID REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.03; 1.55 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : BRANDEIS REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21454 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 40.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 200 DATA REDUNDANCY : 8.000 REMARK 200 R MERGE (I) : 0.05800 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38 REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1 REMARK 200 DATA REDUNDANCY IN SHELL : 7.00 REMARK 200 R MERGE FOR SHELL (I) : 0.25000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL REMARK 200 SOFTWARE USED: PHASES REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS  (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG 400, 250 MM CACL2, 1 REMARK 280 MM SMCL3 REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 −X,1/2+Y,−Z REMARK 290 REMARK 290 WHERE NNN → OPERATOR NUMBER REMARK 290 MMM → TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1  1.000000 0.000000  0.000000  0.00000 REMARK 290 SMTRY2 1  0.000000 1.000000  0.000000  0.00000 REMARK 290 SMTRY3 1  0.000000 0.000000  1.000000  0.00000 REMARK 290 SMTRY1 2 −1.000000 0.000000  0.000000  0.00000 REMARK 290 SMTRY2 2  0.000000 1.000000  0.000000 43.76300 REMARK 290 SMTRY3 2  0.000000 0.000000 −1.000000  0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2 REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). REMARK 350 REMARK 350 GENERATING THE BIOMOLECULE REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1  1.000000 0.000000  0.000000  0.00000 REMARK 350 BIOMT2 1  0.000000 1.000000  0.000000  0.00000 REMARK 350 BIOMT3 1  0.000000 0.000000  1.000000  0.00000 REMARK 350 BIOMOLECULE: 2 REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D REMARK 350 BIOMT1 2  1.000000 0.000000  0.000000  0.00000 REMARK 350 BIOMT2 2  0.000000 1.000000  0.000000  0.00000 REMARK 350 BIOMT3 2  0.000000 0.000000  1.000000  0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 GLU A  1 REMARK 465 GLY A  2 REMARK 465 ILE A  3 REMARK 465 GLU A 134 REMARK 465 THR A 135 REMARK 465 SER A 136 REMARK 465 VAL A 140 REMARK 465 SER A 141 REMARK 465 GLU B 201 REMARK 465 GLU C 401 REMARK 465 GLY C 402 REMARK 465 ILE C 403 REMARK 465 CYS C 404 REMARK 465 ARG C 405 REMARK 465 ASN C 406 REMARK 465 ARG C 407 REMARK 465 VAL C 408 REMARK 465 VAL C 540 REMARK 465 SER C 541 REMARK 465 GLU D 601 REMARK 465 GLY D 602 REMARK 465 ILE D 603 REMARK 465 CYS D 604 REMARK 465 ARG D 605 REMARK 465 ASN D 606 REMARK 465 ARG D 607 REMARK 465 VAL D 608 REMARK 465 SER D 733 REMARK 465 GLU D 734 REMARK 465 THR D 735 REMARK 465 SER D 736 REMARK 465 ASP D 737 REMARK 465 CYS D 738 REMARK 465 VAL D 739 REMARK 465 VAL D 740 REMARK 465 SER D 741 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 ARG A  5 CG CD NE CZ NH1 NH2 REMARK 470 ARG A  7 CG CD NE CZ NH1 NH2 REMARK 470 ASN A  10 CG OD1 ND2 REMARK 470 GLU B 292 CG CD OE1 OE2 REMARK 470 ASN B 293 CG OD1 ND2 REMARK 470 SER B 294 OG REMARK 470 SER B 295 OG REMARK 470 LYS B 296 CG CD CE NZ REMARK 470 ASP B 297 CG OD1 OD2 REMARK 470 LEU B 298 CG CD1 CD2 REMARK 470 LYS B 299 CG CD CE NZ REMARK 470 LYS B 300 CG CD CE NZ REMARK 470 SER B 301 OG REMARK 470 PHE B 302 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 303 CG CD CE NZ REMARK 470 SER B 341 OG REMARK 470 ASN C 410 CG OD1 ND2 REMARK 470 LYS C 413 CG CD CE NZ REMARK 470 LYS C 491 CG CD CE NZ REMARK 470 GLU C 492 CG CD OE1 OE2 REMARK 470 ASN C 493 CG OD1 ND2 REMARK 470 SER C 494 OG REMARK 470 SER C 495 OG REMARK 470 LYS C 496 CG CD CE NZ REMARK 470 ASP C 497 CG OD1 OD2 REMARK 470 LEU C 498 CG CD1 CD2 REMARK 470 LYS C 499 CG CD CE NZ REMARK 470 LYS C 500 CG CD CE NZ REMARK 470 SER C 501 OG REMARK 470 PHE C 502 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS D 696 CG CD CE NZ REMARK 470 LYS D 699 CG CD CE NZ REMARK 470 LYS D 700 CG CD CE NZ REMARK 470 SER D 701 OG REMARK 470 PHE D 702 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS D 703 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI REMARK 500 SM SM C 801 O HOH 946 1.92 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OE1 GLU D 713 SM SM B 803 2645 2.12 REMARK 500 OE2 GLU A  88 SM SM C 801 2656 2.17 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO A  23 CG PRO A  23 CB  0.046 REMARK 500 MET A  48 CE MET A  48 SD −0.081 REMARK 500 MET C 448 SD MET C 448 CG  0.040 REMARK 500 PRO C 512 CG PRO C 512 CB  0.058 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 THR A 111 N - CA - C ANGL. DEV. = −7.7 DEGREES REMARK 500 ARG A 117 N - CA - C ANGL. DEV. = −7.7 DEGREES REMARK 500 PRO B 234 N - CA - C ANGL. DEV. = 10.2 DEGREES REMARK 500 ILE B 245 N - CA - C ANGL. DEV. =  8.5 DEGREES REMARK 500 ARG B 317 N - CA - C ANGL. DEV. = −8.0 DEGREES REMARK 500 LYS C 413 N - CA - C ANGL. DEV. = −8.0 DEGREES REMARK 500 ASP C 414 N - CA - C ANGL. DEV. = −8.4 DEGREES REMARK 500 ASP C 437 N - CA - C ANGL. DEV. =  7.6 DEGREES REMARK 500 TRP C 444 N - CA - C ANGL. DEV. = 10.9 DEGREES REMARK 500 ILE C 445 N - CA - C ANGL. DEV. =  7.2 DEGREES REMARK 500 ASP C 528 N - CA - C ANGL. DEV. = 11.9 DEGREES REMARK 500 VAL C 530 N - CA - C ANGL. DEV. =  8.9 DEGREES REMARK 500 THR D 711 N - CA - C ANGL. DEV. = −8.6 DEGREES REMARK 500 ARG D 717 N - CA - C ANGL. DEV. = −8.1 DEGREES REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER A 101 104.88  120.52 REMARK 500 PHE A 102  78.79 −100.99 REMARK 500 PHE B 302  50.55  −96.61 REMARK 500 PHE C 502  54.70  −95.94 REMARK 500 ASP C 528  25.52 −113.66 REMARK 500 VAL C 530  33.44  113.93 REMARK 500 ILE D 645  61.98  −60.00 DBREF 1EXZ A  1 141 SWS P21583 SCF_HUMAN 26 166 DBREF 1EXZ B 201 341 SWS P21583 SCF_HUMAN 26 166 DBREF 1EXZ C 401 541 SWS P21583 SCF_HUMAN 26 166 DBREF 1EXZ D 601 741 SWS P21583 SCF_HUMAN 26 166 SEQRES  1 A 141 GLU GLY ILE CYS ARG ASN ARG VAL THR ASN ASN VAL LYS SEQRES  2 A 141 ASP VAL THR LYS LEU VAL ALA ASN LEU PRO LYS ASP TYR SEQRES  3 A 141 MET ILE THR LEU LYS TYR VAL PRO GLY MET ASP VAL LEU SEQRES  4 A 141 PRO SER HIS CYS TRP ILE SER GLU MET VAL VAL GLN LEU SEQRES  5 A 141 SER ASP SER LEU THR ASP LEU LEU ASP LYS PHE SER ASN SEQRES  6 A 141 ILE SER GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS SEQRES  7 A 141 LEU VAL ASN ILE VAL ASP ASP LEU VAL GLU CYS VAL LYS SEQRES  8 A 141 GLU ASN SER SER LYS ASP LEU LYS LYS SER PHE LYS SER SEQRES  9 A 141 PRO GLU PRO ARG LEU PHE THR PRO GLU GLU PHE PHE ARG SEQRES  10 A 141 ILE PHE ASN ARG SER ILE ASP ALA PHE LYS ASP PHE VAL SEQRES  11 A 141 VAL ALA SER GLU THR SER ASP CYS VAL VAL SER SEQRES  1 B 141 GLU GLY ILE CYS ARG ASN ARG VAL THR ASN ASN VAL LYS SEQRES  2 B 141 ASP VAL THR LYS LEU VAL ALA ASN LEU PRO LYS ASP TYR SEQRES  3 B 141 MET ILE THR LEU LYS TYR VAL PRO GLY MET ASP VAL LEU SEQRES  4 B 141 PRO SER HIS CYS TRP ILE SER GLU MET VAL VAL GLN LEU SEQRES  5 B 141 SER ASP SER LEU THR ASP LEU LEU ASP LYS PHE SER ASN SEQRES  6 B 141 ILE SER GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS SEQRES  7 B 141 LEU VAL ASN ILE VAL ASP ASP LEU VAL GLU CYS VAL LYS SEQRES  8 B 141 GLU ASN SER SER LYS ASP LEU LYS LYS SER PHE LYS SER SEQRES  9 B 141 PRO GLU PRO ARG LEU PHE THR PRO GLU GLU PHE PHE ARG SEQRES  10 B 141 ILE PHE ASN ARG SER ILE ASP ALA PHE LYS ASP PHE VAL SEQRES  11 B 141 VAL ALA SER GLU THR SER ASP CYS VAL VAL SER SEQRES  1 C 141 GLU GLY ILE CYS ARG ASN ARG VAL THR ASN ASN VAL LYS SEQRES  2 C 141 ASP VAL THR LYS LEU VAL ALA ASN LEU PRO LYS ASP TYR SEQRES  3 C 141 MET ILE THR LEU LYS TYR VAL PRO GLY MET ASP VAL LEU SEQRES  4 C 141 PRO SER HIS CYS TRP ILE SER GLU MET VAL VAL GLN LEU SEQRES  5 C 141 SER ASP SER LEU THR ASP LEU LEU ASP LYS PHE SER ASN SEQRES  6 C 141 ILE SER GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS SEQRES  7 C 141 LEU VAL ASN ILE VAL ASP ASP LEU VAL GLU CYS VAL LYS SEQRES  8 C 141 GLU ASN SER SER LYS ASP LEU LYS LYS SER PHE LYS SER SEQRES  9 C 141 PRO GLU PRO ARG LEU PHE THR PRO GLU GLU PHE PHE ARG SEQRES  10 C 141 ILE PHE ASN ARG SER ILE ASP ALA PHE LYS ASP PHE VAL SEQRES  11 C 141 VAL ALA SER GLU THR SER ASP CYS VAL VAL SER SEQRES  1 D 141 GLU GLY ILE CYS ARG ASN ARG VAL THR ASN ASN VAL LYS SEQRES  2 D 141 ASP VAL THR LYS LEU VAL ALA ASN LEU PRO LYS ASP TYR SEQRES  3 D 141 MET ILE THR LEU LYS TYR VAL PRO GLY MET ASP VAL LEU SEQRES  4 D 141 PRO SER HIS CYS TRP ILE SER GLU MET VAL VAL GLN LEU SEQRES  5 D 141 SER ASP SER LEU THR ASP LEU LEU ASP LYS PHE SER ASN SEQRES  6 D 141 ILE SER GLU GLY LEU SER ASN TYR SER ILE ILE ASP LYS SEQRES  7 D 141 LEU VAL ASN ILE VAL ASP ASP LEU VAL GLU CYS VAL LYS SEQRES  8 D 141 GLU ASN SER SER LYS ASP LEU LYS LYS SER PHE LYS SER SEQRES  9 D 141 PRO GLU PRO ARG LEU PHE THR PRO GLU GLU PHE PHE ARG SEQRES  10 D 141 ILE PHE ASN ARG SER ILE ASP ALA PHE LYS ASP PHE VAL SEQRES  11 D 141 VAL ALA SER GLU THR SER ASP CYS VAL VAL SER HET  SM C 801 1 HET  SM 802 1 HET  SM B 803 1 HET  SM 804 1 HET  CA C 805 1 HET  CA A 806 1 HET TRS 807 8 HETNAM SM SAMARIUM (III) ION HETNAM CA CALCIUM ION HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL HETSYN TRS TRIS BUFFER FORMUL  5  SM  4(SM1 3+) FORMUL  9  CA  2(CA1 2+) FORMUL  11 TRS  C4 H12 N1 O3 1+ FORMUL  12 HOH *132(H2 O1) HELIX  1  1 ASN A  11 ASN A  21 1  11 HELIX  2  2 PRO A  40 CYS A  43 5  4 HELIX  3  3 TRP A  44 ASP A  61 1  18 HELIX  4  4 SER A  71 ASN A  93 1  23 HELIX  5  5 THR A 111 ASP A 128 1  18 HELIX  6  6 ASN B 211 ASN B 221 1  11 HELIX  7  7 PRO B 240 CYS B 243 5  4 HELIX  8  8 TRP B 244 ASP B 261 1  18 HELIX  9  9 SER B 271 VAL B 290 1  20 HELIX  10 10 THR B 311 ALA B 325 1  15 HELIX  11 11 LYS C 413 ASN C 421 1  9 HELIX  12 12 PRO C 440 CYS C 443 5  4 HELIX  13 13 TRP C 444 ASP C 461 1  18 HELIX  14 14 SER C 471 LYS C 491 1  21 HELIX  15 15 THR C 511 ALA C 525 1  15 HELIX  16 16 VAL D 612 ASN D 621 1  10 HELIX  17 17 ILE D 645 ASP D 661 1  17 HELIX  18 18 SER D 671 ASN D 693 1  23 HELIX  19 19 THR D 711 LYS D 727 1  17 SHEET  1 A 2 ILE A  28 TYR A  32  0 SHEET  2 A 2 GLU A 106 PHE A 110 −1 O GLU A 106 N TYR A  32 SHEET  1 B 2 ILE B 228 LYS B 231  0 SHEET  2 B 2 PRO B 307 PHE B 310 −1 O ARG B 308 N LEU B 230 SHEET  1 C 2 ILE C 428 LYS C 431  0 SHEET  2 C 2 PRO C 507 PHE C 510 −1 O ARG C 508 N LEU C 430 SHEET  1 D 2 ILE D 628 LYS D 631  0 SHEET  2 D 2 PRO D 707 PHE D 710 −1 N ARG D 708 O LEU D 630 SSBOND  1 CYS A  4 CYS A  89 SSBOND  2 CYS A  43 CYS A 138 SSBOND  3 CYS B 204 CYS B 289 SSBOND  4 CYS B 243 CYS B 338 SSBOND  5 CYS C 443 CYS C 538 LINK    SM SM B 803  OD2 ASP B 337 CRYST1  36.154 87.526 79.434 90.00 97.76 90.00 P 1 21 1  8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.027659 0.000000 0.003769 0.00000 SCALE2 0.000000 0.011425 0.000000 0.00000 SCALE3 0.000000 0.000000 0.012705 0.00000 ATOM   1 N CYS A  4 24.179 55.019 52.849 1.00 86.63 N ATOM   2 CA CYS A  4 23.377 56.276 52.833 1.00 86.89 C ATOM   3 C CYS A  4 21.900 55.949 52.656 1.00 88.25 C ATOM   4 O CYS A  4 21.366 56.071 51.554 1.00 88.58 O ATOM   5 CB CYS A  4 23.837 57.181 51.687 1.00 84.65 C ATOM   6 SG CYS A  4 25.616 57.570 51.706 1.00 80.96 S ATOM   7 N ARG A  5 21.259 55.533 53.748 1.00 89.34 N ATOM   8 CA ARG A  5 19.840 55.170 53.770 1.00 90.15 C ATOM   9 C ARG A  5 19.129 55.410 52.443 1.00 90.43 C ATOM  10 O ARG A  5 18.685 54.466 51.786 1.00 90.05 O ATOM  11 CB ARG A  5 19.131 55.932 54.884 1.00 90.62 C ATOM  12 N ASN A  6 19.019 56.678 52.059 1.00 90.83 N ATOM  13 CA ASN A  6 18.372 57.045 50.806 1.00 91.40 C ATOM  14 C ASN A  6 19.348 56.829 49.647 1.00 91.43 C ATOM  15 O ASN A  6 20.345 57.544 49.516 1.00 90.94 O ATOM  16 CB ASN A  6 17.927 58.509 50.851 1.00 91.94 C ATOM  17 CG ASN A  6 16.999 58.870 49.709 1.00 92.27 C ATOM  18 OD1 ASN A  6 17.376 58.797 48.541 1.00 92.40 O ATOM  19 ND2 ASN A  6 15.773 59.259 50.043 1.00 92.61 N ATOM  20 N ARG A  7 19.051 55.832 48.815 1.00 91.42 N ATOM  21 CA ARG A  7 19.894 55.494 47.672 1.00 90.97 C ATOM  22 C ARG A  7 19.230 55.836 46.340 1.00 90.59 C ATOM  23 O ARG A  7 19.817 55.635 45.278 1.00 91.32 O ATOM  24 CB ARG A  7 20.247 54.006 47.712 1.00 91.02 C ATOM  25 N VAL A  8 18.005 56.349 46.401 1.00 89.85 N ATOM  26 CA VAL A  8 17.257 56.729 45.203 1.00 88.72 C ATOM  27 C VAL A  8 16.890 55.511 44.345 1.00 87.92 C ATOM  28 O VAL A  8 16.539 55.648 43.170 1.00 87.06 O ATOM  29 CB VAL A  8 18.062 57.740 44.338 1.00 88.56 C ATOM  30 CG1 VAL A  8 17.170 58.340 43.261 1.00 88.77 C ATOM  31 CG2 VAL A  8 18.636 58.840 45.219 1.00 88.36 C ATOM  32 N THR A  9 16.964 54.325 44.944 1.00 86.61 N ATOM  33 CA THR A  9 16.635 53.081 44.249 1.00 85.51 C ATOM  34 C THR A  9 17.126 53.090 42.802 1.00 84.43 C ATOM  35 O THR A  9 16.415 53.524 41.895 1.00 84.69 O ATOM  36 CB THR A  9 15.108 52.823 44.248 1.00 85.48 C ATOM  37 OG1 THR A  9 14.629 52.757 45.598 1.00 85.34 O ATOM  38 CG2 THR A  9 14.788 51.510 43.546 1.00 85.22 C ATOM  39 N ASN A  10 18.345 52.605 42.596 1.00 83.25 N ATOM  40 CA ASN A  10 18.935 52.552 41.265 1.00 81.58 C ATOM  41 C ASN A  10 18.944 51.119 40.754 1.00 80.41 C ATOM  42 O ASN A  10 19.903 50.696 40.108 1.00 80.59 O ATOM  43 CB ASN A  10 20.356 53.091 41.308 1.00 81.52 C ATOM  44 N ASN A  11 17.878 50.377 41.047 1.00 78.05 N ATOM  45 CA ASN A  11 17.777 48.985 40.622 1.00 75.63 C ATOM  46 C ASN A  11 18.070 48.776 39.142 1.00 73.02 C ATOM  47 O ASN A  11 17.862 49.669 38.317 1.00 71.57 O ATOM  48 CB ASN A  11 16.397 48.417 40.958 1.00 77.49 C ATOM  49 CG ASN A  11 16.269 48.032 42.418 1.00 78.14 C ATOM  50 OD1 ASN A  11 17.084 47.269 42.944 1.00 78.66 O ATOM  51 ND2 ASN A  11 15.240 48.552 43.080 1.00 78.86 N ATOM  52 N VAL A  12 18.549 47.576 38.823 1.00 70.35 N ATOM  53 CA VAL A  12 18.911 47.209 37.460 1.00 66.91 C ATOM  54 C VAL A  12 17.720 47.300 36.511 1.00 63.29 C ATOM  55 O VAL A  12 17.827 46.969 35.334 1.00 63.69 O ATOM  56 CB VAL A  12 19.492 45.777 37.411 1.00 67.69 C ATOM  57 CG1 VAL A  12 20.358 45.608 36.170 1.00 68.11 C ATOM  58 CG2 VAL A  12 20.306 45.503 38.665 1.00 68.37 C ATOM  59 N LYS A  13 16.584 47.747 37.030 1.00 58.49 N ATOM  60 CA LYS A  13 15.386 47.899 36.220 1.00 55.37 C ATOM  61 C LYS A  13 15.729 48.723 34.978 1.00 52.98 C ATOM  62 O LYS A  13 15.588 48.259 33.843 1.00 52.47 O ATOM  63 CB LYS A  13 14.299 48.609 37.036 1.00 56.53 C ATOM  64 CG LYS A  13 14.811 49.848 37.769 1.00 58.27 C ATOM  65 CD LYS A  13 13.702 50.667 38.398 1.00 59.14 C ATOM  66 CE LYS A  13 14.263 51.947 39.006 1.00 60.60 C ATOM  67 NZ LYS A  13 13.191 52.883 39.456 1.00 60.73 N ATOM  68 N ASP A  14 16.192 49.949 35.205 1.00 49.63 N ATOM  69 CA ASP A  14 16.558 50.841 34.117 1.00 46.02 C ATOM  70 C ASP A  14 17.959 50.521 33.575 1.00 40.96 C ATOM  71 O ASP A  14 18.231 50.731 32.394 1.00 38.69 O ATOM  72 CB ASP A  14 16.477 52.294 34.591 1.00 50.58 C ATOM  73 CG ASP A  14 17.233 52.528 35.886 1.00 56.43 C ATOM  74 OD1 ASP A  14 16.804 52.008 36.943 1.00 59.62 O ATOM  75 OD2 ASP A  14 18.263 53.233 35.845 1.00 59.80 O ATOM  76 N VAL A  15 18.832 50.004 34.437 1.00 34.36 N ATOM  77 CA VAL A  15 20.187 49.638 34.033 1.00 32.14 C ATOM  78 C VAL A  15 20.136 48.524 32.989 1.00 31.17 C ATOM  79 O VAL A  15 20.816 48.581 31.961 1.00 29.80 O ATOM  80 CB VAL A  15 21.036 49.157 35.241 1.00 29.72 C ATOM  81 CG1 VAL A  15 22.346 48.563 34.753 1.00 30.51 C ATOM  82 CG2 VAL A  15 21.316 50.312 36.176 1.00 24.91 C ATOM  83 N THR A  16 19.312 47.518 33.259 1.00 31.37 N ATOM  84 CA THR A  16 19.137 46.390 32.355 1.00 31.24 C ATOM  85 C THR A  16 18.692 46.881 30.978 1.00 31.26 C ATOM  86 O THR A  16 19.159 46.389 29.952 1.00 32.04 O ATOM  87 CB THR A  16 18.091 45.408 32.919 1.00 33.12 C ATOM  88 OG1 THR A  16 18.636 44.757 34.072 1.00 30.67 O ATOM  89 CG2 THR A  16 17.705 44.364 31.875 1.00 33.49 C ATOM  90 N LYS A  17 17.791 47.857 30.963 1.00 31.79 N ATOM  91 CA LYS A  17 17.316 48.419 29.711 1.00 33.62 C ATOM  92 C LYS A  17 18.479 49.133 29.017 1.00 32.83 C ATOM  93 O LYS A  17 18.739 48.904 27.832 1.00 33.50 O ATOM  94 CB LYS A  17 16.173 49.406 29.967 1.00 38.18 C ATOM  95 CG LYS A  17 15.430 49.840 28.698 1.00 41.80 C ATOM  96 CD LYS A  17 14.288 50.804 29.014 1.00 43.51 C ATOM  97 CE LYS A  17 13.416 51.080 27.783 1.00 46.10 C ATOM  98 NZ LYS A  17 14.145 51.735 26.648 1.00 45.83 N ATOM  99 N LEU A  18 19.192 49.976 29.763 1.00 30.88 N ATOM  100 CA LEU A  18 20.333 50.716 29.205 1.00 28.79 C ATOM  101 C LEU A  18 21.328 49.767 28.545 1.00 25.72 C ATOM  102 O LEU A  18 21.734 49.973 27.408 1.00 23.33 O ATOM  103 CB LEU A  18 21.060 51.494 30.298 1.00 27.65 C ATOM  104 CG LEU A  18 21.681 52.831 29.903 1.00 28.11 C ATOM  105 CD1 LEU A  18 22.621 53.255 31.012 1.00 27.08 C ATOM  106 CD2 LEU A  18 22.398 52.747 28.579 1.00 23.78 C ATOM  107 N VAL A  19 21.722 48.731 29.278 1.00 26.84 N ATOM  108 CA VAL A  19 22.661 47.740 28.765 1.00 25.57 C ATOM  109 C VAL A  19 22.113 47.044 27.513 1.00 27.11 C ATOM  110 O VAL A  19 22.869 46.674 26.612 1.00 27.07 O ATOM  111 CB VAL A  19 22.987 46.691 29.855 1.00 26.55 C ATOM  112 CG1 VAL A  19 23.796 45.507 29.265 1.00 22.88 C ATOM  113 CG2 VAL A  19 23.775 47.355 30.960 1.00 23.60 C ATOM  114 N ALA A  20 20.798 46.880 27.443 1.00 27.84 N ATOM  115 CA ALA A  20 20.195 46.227 26.287 1.00 29.20 C ATOM  116 C ALA A  20 20.309 47.120 25.050 1.00 30.00 C ATOM  117 O ALA A  20 20.302 46.636 23.914 1.00 30.00 O ATOM  118 CB ALA A  20 18.725 45.906 26.577 1.00 29.27 C ATOM  119 N ASN A  21 20.436 48.424 25.276 1.00 28.74 N ATOM  120 CA ASN A  21 20.527 49.375 24.179 1.00 28.64 C ATOM  121 C ASN A  21 21.868 50.041 23.929 1.00 27.97 C ATOM  122 O ASN A  21 21.957 50.999 23.159 1.00 30.28 O ATOM  123 CB ASN A  21 19.433 50.424 24.331 1.00 30.91 C ATOM  124 CG ASN A  21 18.088 49.889 23.918 1.00 34.80 C ATOM  125 OD1 ASN A  21 17.787 49.800 22.721 1.00 34.75 O ATOM  126 ND2 ASN A  21 17.278 49.487 24.900 1.00 35.75 N ATOM  127 N LEU A  22 22.910 49.541 24.579 1.00 26.09 N ATOM  128 CA LEU A  22 24.259 50.055 24.359 1.00 24.16 C ATOM  129 C LEU A  22 24.997 48.954 23.614 1.00 23.68 C ATOM  130 O LEU A  22 24.936 47.802 24.002 1.00 25.86 O ATOM  131 CB LEU A  22 24.970 50.339 25.677 1.00 21.67 C ATOM  132 CG LEU A  22 24.581 51.606 26.436 1.00 23.31 C ATOM  133 CD1 LEU A  22 25.367 51.654 27.735 1.00 22.70 C ATOM  134 CD2 LEU A  22 24.863 52.849 25.576 1.00 22.30 C ATOM  135 N PRO A  23 25.699 49.293 22.530 1.00 25.53 N ATOM  136 CA PRO A  23 26.411 48.232 21.803 1.00 26.11 C ATOM  137 C PRO A  23 27.359 47.413 22.679 1.00 27.55 C ATOM  138 O PRO A  23 28.058 47.961 23.541 1.00 24.70 O ATOM  139 CB PRO A  23 27.123 48.985 20.674 1.00 24.80 C ATOM  140 CG PRO A  23 27.176 50.440 21.169 1.00 27.41 C ATOM  141 CD PRO A  23 25.897 50.620 21.917 1.00 24.42 C ATOM  142 N LYS A  24 27.371 46.099 22.458 1.00 27.34 N ATOM  143 CA LYS A  24 28.220 45.195 23.242 1.00 30.02 C ATOM  144 C LYS A  24 29.719 45.471 23.142 1.00 30.51 C ATOM  145 O LYS A  24 30.450 45.308 24.121 1.00 30.43 O ATOM  146 CB LYS A  24 27.961 43.742 22.840 1.00 30.74 C ATOM  147 CG LYS A  24 26.542 43.262 23.107 1.00 34.37 C ATOM  148 CD LYS A  24 26.346 41.840 22.584 1.00 41.43 C ATOM  149 CE LYS A  24 24.910 41.362 22.785 1.00 43.00 C ATOM  150 NZ LYS A  24 24.527 41.438 24.225 1.00 47.05 N ATOM  151 N ASP A  25 30.173 45.879 21.960 1.00 30.41 N ATOM  152 CA ASP A  25 31.587 46.155 21.734 1.00 31.71 C ATOM  153 C ASP A  25 31.951 47.631 21.953 1.00 33.42 C ATOM  154 O ASP A  25 33.007 48.091 21.522 1.00 33.11 O ATOM  155 CB ASP A  25 31.977 45.711 20.313 1.00 31.70 C ATOM  156 CG ASP A  25 31.118 46.358 19.237 1.00 35.19 C ATOM  157 OD1 ASP A  25 30.109 47.007 19.581 1.00 36.20 O ATOM  158 OD2 ASP A  25 31.446 46.211 18.041 1.00 37.53 O ATOM  159 N TYR A  26 31.075 48.372 22.622 1.00 33.64 N ATOM  160 CA TYR A  26 31.342 49.782 22.895 1.00 34.35 C ATOM  161 C TYR A  26 32.009 49.905 24.262 1.00 34.80 C ATOM  162 O TYR A  26 31.402 49.628 25.297 1.00 35.59 O ATOM  163 CB TYR A  26 30.045 50.588 22.879 1.00 33.06 C ATOM  164 CG TYR A  26 30.249 52.049 23.176 1.00 34.30 C ATOM  165 CD1 TYR A  26 31.007 52.855 22.327 1.00 35.11 C ATOM  166 CD2 TYR A  26 29.677 52.631 24.306 1.00 33.42 C ATOM  167 CE1 TYR A  26 31.188 54.208 22.597 1.00 36.03 C ATOM  168 CE2 TYR A  26 29.847 53.974 24.585 1.00 35.98 C ATOM  169 CZ TYR A  26 30.602 54.761 23.729 1.00 37.37 C ATOM  170 OH TYR A  26 30.745 56.101 24.003 1.00 38.88 O ATOM  171 N MET A  27 33.263 50.334 24.258 1.00 35.01 N ATOM  172 CA MET A  27 34.022 50.467 25.483 1.00 35.27 C ATOM  173 C MET A  27 33.797 51.783 26.227 1.00 33.91 C ATOM  174 O MET A  27 33.930 52.866 25.661 1.00 35.37 O ATOM  175 CB MET A  27 35.509 50.295 25.173 1.00 38.11 C ATOM  176 CG MET A  27 35.827 48.994 24.473 1.00 40.65 C ATOM  177 SD MET A  27 35.230 47.613 25.440 1.00 45.39 S ATOM  178 CE MET A  27 36.529 47.464 26.649 1.00 44.54 C ATOM  179 N ILE A  28 33.452 51.666 27.504 1.00 32.21 N ATOM  180 CA ILE A  28 33.235 52.812 28.377 1.00 29.60 C ATOM  181 C ILE A  28 34.472 52.920 29.264 1.00 28.54 C ATOM  182 O ILE A  28 34.956 51.908 29.776 1.00 26.71 O ATOM  183 CB ILE A  28 32.008 52.611 29.299 1.00 27.09 C ATOM  184 CG1 ILE A  28 30.735 52.462 28.467 1.00 22.92 C ATOM  185 CG2 ILE A  28 31.883 53.801 30.253 1.00 28.05 C ATOM  186 CD1 ILE A  28 29.551 51.907 29.255 1.00 19.41 C ATOM  187 N THR A  29 34.986 54.134 29.439 1.00 27.86 N ATOM  188 CA THR A  29 36.168 54.339 30.274 1.00 30.19 C ATOM  189 C THR A  29 35.818 54.633 31.728 1.00 27.73 C ATOM  190 O THR A  29 34.914 55.412 32.022 1.00 26.96 O ATOM  191 CB THR A  29 37.053 55.491 29.736 1.00 32.36 C ATOM  192 OG1 THR A  29 37.714 55.061 28.537 1.00 37.55 O ATOM  193 CG2 THR A  29 38.107 55.892 30.769 1.00 32.81 C ATOM  194 N LEU A  30 36.548 53.998 32.635 1.00 26.14 N ATOM  195 CA LEU A  30 36.332 54.181 34.061 1.00 27.37 C ATOM  196 C LEU A  30 37.639 54.031 34.835 1.00 28.61 C ATOM  197 O LEU A  30 38.371 53.054 34.666 1.00 27.18 O ATOM  198 CB LEU A  30 35.320 53.153 34.584 1.00 24.35 C ATOM  199 CG LEU A  30 35.225 53.000 36.107 1.00 24.14 C ATOM  200 CD1 LEU A  30 34.569 54.255 36.734 1.00 22.13 C ATOM  201 CD2 LEU A  30 34.428 51.746 36.437 1.00 21.25 C ATOM  202 N LYS A  31 37.934 55.015 35.677 1.00 30.12 N ATOM  203 CA LYS A  31 39.126 54.949 36.504 1.00 31.06 C ATOM  204 C LYS A  31 38.734 54.049 37.662 1.00 31.36 C ATOM  205 O LYS A  31 38.219 54.489 38.688 1.00 30.60 O ATOM  206 CB LYS A  31 39.527 56.351 36.968 1.00 30.41 C ATOM  207 CG LYS A  31 40.114 57.159 35.829 1.00 32.85 C ATOM  208 CD LYS A  31 40.245 58.636 36.136 1.00 37.32 C ATOM  209 CE LYS A  31 40.798 59.359 34.910 1.00 41.56 C ATOM  210 NZ LYS A  31 40.802 60.837 35.049 1.00 48.16 N ATOM  211 N TYR A  32 38.951 52.760 37.441 1.00 33.38 N ATOM  212 CA TYR A  32 38.637 51.702 38.391 1.00 33.81 C ATOM  213 C TYR A  32 39.514 51.758 39.638 1.00 34.38 C ATOM  214 O TYR A  32 40.725 51.937 39.538 1.00 35.35 O ATOM  215 CB TYR A  32 38.839 50.357 37.689 1.00 36.33 C ATOM  216 CG TYR A  32 38.578 49.136 38.534 1.00 36.76 C ATOM  217 CD1 TYR A  32 37.278 48.761 38.858 1.00 36.76 C ATOM  218 CD2 TYR A  32 39.629 48.337 38.983 1.00 37.06 C ATOM  219 CE1 TYR A  32 37.021 47.620 39.606 1.00 39.37 C ATOM  220 CE2 TYR A  32 39.386 47.182 39.740 1.00 37.96 C ATOM  221 CZ TYR A  32 38.075 46.833 40.046 1.00 39.51 C ATOM  222 OH TYR A  32 37.804 45.715 40.798 1.00 39.29 O ATOM  223 N VAL A  33 38.908 51.617 40.813 1.00 34.07 N ATOM  224 CA VAL A  33 39.692 51.607 42.037 1.00 36.48 C ATOM  225 C VAL A  33 40.079 50.159 42.291 1.00 39.60 C ATOM  226 O VAL A  33 39.234 49.324 42.609 1.00 39.23 O ATOM  227 CB VAL A  33 38.909 52.124 43.259 1.00 35.71 C ATOM  228 CG1 VAL A  33 39.733 51.913 44.518 1.00 35.41 C ATOM  229 CG2 VAL A  33 38.597 53.611 43.095 1.00 36.35 C ATOM  230 N PRO A  34 41.367 49.837 42.130 1.00 42.06 N ATOM  231 CA PRO A  34 41.817 48.463 42.357 1.00 43.30 C ATOM  232 C PRO A  34 41.602 48.070 43.815 1.00 44.25 C ATOM  233 O PRO A  34 41.793 48.885 44.719 1.00 45.62 O ATOM  234 CB PRO A  34 43.290 48.515 41.953 1.00 44.82 C ATOM  235 CG PRO A  34 43.685 49.927 42.293 1.00 46.23 C ATOM  236 CD PRO A  34 42.498 50.730 41.812 1.00 43.18 C ATOM  237 N GLY A  35 41.186 46.828 44.037 1.00 44.70 N ATOM  238 CA GLY A  35 40.941 46.361 45.390 1.00 44.83 C ATOM  239 C GLY A  35 39.453 46.290 45.676 1.00 45.03 C ATOM  240 O GLY A  35 39.026 45.681 46.656 1.00 44.02 O ATOM  241 N MET A  36 38.666 46.909 44.798 1.00 46.50 N ATOM  242 CA MET A  36 37.212 46.942 44.929 1.00 47.66 C ATOM  243 C MET A  36 36.600 45.553 45.023 1.00 48.06 C ATOM  244 O MET A  36 35.488 45.393 45.521 1.00 47.40 O ATOM  245 CB MET A  36 36.587 47.657 43.731 1.00 47.93 C ATOM  246 CG MET A  36 35.075 47.720 43.805 1.00 50.30 C ATOM  247 SD MET A  36 34.244 48.051 42.237 1.00 51.54 S ATOM  248 CE MET A  36 32.603 47.354 42.593 1.00 48.10 C ATOM  249 N ASP A  37 37.326 44.553 44.535 1.00 49.01 N ATOM  250 CA ASP A  37 36.843 43.177 44.534 1.00 50.28 C ATOM  251 C ASP A  37 37.333 42.330 45.705 1.00 50.50 C ATOM  252 O ASP A  37 37.091 41.123 45.737 1.00 51.60 O ATOM  253 CB ASP A  37 37.235 42.506 43.215 1.00 51.52 C ATOM  254 CG ASP A  37 38.739 42.529 42.968 1.00 53.79 C ATOM  255 OD1 ASP A  37 39.378 43.583 43.202 1.00 53.58 O ATOM  256 OD2 ASP A  37 39.283 41.492 42.524 1.00 54.54 O ATOM  257 N VAL A  38 38.010 42.957 46.666 1.00 49.28 N ATOM  258 CA VAL A  38 38.536 42.236 47.825 1.00 47.15 C ATOM  259 C VAL A  38 38.533 43.060 49.106 1.00 46.60 C ATOM  260 O VAL A  38 38.300 42.534 50.194 1.00 44.87 O ATOM  261 CB VAL A  38 39.980 41.772 47.576 1.00 45.99 C ATOM  262 CG1 VAL A  38 39.992 40.604 46.617 1.00 47.70 C ATOM  263 CG2 VAL A  38 40.797 42.923 47.016 1.00 45.04 C ATOM  264 N LEU A  39 38.811 44.350 48.977 1.00 45.27 N ATOM  265 CA LEU A  39 38.844 45.226 50.136 1.00 45.37 C ATOM  266 C LEU A  39 37.446 45.557 50.649 1.00 45.34 C ATOM  267 O LEU A  39 36.455 45.427 49.928 1.00 43.74 O ATOM  268 CB LEU A  39 39.559 46.532 49.786 1.00 45.66 C ATOM  269 CG LEU A  39 41.085 46.576 49.709 1.00 47.47 C ATOM  270 CD1 LEU A  39 41.610 45.445 48.841 1.00 49.34 C ATOM  271 CD2 LEU A  39 41.513 47.931 49.150 1.00 45.50 C ATOM  272 N PRO A  40 37.348 45.973 51.921 1.00 45.95 N ATOM  273 CA PRO A  40 36.039 46.324 52.471 1.00 45.59 C ATOM  274 C PRO A  40 35.600 47.603 51.763 1.00 44.61 C ATOM  275 O PRO A  40 36.436 48.364 51.274 1.00 42.94 O ATOM  276 CB PRO A  40 36.331 46.528 53.954 1.00 47.00 C ATOM  277 CG PRO A  40 37.764 46.999 53.946 1.00 48.81 C ATOM  278 CD PRO A  40 38.395 46.070 52.951 1.00 45.63 C ATOM  279 N SER A  41 34.294 47.831 51.708 1.00 44.09 N ATOM  280 CA SER A  41 33.745 48.988 51.019 1.00 44.85 C ATOM  281 C SER A  41 34.251 50.349 51.471 1.00 44.18 C ATOM  282 O SER A  41 34.469 51.233 50.637 1.00 44.01 O ATOM  283 CB SER A  41 32.221 48.971 51.109 1.00 46.19 C ATOM  284 OG SER A  41 31.801 49.153 52.447 1.00 50.69 O ATOM  285 N HIS A  42 34.450 50.528 52.774 1.00 43.90 N ATOM  286 CA HIS A  42 34.907 51.824 53.275 1.00 43.39 C ATOM  287 C HIS A  42 36.261 52.205 52.717 1.00 41.97 C ATOM  288 O HIS A  42 36.696 53.344 52.870 1.00 41.77 O ATOM  289 CB HIS A  42 34.969 51.846 54.809 1.00 45.03 C ATOM  290 CG HIS A  42 36.162 51.148 55.383 1.00 46.34 C ATOM  291 ND1 HIS A  42 36.161 49.806 55.699 1.00 47.87 N ATOM  292 CD2 HIS A  42 37.399 51.607 55.689 1.00 47.30 C ATOM  293 CE1 HIS A  42 37.346 49.468 56.176 1.00 48.29 C ATOM  294 NE2 HIS A  42 38.116 50.542 56.180 1.00 48.92 N ATOM  295 N CYS A  43 36.919 51.252 52.065 1.00 39.35 N ATOM  296 CA CYS A  43 38.234 51.492 51.487 1.00 39.79 C ATOM  297 C CYS A  43 38.171 51.960 50.045 1.00 37.47 C ATOM  298 O CYS A  43 39.160 52.448 49.513 1.00 34.98 O ATOM  299 CB CYS A  43 39.090 50.221 51.533 1.00 45.85 C ATOM  300 SG CYS A  43 39.570 49.651 53.193 1.00 51.16 S ATOM  301 N TRP A  44 37.016 51.823 49.404 1.00 34.72 N ATOM  302 CA TRP A  44 36.931 52.221 48.006 1.00 32.06 C ATOM  303 C TRP A  44 35.641 52.893 47.534 1.00 30.52 C ATOM  304 O TRP A  44 35.642 53.590 46.521 1.00 27.80 O ATOM  305 CB TRP A  44 37.188 50.994 47.127 1.00 31.65 C ATOM  306 CG TRP A  44 36.299 49.824 47.460 1.00 29.05 C ATOM  307 CD1 TRP A  44 36.620 48.743 48.226 1.00 32.56 C ATOM  308 CD2 TRP A  44 34.948 49.624 47.030 1.00 27.71 C ATOM  309 NE1 TRP A  44 35.552 47.874 48.298 1.00 32.12 N ATOM  310 CE2 TRP A  44 34.513 48.392 47.572 1.00 28.95 C ATOM  311 CE3 TRP A  44 34.061 50.366 46.237 1.00 29.91 C ATOM  312 CZ2 TRP A  44 33.230 47.883 47.348 1.00 29.41 C ATOM  313 CZ3 TRP A  44 32.781 49.863 46.010 1.00 30.10 C ATOM  314 CH2 TRP A  44 32.378 48.629 46.565 1.00 29.97 C ATOM  315 N ILE A  45 34.552 52.693 48.264 1.00 31.20 N ATOM  316 CA ILE A  45 33.268 53.236 47.850 1.00 32.95 C ATOM  317 C ILE A  45 33.283 54.722 47.516 1.00 34.02 C ATOM  318 O ILE A  45 32.658 55.144 46.543 1.00 33.17 O ATOM  319 CB ILE A  45 32.178 52.922 48.903 1.00 35.47 C ATOM  320 CG1 ILE A  45 30.810 52.896 48.221 1.00 37.51 C ATOM  321 CG2 ILE A  45 32.220 53.935 50.052 1.00 34.79 C ATOM  322 CD1 ILE A  45 29.720 52.293 49.086 1.00 39.88 C ATOM  323 N SER A  46 34.022 55.509 48.293 1.00 34.50 N ATOM  324 CA SER A  46 34.108 56.945 48.062 1.00 34.72 C ATOM  325 C SER A  46 34.660 57.298 46.682 1.00 33.50 C ATOM  326 O SER A  46 34.049 58.059 45.931 1.00 35.31 O ATOM  327 CB SER A  46 34.979 57.599 49.139 1.00 37.01 C ATOM  328 OG SER A  46 35.062 59.004 48.952 1.00 36.66 O ATOM  329 N GLU A  47 35.817 56.752 46.342 1.00 32.45 N ATOM  330 CA GLU A  47 36.426 57.052 45.051 1.00 30.79 C ATOM  331 C GLU A  47 35.655 56.407 43.898 1.00 28.80 C ATOM  332 O GLU A  47 35.560 56.967 42.815 1.00 28.45 O ATOM  333 CB GLU A  47 37.890 56.586 45.047 1.00 32.29 C ATOM  334 CG GLU A  47 38.739 57.103 43.885 1.00 33.02 C ATOM  335 CD GLU A  47 38.694 58.623 43.750 1.00 35.38 C ATOM  336 OE1 GLU A  47 38.484 59.322 44.765 1.00 34.56 O ATOM  337 OE2 GLU A  47 38.880 59.121 42.622 1.00 37.44 O ATOM  338 N MET A  48 35.102 55.224 44.125 1.00 28.98 N ATOM  339 CA MET A  48 34.347 54.563 43.067 1.00 29.38 C ATOM  340 C MET A  48 33.124 55.371 42.661 1.00 26.16 C ATOM  341 O MET A  48 32.835 55.548 41.474 1.00 25.57 O ATOM  342 CB MET A  48 33.929 53.163 43.510 1.00 30.17 C ATOM  343 CG MET A  48 34.984 52.140 43.181 1.00 35.54 C ATOM  344 SD MET A  48 35.418 52.268 41.419 1.00 41.72 S ATOM  345 CE MET A  48 34.088 51.459 40.712 1.00 37.21 C ATOM  346 N VAL A  49 32.419 55.877 43.658 1.00 24.72 N ATOM  347 CA VAL A  49 31.230 56.664 43.415 1.00 26.13 C ATOM  348 C VAL A  49 31.571 57.936 42.627 1.00 26.91 C ATOM  349 O VAL A  49 30.843 58.328 41.720 1.00 26.96 O ATOM  350 CB VAL A  49 30.536 56.929 44.775 1.00 27.95 C ATOM  351 CG1 VAL A  49 30.127 58.356 44.919 1.00 31.34 C ATOM  352 CG2 VAL A  49 29.345 55.986 44.912 1.00 26.79 C ATOM  353 N VAL A  50 32.711 58.547 42.940 1.00 28.46 N ATOM  354 CA VAL A  50 33.167 59.755 42.246 1.00 26.04 C ATOM  355 C VAL A  50 33.530 59.456 40.795 1.00 24.79 C ATOM  356 O VAL A  50 33.280 60.268 39.888 1.00 24.49 O ATOM  357 CB VAL A  50 34.434 60.343 42.927 1.00 28.79 C ATOM  358 CG1 VAL A  50 35.064 61.428 42.034 1.00 31.79 C ATOM  359 CG2 VAL A  50 34.076 60.916 44.283 1.00 30.83 C ATOM  360 N GLN A  51 34.149 58.299 40.575 1.00 21.97 N ATOM  361 CA GLN A  51 34.556 57.921 39.230 1.00 20.73 C ATOM  362 C GLN A  51 33.372 57.469 38.376 1.00 20.16 C ATOM  363 O GLN A  51 33.330 57.730 37.169 1.00 18.64 O ATOM  364 CB GLN A  51 35.624 56.820 39.281 1.00 23.46 C ATOM  365 CG GLN A  51 36.954 57.225 39.943 1.00 25.10 C ATOM  366 CD GLN A  51 37.537 58.540 39.407 1.00 26.66 C ATOM  367 OE1 GLN A  51 37.426 58.857 38.220 1.00 26.21 O ATOM  368 NE2 GLN A  51 38.175 59.302 40.291 1.00 27.46 N ATOM  369 N LEU A  52 32.413 56.779 38.988 1.00 19.42 N ATOM  370 CA LEU A  52 31.234 56.348 38.233 1.00 20.76 C ATOM  371 C LEU A  52 30.499 57.613 37.797 1.00 22.46 C ATOM  372 O LEU A  52 29.989 57.688 36.684 1.00 25.99 O ATOM  373 CB LEU A  52 30.316 55.470 39.098 1.00 14.75 C ATOM  374 CG LEU A  52 30.913 54.124 39.544 1.00 16.56 C ATOM  375 CD1 LEU A  52 30.008 53.506 40.584 1.00 13.24 C ATOM  376 CD2 LEU A  52 31.094 53.187 38.341 1.00 11.80 C ATOM  377 N SER A  53 30.463 58.613 38.671 1.00 24.81 N ATOM  378 CA SER A  53 29.795 59.877 38.353 1.00 28.85 C ATOM  379 C SER A  53 30.403 60.571 37.142 1.00 29.16 C ATOM  380 O SER A  53 29.681 61.037 36.260 1.00 30.24 O ATOM  381 CB SER A  53 29.842 60.826 39.552 1.00 29.60 C ATOM  382 OG SER A  53 29.572 62.150 39.138 1.00 32.77 O ATOM  383 N ASP A  54 31.729 60.638 37.097 1.00 30.41 N ATOM  384 CA ASP A  54 32.415 61.273 35.980 1.00 31.60 C ATOM  385 C ASP A  54 32.275 60.481 34.681 1.00 31.53 C ATOM  386 O ASP A  54 32.151 61.060 33.595 1.00 31.38 O ATOM  387 CB ASP A  54 33.904 61.465 36.296 1.00 36.88 C ATOM  388 CG ASP A  54 34.685 62.011 35.101 1.00 43.96 C ATOM  389 OD1 ASP A  54 34.214 62.999 34.483 1.00 45.13 O ATOM  390 OD2 ASP A  54 35.767 61.459 34.780 1.00 47.18 O ATOM  391 N SER A  55 32.304 59.158 34.775 1.00 29.76 N ATOM  392 CA SER A  55 32.166 58.350 33.571 1.00 28.65 C ATOM  393 C SER A  55 30.763 58.498 32.994 1.00 27.32 C ATOM  394 O SER A  55 30.593 58.691 31.791 1.00 25.98 O ATOM  395 CB SER A  55 32.441 56.878 33.877 1.00 29.08 C ATOM  396 OG SER A  55 33.829 56.635 33.964 1.00 30.44 O ATOM  397 N LEU A  56 29.765 58.410 33.869 1.00 26.64 N ATOM  398 CA LEU A  56 28.367 58.520 33.466 1.00 25.98 C ATOM  399 C LEU A  56 28.066 59.885 32.882 1.00 27.34 C ATOM  400 O LEU A  56 27.374 59.987 31.875 1.00 27.45 O ATOM  401 CB LEU A  56 27.447 58.255 34.663 1.00 23.93 C ATOM  402 CG LEU A  56 27.346 56.784 35.086 1.00 24.56 C ATOM  403 CD1 LEU A  56 26.606 56.659 36.417 1.00 23.11 C ATOM  404 CD2 LEU A  56 26.643 55.990 33.987 1.00 16.90 C ATOM  405 N THR A  57 28.596 60.934 33.507 1.00 27.77 N ATOM  406 CA THR A  57 28.356 62.286 33.012 1.00 30.04 C ATOM  407 C THR A  57 28.983 62.441 31.630 1.00 30.98 C ATOM  408 O THR A  57 28.386 63.039 30.743 1.00 29.51 O ATOM  409 CB THR A  57 28.936 63.363 33.960 1.00 29.71 C ATOM  410 OG1 THR A  57 28.451 63.150 35.289 1.00 30.34 O ATOM  411 CG2 THR A  57 28.492 64.742 33.514 1.00 33.01 C ATOM  412 N ASP A  58 30.184 61.898 31.447 1.00 34.63 N ATOM  413 CA ASP A  58 30.853 61.973 30.151 1.00 36.67 C ATOM  414 C ASP A  58 30.102 61.115 29.124 1.00 37.45 C ATOM  415 O ASP A  58 30.080 61.429 27.934 1.00 37.92 O ATOM  416 CB ASP A  58 32.307 61.487 30.267 1.00 38.61 C ATOM  417 CG ASP A  58 33.184 62.428 31.097 1.00 44.86 C ATOM  418 OD1 ASP A  58 34.403 62.165 31.223 1.00 46.37 O ATOM  419 OD2 ASP A  58 32.662 63.433 31.630 1.00 48.63 O ATOM  420 N LEU A  59 29.481 60.036 29.594 1.00 37.77 N ATOM  421 CA LEU A  59 28.735 59.128 28.719 1.00 37.88 C ATOM  422 C LEU A  59 27.447 59.817 28.283 1.00 38.34 C ATOM  423 O LEU A  59 26.964 59.634 27.165 1.00 35.35 O ATOM  424 CB LEU A  59 28.423 57.828 29.476 1.00 37.16 C ATOM  425 CG LEU A  59 28.103 56.510 28.750 1.00 39.59 C ATOM  426 CD1 LEU A  59 26.637 56.374 28.565 1.00 37.24 C ATOM  427 CD2 LEU A  59 28.831 56.428 27.414 1.00 38.18 C ATOM  428 N LEU A  60 26.914 60.632 29.182 1.00 39.99 N ATOM  429 CA LEU A  60 25.685 61.364 28.938 1.00 42.03 C ATOM  430 C LEU A  60 25.788 62.336 27.760 1.00 43.49 C ATOM  431 O LEU A  60 24.829 62.522 27.010 1.00 43.75 O ATOM  432 CB LEU A  60 25.291 62.118 30.208 1.00 41.27 C ATOM  433 CG LEU A  60 23.996 62.931 30.171 1.00 43.03 C ATOM  434 CD1 LEU A  60 22.830 62.045 29.746 1.00 40.00 C ATOM  435 CD2 LEU A  60 23.746 63.519 31.556 1.00 41.13 C ATOM  436 N ASP A  61 26.949 62.955 27.587 1.00 45.27 N ATOM  437 CA ASP A  61 27.116 63.904 26.491 1.00 46.56 C ATOM  438 C ASP A  61 27.148 63.215 25.128 1.00 45.61 C ATOM  439 O ASP A  61 27.019 63.866 24.087 1.00 43.88 O ATOM  440 CB ASP A  61 28.397 64.715 26.694 1.00 51.20 C ATOM  441 CG ASP A  61 28.573 65.800 25.644 1.00 56.47 C ATOM  442 OD1 ASP A  61 28.936 65.473 24.490 1.00 57.52 O ATOM  443 OD2 ASP A  61 28.340 66.984 25.975 1.00 59.41 O ATOM  444 N LYS A  62 27.299 61.893 25.136 1.00 43.35 N ATOM  445 CA LYS A  62 27.368 61.130 23.897 1.00 42.66 C ATOM  446 C LYS A  62 26.016 60.770 23.290 1.00 41.38 C ATOM  447 O LYS A  62 25.952 60.226 22.190 1.00 39.37 O ATOM  448 CB LYS A  62 28.203 59.869 24.122 1.00 43.03 C ATOM  449 CG LYS A  62 29.589 60.198 24.636 1.00 44.02 C ATOM  450 CD LYS A  62 30.413 58.960 24.877 1.00 47.44 C ATOM  451 CE LYS A  62 31.784 59.335 25.411 1.00 47.28 C ATOM  452 NZ LYS A  62 32.464 60.280 24.484 1.00 43.52 N ATOM  453 N PHE A  63 24.938 61.091 23.998 1.00 41.93 N ATOM  454 CA PHE A  63 23.595 60.796 23.507 1.00 43.46 C ATOM  455 C PHE A  63 22.748 62.065 23.432 1.00 46.25 C ATOM  456 O PHE A  63 22.971 63.017 24.178 1.00 46.18 O ATOM  457 CB PHE A  63 22.900 59.768 24.417 1.00 40.85 C ATOM  458 CG PHE A  63 23.607 58.442 24.492 1.00 38.31 C ATOM  459 CD1 PHE A  63 24.746 58.286 25.274 1.00 39.31 C ATOM  460 CD2 PHE A  63 23.149 57.353 23.757 1.00 39.73 C ATOM  461 CE1 PHE A  63 25.420 57.065 25.325 1.00 38.30 C ATOM  462 CE2 PHE A  63 23.816 56.128 23.800 1.00 38.66 C ATOM  463 CZ PHE A  63 24.954 55.987 24.586 1.00 38.08 C ATOM  464 N SER A  64 21.776 62.074 22.526 1.00 48.63 N ATOM  465 CA SER A  64 20.890 63.218 22.370 1.00 50.37 C ATOM  466 C SER A  64 19.587 62.934 23.102 1.00 52.06 C ATOM  467 O SER A  64 19.213 61.780 23.296 1.00 51.64 O ATOM  468 CB SER A  64 20.621 63.479 20.893 1.00 49.86 C ATOM  469 OG SER A  64 21.835 63.733 20.205 1.00 52.62 O ATOM  470 N ASN A  65 18.890 63.992 23.493 1.00 54.25 N ATOM  471 CA ASN A  65 17.649 63.856 24.239 1.00 57.80 C ATOM  472 C ASN A  65 16.454 63.355 23.425 1.00 59.71 C ATOM  473 O ASN A  65 16.451 63.421 22.195 1.00 60.42 O ATOM  474 CB ASN A  65 17.315 65.198 24.894 1.00 59.02 C ATOM  475 CG ASN A  65 16.637 65.042 26.241 1.00 60.67 C ATOM  476 OD1 ASN A  65 16.614 65.975 27.050 1.00 61.56 O ATOM  477 ND2 ASN A  65 16.074 63.865 26.490 1.00 61.15 N ATOM  478 N ILE A  66 15.459 62.843 24.153 1.00 61.50 N ATOM  479 CA ILE A  66 14.186 62.305 23.643 1.00 62.44 C ATOM  480 C ILE A  66 13.529 61.546 24.806 1.00 63.95 C ATOM  481 O ILE A  66 12.870 60.519 24.616 1.00 64.12 O ATOM  482 CB ILE A  66 14.365 61.321 22.447 1.00 61.28 C ATOM  483 CG1 ILE A  66 15.643 60.496 22.623 1.00 61.28 C ATOM  484 CG2 ILE A  66 14.337 62.085 21.132 1.00 61.26 C ATOM  485 CD1 ILE A  66 15.873 59.478 21.519 1.00 59.60 C ATOM  486 N SER A  67 13.718 62.085 26.009 1.00 65.07 N ATOM  487 CA SER A  67 13.213 61.514 27.262 1.00 65.71 C ATOM  488 C SER A  67 11.736 61.136 27.338 1.00 65.66 C ATOM  489 O SER A  67 11.220 60.882 28.431 1.00 65.09 O ATOM  490 CB SER A  67 13.534 62.467 28.420 1.00 66.10 C ATOM  491 OG SER A  67 12.963 63.747 28.205 1.00 64.67 O ATOM  492 N GLU A  68 11.058 61.086 26.196 1.00 65.62 N ATOM  493 CA GLU A  68 9.641 60.736 26.182 1.00 65.03 C ATOM  494 C GLU A  68 9.419 59.263 25.815 1.00 63.78 C ATOM  495 O GLU A  68 8.519 58.935 25.040 1.00 63.37 O ATOM  496 CB GLU A  68 8.898 61.640 25.197 1.00 65.93 C ATOM  497 CG GLU A  68 7.406 61.729 25.450 1.00 67.61 C ATOM  498 CD GLU A  68 6.706 62.641 24.464 1.00 68.82 C ATOM  499 OE1 GLU A  68 6.517 62.225 23.299 1.00 68.58 O ATOM  500 OE2 GLU A  68 6.356 63.776 24.857 1.00 68.78 O ATOM  501 N GLY A  69 10.242 58.380 26.376 1.00 62.73 N ATOM  502 CA GLY A  69 10.112 56.960 26.089 1.00 60.38 C ATOM  503 C GLY A  69 11.318 56.129 26.496 1.00 58.08 C ATOM  504 O GLY A  69 11.721 55.220 25.766 1.00 57.97 O ATOM  505 N LEU A  70 11.891 56.449 27.659 1.00 55.78 N ATOM  506 CA LEU A  70 13.061 55.748 28.204 1.00 51.80 C ATOM  507 C LEU A  70 14.243 55.633 27.242 1.00 49.05 C ATOM  508 O LEU A  70 14.664 54.529 26.895 1.00 47.57 O ATOM  509 CB LEU A  70 12.670 54.344 28.669 1.00 53.32 C ATOM  510 CG LEU A  70 11.781 54.192 29.902 1.00 54.23 C ATOM  511 CD1 LEU A  70 11.330 52.742 30.021 1.00 55.04 C ATOM  512 CD2 LEU A  70 12.542 54.631 31.143 1.00 53.18 C ATOM  513 N SER A  71 14.776 56.770 26.812 1.00 45.73 N ATOM  514 CA SER A  71 15.924 56.781 25.912 1.00 41.79 C ATOM  515 C SER A  71 17.195 56.580 26.741 1.00 38.39 C ATOM  516 O SER A  71 17.169 56.692 27.962 1.00 36.09 O ATOM  517 CB SER A  71 16.004 58.122 25.182 1.00 40.37 C ATOM  518 OG SER A  71 16.164 59.185 26.107 1.00 40.70 O ATOM  519 N ASN A  72 18.307 56.286 26.078 1.00 36.35 N ATOM  520 CA ASN A  72 19.559 56.102 26.794 1.00 34.21 C ATOM  521 C ASN A  72 19.874 57.380 27.554 1.00 32.13 C ATOM  522 O ASN A  72 20.222 57.343 28.734 1.00 32.02 O ATOM  523 CB ASN A  72 20.699 55.750 25.823 1.00 33.32 C ATOM  524 CG ASN A  72 20.574 54.334 25.271 1.00 34.31 C ATOM  525 OD1 ASN A  72 19.927 53.489 25.878 1.00 34.94 O ATOM  526 ND2 ASN A  72 21.205 54.068 24.128 1.00 36.96 N ATOM  527 N TYR A  73 19.723 58.511 26.880 1.00 32.21 N ATOM  528 CA TYR A  73 19.986 59.810 27.490 1.00 33.90 C ATOM  529 C TYR A  73 19.269 59.956 28.833 1.00 34.77 C ATOM  530 O TYR A  73 19.876 60.292 29.854 1.00 35.67 O ATOM  531 CB TYR A  73 19.522 60.941 26.557 1.00 34.65 C ATOM  532 CG TYR A  73 19.867 62.324 27.081 1.00 35.46 C ATOM  533 CD1 TYR A  73 21.042 62.965 26.695 1.00 36.50 C ATOM  534 CD2 TYR A  73 19.057 62.951 28.024 1.00 36.48 C ATOM  535 CE1 TYR A  73 21.402 64.196 27.242 1.00 40.10 C ATOM  536 CE2 TYR A  73 19.408 64.175 28.580 1.00 37.06 C ATOM  537 CZ TYR A  73 20.578 64.793 28.189 1.00 40.24 C ATOM  538 OH TYR A  73 20.931 65.999 28.757 1.00 44.57 O ATOM  539 N SER A  74 17.967 59.702 28.820 1.00 34.84 N ATOM  540 CA SER A  74 17.142 59.827 30.014 1.00 35.51 C ATOM  541 C SER A  74 17.541 58.899 31.151 1.00 33.42 C ATOM  542 O SER A  74 17.619 59.317 32.310 1.00 34.04 O ATOM  543 CB SER A  74 15.674 59.599 29.642 1.00 38.11 C ATOM  544 OG SER A  74 15.547 58.459 28.803 1.00 42.69 O ATOM  545 N ILE A  75 17.785 57.637 30.825 1.00 31.51 N ATOM  546 CA ILE A  75 18.167 56.660 31.833 1.00 28.28 C ATOM  547 C ILE A  75 19.512 57.029 32.469 1.00 28.34 C ATOM  548 O ILE A  75 19.673 56.975 33.688 1.00 28.58 O ATOM  549 CB ILE A  75 18.243 55.254 31.203 1.00 28.45 C ATOM  550 CG1 ILE A  75 16.832 54.800 30.812 1.00 27.74 C ATOM  551 CG2 ILE A  75 18.895 54.269 32.174 1.00 25.94 C ATOM  552 CD1 ILE A  75 16.796 53.502 30.039 1.00 26.89 C ATOM  553 N ILE A  76 20.471 57.400 31.632 1.00 27.29 N ATOM  554 CA ILE A  76 21.788 57.787 32.095 1.00 27.88 C ATOM  555 C ILE A  76 21.663 59.010 32.997 1.00 29.70 C ATOM  556 O ILE A  76 22.229 59.046 34.100 1.00 27.15 O ATOM  557 CB ILE A  76 22.694 58.113 30.904 1.00 26.65 C ATOM  558 CG1 ILE A  76 22.845 56.863 30.028 1.00 24.16 C ATOM  559 CG2 ILE A  76 24.053 58.595 31.397 1.00 28.04 C ATOM  560 CD1 ILE A  76 23.625 57.094 28.747 1.00 21.67 C ATOM  561 N ASP A  77 20.914 60.009 32.537 1.00 32.01 N ATOM  562 CA ASP A  77 20.709 61.219 33.338 1.00 34.74 C ATOM  563 C ASP A  77 20.169 60.786 34.701 1.00 33.99 C ATOM  564 O ASP A  77 20.594 61.286 35.738 1.00 34.81 O ATOM  565 CB ASP A  77 19.710 62.158 32.650 1.00 38.27 C ATOM  566 CG ASP A  77 19.685 63.550 33.273 1.00 41.20 C ATOM  567 OD1 ASP A  77 18.592 63.993 33.692 1.00 40.44 O ATOM  568 OD2 ASP A  77 20.754 64.204 33.338 1.00 40.25 O ATOM  569 N LYS A  78 19.249 59.828 34.698 1.00 33.71 N ATOM  570 CA LYS A  78 18.682 59.336 35.952 1.00 34.96 C ATOM  571 C LYS A  78 19.762 58.680 36.824 1.00 34.39 C ATOM  572 O LYS A  78 19.722 58.768 38.060 1.00 33.35 O ATOM  573 CB LYS A  78 17.569 58.319 35.685 1.00 35.88 C ATOM  574 CG LYS A  78 16.930 57.796 36.968 1.00 41.99 C ATOM  575 CD LYS A  78 16.212 56.471 36.767 1.00 46.87 C ATOM  576 CE LYS A  78 15.618 55.961 38.080 1.00 50.42 C ATOM  577 NZ LYS A  78 16.653 55.759 39.140 1.00 51.21 N ATOM  578 N LEU A  79 20.717 58.013 36.182 1.00 31.75 N ATOM  579 CA LEU A  79 21.791 57.358 36.921 1.00 32.48 C ATOM  580 C LEU A  79 22.852 58.371 37.357 1.00 31.83 C ATOM  581 O LEU A  79 23.494 58.205 38.392 1.00 31.52 O ATOM  582 CB LEU A  79 22.410 56.244 36.074 1.00 29.79 C ATOM  583 CG LEU A  79 21.396 55.148 35.706 1.00 27.89 C ATOM  584 CD1 LEU A  79 22.032 54.135 34.757 1.00 29.30 C ATOM  585 CD2 LEU A  79 20.899 54.470 36.978 1.00 25.77 C ATOM  586 N VAL A  80 23.025 59.427 36.573 1.00 32.63 N ATOM  587 CA VAL A  80 23.982 60.460 36.928 1.00 33.72 C ATOM  588 C VAL A  80 23.559 61.094 38.251 1.00 34.77 C ATOM  589 O VAL A  80 24.379 61.298 39.149 1.00 35.56 O ATOM  590 CB VAL A  80 24.049 61.562 35.861 1.00 34.70 C ATOM  591 CG1 VAL A  80 24.734 62.792 36.435 1.00 35.98 C ATOM  592 CG2 VAL A  80 24.812 61.065 34.653 1.00 34.16 C ATOM  593 N ASN A  81 22.269 61.390 38.373 1.00 34.14 N ATOM  594 CA ASN A  81 21.747 62.008 39.584 1.00 33.35 C ATOM  595 C ASN A  81 21.853 61.128 40.824 1.00 32.98 C ATOM  596 O ASN A  81 22.174 61.610 41.914 1.00 32.45 O ATOM  597 CB ASN A  81 20.300 62.432 39.355 1.00 35.05 C ATOM  598 CG ASN A  81 20.147 63.289 38.115 1.00 36.59 C ATOM  599 OD1 ASN A  81 20.902 64.240 37.906 1.00 35.13 O ATOM  600 ND2 ASN A  81 19.169 62.955 37.282 1.00 39.80 N ATOM  601 N ILE A  82 21.584 59.840 40.672 1.00 33.56 N ATOM  602 CA ILE A  82 21.676 58.927 41.806 1.00 33.86 C ATOM  603 C ILE A  82 23.092 58.918 42.372 1.00 32.61 C ATOM  604 O ILE A  82 23.281 59.059 43.576 1.00 32.75 O ATOM  605 CB ILE A  82 21.334 57.482 41.408 1.00 34.33 C ATOM  606 CG1 ILE A  82 19.888 57.396 40.932 1.00 36.95 C ATOM  607 CG2 ILE A  82 21.536 56.563 42.593 1.00 35.34 C ATOM  608 CD1 ILE A  82 19.521 56.046 40.357 1.00 36.95 C ATOM  609 N VAL A  83 24.077 58.767 41.489 1.00 32.99 N ATOM  610 CA VAL A  83 25.484 58.701 41.887 1.00 33.17 C ATOM  611 C VAL A  83 26.003 60.031 42.447 1.00 33.20 C ATOM  612 O VAL A  83 26.795 60.046 43.391 1.00 31.86 O ATOM  613 CB VAL A  83 26.369 58.204 40.689 1.00 32.36 C ATOM  614 CG1 VAL A  83 26.508 59.288 39.642 1.00 34.69 C ATOM  615 CG2 VAL A  83 27.724 57.756 41.176 1.00 32.84 C ATOM  616 N ASP A  84 25.556 61.147 41.881 1.00 33.98 N ATOM  617 CA ASP A  84 25.985 62.445 42.392 1.00 34.87 C ATOM  618 C ASP A  84 25.539 62.619 43.830 1.00 33.82 C ATOM  619 O ASP A  84 26.292 63.135 44.649 1.00 33.58 O ATOM  620 CB ASP A  84 25.428 63.600 41.556 1.00 37.69 C ATOM  621 CG ASP A  84 26.204 63.817 40.275 1.00 41.84 C ATOM  622 OD1 ASP A  84 27.410 63.473 40.255 1.00 44.26 O ATOM  623 OD2 ASP A  84 25.620 64.341 39.298 1.00 42.50 O ATOM  624 N ASP A  85 24.319 62.195 44.147 1.00 33.77 N ATOM  625 CA ASP A  85 23.843 62.330 45.516 1.00 34.83 C ATOM  626 C ASP A  85 24.598 61.405 46.453 1.00 34.94 C ATOM  627 O ASP A  85 24.789 61.722 47.622 1.00 35.58 O ATOM  628 CB ASP A  85 22.338 62.056 45.621 1.00 34.28 C ATOM  629 CG ASP A  85 21.494 63.238 45.159 1.00 34.19 C ATOM  630 OD1 ASP A  85 21.834 64.409 45.479 1.00 35.35 O ATOM  631 OD2 ASP A  85 20.480 62.995 44.483 1.00 31.86 O ATOM  632 N LEU A  86 25.021 60.253 45.950 1.00 35.16 N ATOM  633 CA LEU A  86 25.779 59.331 46.776 1.00 35.91 C ATOM  634 C LEU A  86 27.117 60.003 47.051 1.00 37.76 C ATOM  635 O LEU A  86 27.698 59.853 48.126 1.00 38.30 O ATOM  636 CB LEU A  86 25.988 58.007 46.043 1.00 38.20 C ATOM  637 CG LEU A  86 24.740 57.137 45.912 1.00 37.91 C ATOM  638 CD1 LEU A  86 25.039 55.940 45.016 1.00 36.31 C ATOM  639 CD2 LEU A  86 24.288 56.696 47.308 1.00 36.80 C ATOM  640 N VAL A  87 27.602 60.748 46.066 1.00 38.12 N ATOM  641 CA VAL A  87 28.853 61.468 46.223 1.00 42.55 C ATOM  642 C VAL A  87 28.661 62.462 47.362 1.00 45.41 C ATOM  643 O VAL A  87 29.497 62.575 48.259 1.00 44.45 O ATOM  644 CB VAL A  87 29.208 62.266 44.956 1.00 42.27 C ATOM  645 CG1 VAL A  87 30.362 63.207 45.250 1.00 42.69 C ATOM  646 CG2 VAL A  87 29.549 61.319 43.817 1.00 41.63 C ATOM  647 N GLU A  88 27.550 63.191 47.309 1.00 48.56 N ATOM  648 CA GLU A  88 27.239 64.179 48.330 1.00 52.09 C ATOM  649 C GLU A  88 27.298 63.531 49.699 1.00 54.56 C ATOM  650 O GLU A  88 28.064 63.956 50.560 1.00 54.23 O ATOM  651 CB GLU A  88 25.847 64.761 48.089 1.00 53.28 C ATOM  652 CG GLU A  88 25.791 65.815 46.995 1.00 54.41 C ATOM  653 CD GLU A  88 24.377 66.096 46.532 1.00 55.68 C ATOM  654 OE1 GLU A  88 23.475 66.192 47.387 1.00 58.43 O ATOM  655 OE2 GLU A  88 24.166 66.230 45.312 1.00 58.39 O ATOM  656 N CYS A  89 26.499 62.490 49.890 1.00 57.50 N ATOM  657 CA CYS A  89 26.467 61.792 51.161 1.00 62.27 C ATOM  658 C CYS A  89 27.866 61.420 51.647 1.00 62.66 C ATOM  659 O CYS A  89 28.289 61.839 52.724 1.00 62.85 O ATOM  660 CB CYS A  89 25.601 60.536 51.050 1.00 67.26 C ATOM  661 SG CYS A  89 25.709 59.436 52.501 1.00 78.05 S ATOM  662 N VAL A  90 28.583 60.638 50.849 1.00 62.27 N ATOM  663 CA VAL A  90 29.927 60.210 51.214 1.00 63.33 C ATOM  664 C VAL A  90 30.805 61.341 51.768 1.00 62.95 C ATOM  665 O VAL A  90 31.500 61.159 52.765 1.00 61.82 O ATOM  666 CB VAL A  90 30.628 59.537 50.010 1.00 63.19 C ATOM  667 CG1 VAL A  90 32.103 59.345 50.300 1.00 64.89 C ATOM  668 CG2 VAL A  90 29.981 58.191 49.732 1.00 61.96 C ATOM  669 N LYS A  91 30.773 62.504 51.126 1.00 63.59 N ATOM  670 CA LYS A  91 31.563 63.642 51.587 1.00 64.50 C ATOM  671 C LYS A  91 31.004 64.194 52.893 1.00 65.68 C ATOM  672 O LYS A  91 31.742 64.743 53.712 1.00 65.73 O ATOM  673 CB LYS A  91 31.553 64.766 50.553 1.00 64.42 C ATOM  674 CG LYS A  91 32.276 64.464 49.263 1.00 65.33 C ATOM  675 CD LYS A  91 32.184 65.663 48.337 1.00 66.20 C ATOM  676 CE LYS A  91 32.915 65.423 47.028 1.00 67.45 C ATOM  677 NZ LYS A  91 32.938 66.661 46.200 1.00 67.45 N ATOM  678 N GLU A  92 29.697 64.047 53.080 1.00 66.60 N ATOM  679 CA GLU A  92 29.037 64.553 54.274 1.00 68.25 C ATOM  680 C GLU A  92 29.061 63.561 55.430 1.00 68.30 C ATOM  681 O GLU A  92 29.281 63.944 56.575 1.00 68.42 O ATOM  682 CB GLU A  92 27.591 64.950 53.940 1.00 68.61 C ATOM  683 CG GLU A  92 27.496 65.964 52.791 1.00 71.45 C ATOM  684 CD GLU A  92 26.065 66.347 52.416 1.00 72.08 C ATOM  685 OE1 GLU A  92 25.233 65.437 52.196 1.00 70.81 O ATOM  686 OE2 GLU A  92 25.782 67.564 52.327 1.00 71.57 O ATOM  687 N ASN A  93 28.843 62.286 55.129 1.00 69.10 N ATOM  688 CA ASN A  93 28.832 61.254 56.161 1.00 69.73 C ATOM  689 C ASN A  93 30.151 60.498 56.216 1.00 69.75 C ATOM  690 O ASN A  93 30.178 59.269 56.140 1.00 67.54 O ATOM  691 CB ASN A  93 27.677 60.282 55.914 1.00 70.14 C ATOM  692 CG ASN A  93 26.317 60.936 56.107 1.00 71.63 C ATOM  693 OD1 ASN A  93 26.000 61.420 57.193 1.00 71.75 O ATOM  694 ND2 ASN A  93 25.510 60.956 55.052 1.00 71.69 N ATOM  695 N SER A  94 31.239 61.250 56.366 1.00 71.08 N ATOM  696 CA SER A  94 32.582 60.680 56.420 1.00 72.71 C ATOM  697 C SER A  94 33.074 60.398 57.841 1.00 72.70 C ATOM  698 O SER A  94 32.984 61.248 58.730 1.00 72.27 O ATOM  699 CB SER A  94 33.568 61.608 55.703 1.00 73.81 C ATOM  700 OG SER A  94 33.476 62.940 56.181 1.00 75.51 O ATOM  701 N SER A  95 33.599 59.189 58.031 1.00 72.69 N ATOM  702 CA SER A  95 34.111 58.721 59.316 1.00 72.24 C ATOM  703 C SER A  95 34.363 57.224 59.161 1.00 72.10 C ATOM  704 O SER A  95 33.463 56.484 58.757 1.00 72.07 O ATOM  705 CB SER A  95 33.078 58.963 60.421 1.00 72.42 C ATOM  706 OG SER A  95 31.836 58.353 60.102 1.00 71.47 O ATOM  707 N LYS A  96 35.581 56.781 59.473 1.00 71.80 N ATOM  708 CA LYS A  96 35.948 55.369 59.334 1.00 70.97 C ATOM  709 C LYS A  96 35.941 55.055 57.840 1.00 70.26 C ATOM  710 O LYS A  96 36.373 53.990 57.404 1.00 69.79 O ATOM  711 CB LYS A  96 34.929 54.470 60.043 1.00 71.97 C ATOM  712 CG LYS A  96 34.719 54.773 61.518 1.00 72.65 C ATOM  713 CD LYS A  96 33.535 53.988 62.067 1.00 72.31 C ATOM  714 CE LYS A  96 33.365 54.197 63.563 1.00 72.18 C ATOM  715 NZ LYS A  96 34.501 53.627 64.341 1.00 72.30 N ATOM  716 N ASP A  97 35.435 56.015 57.073 1.00 70.01 N ATOM  717 CA ASP A  97 35.321 55.930 55.623 1.00 69.44 C ATOM  718 C ASP A  97 36.425 56.795 55.011 1.00 68.15 C ATOM  719 O ASP A  97 36.615 57.937 55.427 1.00 67.24 O ATOM  720 CB ASP A  97 33.937 56.449 55.215 1.00 70.94 C ATOM  721 CG ASP A  97 33.650 56.265 53.745 1.00 72.18 C ATOM  722 OD1 ASP A  97 34.271 56.973 52.923 1.00 73.65 O ATOM  723 OD2 ASP A  97 32.800 55.408 53.415 1.00 72.87 O ATOM  724 N LEU A  98 37.157 56.256 54.038 1.00 67.60 N ATOM  725 CA LEU A  98 38.240 57.017 53.415 1.00 68.68 C ATOM  726 C LEU A  98 37.741 58.216 52.616 1.00 69.78 C ATOM  727 O LEU A  98 38.022 58.334 51.423 1.00 69.16 O ATOM  728 CB LEU A  98 39.096 56.121 52.507 1.00 67.38 C ATOM  729 CG LEU A  98 40.061 55.113 53.148 1.00 67.16 C ATOM  730 CD1 LEU A  98 41.063 54.637 52.097 1.00 65.06 C ATOM  731 CD2 LEU A  98 40.807 55.758 54.311 1.00 66.45 C ATOM  732 N LYS A  99 37.010 59.106 53.284 1.00 71.95 N ATOM  733 CA LYS A  99 36.470 60.300 52.641 1.00 73.06 C ATOM  734 C LYS A  99 37.514 60.934 51.733 1.00 73.45 C ATOM  735 O LYS A  99 38.408 61.647 52.188 1.00 74.34 O ATOM  736 CB LYS A  99 36.013 61.324 53.689 1.00 73.26 C ATOM  737 CG LYS A  99 37.123 61.846 54.598 1.00 76.26 C ATOM  738 CD LYS A  99 36.663 63.051 55.420 1.00 78.03 C ATOM  739 CE LYS A  99 37.794 63.598 56.295 1.00 78.42 C ATOM  740 NZ LYS A  99 37.377 64.795 57.091 1.00 77.23 N ATOM  741 N LYS A 100 37.397 60.657 50.440 1.00 74.11 N ATOM  742 CA LYS A 100 38.320 61.197 49.453 1.00 73.86 C ATOM  743 C LYS A 100 39.731 60.728 49.762 1.00 73.67 C ATOM  744 O LYS A 100 39.917 59.744 50.475 1.00 73.41 O ATOM  745 CB LYS A 100 38.255 62.727 49.453 1.00 74.51 C ATOM  746 CG LYS A 100 38.514 63.373 48.097 1.00 75.16 C ATOM  747 CD LYS A 100 38.165 64.857 48.144 1.00 76.21 C ATOM  748 CE LYS A 100 38.280 65.517 46.776 1.00 75.62 C ATOM  749 NZ LYS A 100 37.939 66.967 46.843 1.00 74.24 N ATOM  750 N SER A 101 40.705 61.454 49.222 1.00 73.99 N ATOM  751 CA SER A 101 42.134 61.174 49.366 1.00 74.29 C ATOM  752 C SER A 101 42.577 60.588 48.037 1.00 75.40 C ATOM  753 O SER A 101 42.055 59.561 47.595 1.00 75.14 O ATOM  754 CB SER A 101 42.424 60.165 50.478 1.00 73.98 C ATOM  755 OG SER A 101 42.249 58.840 50.009 1.00 70.78 O ATOM  756 N PHE A 102 43.532 61.255 47.398 1.00 76.34 N ATOM  757 CA PHE A 102 44.047 60.822 46.108 1.00 76.69 C ATOM  758 C PHE A 102 43.071 61.231 45.006 1.00 76.76 C ATOM  759 O PHE A 102 43.028 62.394 44.595 1.00 76.40 O ATOM  760 CB PHE A 102 44.237 59.299 46.092 1.00 75.92 C ATOM  761 CG PHE A 102 45.223 58.823 45.069 1.00 77.00 C ATOM  762 CD1 PHE A 102 46.583 59.073 45.231 1.00 77.34 C ATOM  763 CD2 PHE A 102 44.799 58.129 43.945 1.00 76.96 C ATOM  764 CE1 PHE A 102 47.507 58.638 44.289 1.00 77.66 C ATOM  765 CE2 PHE A 102 45.714 57.688 42.994 1.00 78.03 C ATOM  766 CZ PHE A 102 47.073 57.944 43.167 1.00 78.07 C ATOM  767 N LYS A 103 42.278 60.265 44.555 1.00 76.89 N ATOM  768 CA LYS A 103 41.300 60.467 43.489 1.00 75.84 C ATOM  769 C LYS A 103 42.016 60.600 42.151 1.00 74.97 C ATOM  770 O LYS A 103 42.033 61.670 41.538 1.00 75.72 O ATOM  771 CB LYS A 103 40.434 61.706 43.754 1.00 76.14 C ATOM  772 CG LYS A 103 39.321 61.908 42.727 1.00 75.38 C ATOM  773 CD LYS A 103 38.326 62.977 43.159 1.00 75.24 C ATOM  774 CE LYS A 103 37.647 62.607 44.470 1.00 76.66 C ATOM  775 NZ LYS A 103 36.670 63.644 44.905 1.00 77.05 N ATOM  776 N SER A 104 42.621 59.496 41.720 1.00 73.25 N ATOM  777 CA SER A 104 43.343 59.435 40.457 1.00 70.83 C ATOM  778 C SER A 104 43.823 58.012 40.156 1.00 68.77 C ATOM  779 O SER A 104 44.997 57.790 39.849 1.00 67.79 O ATOM  780 CB SER A 104 44.536 60.396 40.478 1.00 71.12 C ATOM  781 OG SER A 104 45.419 60.096 41.542 1.00 72.02 O ATOM  782 N PRO A 105 42.918 57.023 40.255 1.00 66.86 N ATOM  783 CA PRO A 105 43.317 55.641 39.971 1.00 64.75 C ATOM  784 C PRO A 105 43.604 55.486 38.481 1.00 61.83 C ATOM  785 O PRO A 105 43.587 56.464 37.738 1.00 60.17 O ATOM  786 CB PRO A 105 42.104 54.830 40.429 1.00 64.56 C ATOM  787 CG PRO A 105 40.969 55.755 40.161 1.00 65.66 C ATOM  788 CD PRO A 105 41.499 57.085 40.652 1.00 66.17 C ATOM  789 N GLU A 106 43.864 54.261 38.045 1.00 60.87 N ATOM  790 CA GLU A 106 44.160 54.022 36.640 1.00 59.84 C ATOM  791 C GLU A 106 42.910 53.757 35.812 1.00 57.01 C ATOM  792 O GLU A 106 42.089 52.900 36.151 1.00 55.55 O ATOM  793 CB GLU A 106 45.109 52.838 36.477 1.00 62.12 C ATOM  794 CG GLU A 106 45.608 52.680 35.053 1.00 64.12 C ATOM  795 CD GLU A 106 45.997 51.260 34.728 1.00 64.48 C ATOM  796 OE1 GLU A 106 46.598 51.047 33.656 1.00 65.35 O ATOM  797 OE2 GLU A 106 45.694 50.358 35.539 1.00 64.07 O ATOM  798 N PRO A 107 42.765 54.486 34.700 1.00 54.46 N ATOM  799 CA PRO A 107 41.633 54.374 33.781 1.00 53.06 C ATOM  800 C PRO A 107 41.696 53.166 32.851 1.00 50.35 C ATOM  801 O PRO A 107 42.691 52.962 32.162 1.00 49.73 O ATOM  802 CB PRO A 107 41.702 55.684 33.005 1.00 55.58 C ATOM  803 CG PRO A 107 43.183 55.913 32.905 1.00 54.79 C ATOM  804 CD PRO A 107 43.654 55.595 34.303 1.00 54.48 C ATOM  805 N ARG A 108 40.640 52.359 32.844 1.00 47.27 N ATOM  806 CA ARG A 108 40.589 51.216 31.945 1.00 45.13 C ATOM  807 C ARG A 108 39.271 51.171 31.180 1.00 42.72 C ATOM  808 O ARG A 108 38.344 51.927 31.469 1.00 41.21 O ATOM  809 CB ARG A 108 40.839 49.895 32.688 1.00 46.99 C ATOM  810 CG ARG A 108 40.379 49.829 34.119 1.00 47.99 C ATOM  811 CD ARG A 108 40.904 48.555 34.807 1.00 49.01 C ATOM  812 NE ARG A 108 40.328 47.316 34.274 1.00 48.82 N ATOM  813 CZ ARG A 108 40.335 46.146 34.918 1.00 49.68 C ATOM  814 NH1 ARG A 108 40.887 46.047 36.121 1.00 47.24 N ATOM  815 NH2 ARG A 108 39.775 45.074 34.370 1.00 47.63 N ATOM  816 N LEU A 109 39.196 50.289 30.192 1.00 40.92 N ATOM  817 CA LEU A 109 38.001 50.174 29.375 1.00 38.05 C ATOM  818 C LEU A 109 37.110 49.010 29.788 1.00 36.27 C ATOM  819 O LEU A 109 37.594 47.933 30.134 1.00 36.26 O ATOM  820 CB LEU A 109 38.400 50.037 27.909 1.00 38.61 C ATOM  821 CG LEU A 109 39.249 51.180 27.345 1.00 38.72 C ATOM  822 CD1 LEU A 109 39.475 50.955 25.851 1.00 38.93 C ATOM  823 CD2 LEU A 109 38.545 52.508 27.566 1.00 38.92 C ATOM  824 N PHE A 110 35.801 49.245 29.766 1.00 33.35 N ATOM  825 CA PHE A 110 34.830 48.221 30.135 1.00 31.65 C ATOM  826 C PHE A 110 33.674 48.129 29.146 1.00 31.77 C ATOM  827 O PHE A 110 33.274 49.127 28.520 1.00 29.31 O ATOM  828 CB PHE A 110 34.231 48.494 31.525 1.00 30.30 C ATOM  829 CG PHE A 110 35.226 48.441 32.643 1.00 29.40 C ATOM  830 CD1 PHE A 110 35.999 49.560 32.963 1.00 30.14 C ATOM  831 CD2 PHE A 110 35.427 47.260 33.353 1.00 29.90 C ATOM  832 CE1 PHE A 110 36.964 49.498 33.976 1.00 29.02 C ATOM  833 CE2 PHE A 110 36.392 47.184 34.372 1.00 28.63 C ATOM  834 CZ PHE A 110 37.160 48.304 34.681 1.00 29.05 C ATOM  835 N THR A 111 33.144 46.920 29.003 1.00 28.64 N ATOM  836 CA THR A 111 31.988 46.710 28.139 1.00 27.53 C ATOM  837 C THR A 111 30.832 47.280 28.946 1.00 24.61 C ATOM  838 O THR A 111 30.939 47.436 30.166 1.00 23.79 O ATOM  839 CB THR A 111 31.709 45.207 27.917 1.00 27.63 C ATOM  840 OG1 THR A 111 30.479 45.049 27.198 1.00 37.58 O ATOM  841 CG2 THR A 111 31.560 44.509 29.240 1.00 27.65 C ATOM  842 N PRO A 112 29.718 47.618 28.289 1.00 24.99 N ATOM  843 CA PRO A 112 28.607 48.158 29.078 1.00 25.57 C ATOM  844 C PRO A 112 28.216 47.186 30.206 1.00 27.59 C ATOM  845 O PRO A 112 27.982 47.593 31.348 1.00 27.07 O ATOM  846 CB PRO A 112 27.514 48.340 28.032 1.00 25.52 C ATOM  847 CG PRO A 112 28.320 48.756 26.798 1.00 24.47 C ATOM  848 CD PRO A 112 29.480 47.776 26.840 1.00 24.44 C ATOM  849 N GLU A 113 28.183 45.898 29.880 1.00 29.83 N ATOM  850 CA GLU A 113 27.837 44.850 30.839 1.00 33.19 C ATOM  851 C GLU A 113 28.733 44.907 32.079 1.00 30.68 C ATOM  852 O GLU A 113 28.243 44.928 33.204 1.00 30.34 O ATOM  853 CB GLU A 113 27.981 43.475 30.174 1.00 37.00 C ATOM  854 CG GLU A 113 26.730 42.612 30.231 1.00 45.69 C ATOM  855 CD GLU A 113 26.314 42.255 31.651 1.00 50.82 C ATOM  856 OE1 GLU A 113 25.922 43.167 32.418 1.00 52.22 O ATOM  857 OE2 GLU A 113 26.379 41.054 31.997 1.00 54.13 O ATOM  858 N GLU A 114 30.044 44.907 31.852 1.00 29.98 N ATOM  859 CA GLU A 114 31.041 44.969 32.918 1.00 29.70 C ATOM  860 C GLU A 114 30.951 46.295 33.662 1.00 27.58 C ATOM  861 O GLU A 114 30.993 46.331 34.887 1.00 25.96 O ATOM  862 CB GLU A 114 32.446 44.825 32.332 1.00 33.04 C ATOM  863 CG GLU A 114 32.800 43.427 31.863 1.00 37.74 C ATOM  864 CD GLU A 114 34.018 43.395 30.940 1.00 39.47 C ATOM  865 OE1 GLU A 114 34.524 42.280 30.682 1.00 42.15 O ATOM  866 OE2 GLU A 114 34.461 44.471 30.467 1.00 37.94 O ATOM  867 N PHE A 115 30.833 47.388 32.920 1.00 26.11 N ATOM  868 CA PHE A 115 30.741 48.694 33.555 1.00 27.02 C ATOM  869 C PHE A 115 29.579 48.772 34.542 1.00 26.62 C ATOM  870 O PHE A 115 29.754 49.149 35.700 1.00 25.93 O ATOM  871 CB PHE A 115 30.556 49.794 32.521 1.00 26.88 C ATOM  872 CG PHE A 115 30.456 51.163 33.128 1.00 30.78 C ATOM  873 CD1 PHE A 115 31.591 51.970 33.254 1.00 30.44 C ATOM  874 CD2 PHE A 115 29.236 51.635 33.616 1.00 30.33 C ATOM  875 CE1 PHE A 115 31.509 53.230 33.857 1.00 29.53 C ATOM  876 CE2 PHE A 115 29.143 52.891 34.221 1.00 31.72 C ATOM  877 CZ PHE A 115 30.284 53.691 34.341 1.00 30.73 C ATOM  878 N PHE A 116 28.385 48.424 34.083 1.00 26.41 N ATOM  879 CA PHE A 116 27.225 48.499 34.950 1.00 24.93 C ATOM  880 C PHE A 116 27.144 47.446 36.050 1.00 26.82 C ATOM  881 O PHE A 116 26.349 47.561 36.985 1.00 26.48 O ATOM  882 CB PHE A 116 25.972 48.548 34.093 1.00 21.48 C ATOM  883 CG PHE A 116 25.814 49.857 33.376 1.00 22.31 C ATOM  884 CD1 PHE A 116 26.231 50.004 32.050 1.00 21.26 C ATOM  885 CD2 PHE A 116 25.298 50.972 34.048 1.00 19.11 C ATOM  886 CE1 PHE A 116 26.136 51.232 31.406 1.00 21.62 C ATOM  887 CE2 PHE A 116 25.201 52.210 33.409 1.00 18.12 C ATOM  888 CZ PHE A 116 25.614 52.348 32.095 1.00 17.80 C ATOM  889 N ARG A 117 28.000 46.436 35.958 1.00 29.44 N ATOM  890 CA ARG A 117 28.061 45.400 36.979 1.00 31.66 C ATOM  891 C ARG A 117 28.838 46.065 38.115 1.00 32.46 C ATOM  892 O ARG A 117 28.516 45.900 39.294 1.00 32.67 O ATOM  893 CB ARG A 117 28.832 44.194 36.438 1.00 35.82 C ATOM  894 CG ARG A 117 28.651 42.903 37.210 1.00 39.66 C ATOM  895 CD ARG A 117 28.987 41.725 36.308 1.00 43.82 C ATOM  896 NE ARG A 117 30.354 41.798 35.792 1.00 47.67 N ATOM  897 CZ ARG A 117 30.746 41.285 34.627 1.00 49.48 C ATOM  898 NH1 ARG A 117 29.878 40.660 33.842 1.00 50.53 N ATOM  899 NH2 ARG A 117 32.010 41.398 34.245 1.00 50.55 N ATOM  900 N ILE A 118 29.867 46.821 37.737 1.00 29.93 N ATOM  901 CA ILE A 118 30.689 47.549 38.694 1.00 29.90 C ATOM  902 C ILE A 118 29.807 48.629 39.316 1.00 29.75 C ATOM  903 O ILE A 118 29.908 48.929 40.503 1.00 29.74 O ATOM  904 CB ILE A 118 31.892 48.211 37.989 1.00 28.84 C ATOM  905 CG1 ILE A 118 32.917 47.144 37.613 1.00 30.83 C ATOM  906 CG2 ILE A 118 32.513 49.279 38.881 1.00 26.59 C ATOM  907 CD1 ILE A 118 33.987 47.647 36.674 1.00 31.10 C ATOM  908 N PHE A 119 28.931 49.203 38.501 1.00 30.34 N ATOM  909 CA PHE A 119 28.010 50.233 38.959 1.00 31.08 C ATOM  910 C PHE A 119 27.031 49.710 40.019 1.00 32.65 C ATOM  911 O PHE A 119 26.774 50.371 41.027 1.00 31.33 O ATOM  912 CB PHE A 119 27.208 50.772 37.776 1.00 31.48 C ATOM  913 CG PHE A 119 26.095 51.693 38.176 1.00 32.42 C ATOM  914 CD1 PHE A 119 26.270 53.069 38.142 1.00 31.11 C ATOM  915 CD2 PHE A 119 24.878 51.181 38.625 1.00 31.66 C ATOM  916 CE1 PHE A 119 25.252 53.930 38.551 1.00 30.46 C ATOM  917 CE2 PHE A 119 23.862 52.027 39.034 1.00 33.26 C ATOM  918 CZ PHE A 119 24.051 53.412 38.997 1.00 32.00 C ATOM  919 N ASN A 120 26.465 48.532 39.769 1.00 33.86 N ATOM  920 CA ASN A 120 25.497 47.933 40.684 1.00 32.06 C ATOM  921 C ASN A 120 26.118 47.493 42.009 1.00 31.89 C ATOM  922 O ASN A 120 25.499 47.628 43.066 1.00 27.46 O ATOM  923 CB ASN A 120 24.813 46.740 40.009 1.00 32.78 C ATOM  924 CG ASN A 120 23.845 47.164 38.909 1.00 33.81 C ATOM  925 OD1 ASN A 120 23.476 46.363 38.050 1.00 33.86 O ATOM  926 ND2 ASN A 120 23.419 48.420 38.944 1.00 35.07 N ATOM  927 N ARG A 121 27.332 46.956 41.949 1.00 31.62 N ATOM  928 CA ARG A 121 28.012 46.519 43.157 1.00 34.36 C ATOM  929 C ARG A 121 28.363 47.722 44.023 1.00 35.61 C ATOM  930 O ARG A 121 28.255 47.666 45.249 1.00 33.43 O ATOM  931 CB ARG A 121 29.274 45.711 42.814 1.00 37.30 C ATOM  932 CG ARG A 121 28.962 44.255 42.456 1.00 44.29 C ATOM  933 CD ARG A 121 30.205 43.407 42.180 1.00 51.94 C ATOM  934 NE ARG A 121 30.815 43.668 40.873 1.00 57.49 N ATOM  935 CZ ARG A 121 31.775 42.916 40.334 1.00 61.41 C ATOM  936 NH1 ARG A 121 32.236 41.852 40.990 1.00 62.64 N ATOM  937 NH2 ARG A 121 32.275 43.216 39.137 1.00 62.08 N ATOM  938 N SER A 122 28.768 48.816 43.384 1.00 36.07 N ATOM  939 CA SER A 122 29.113 50.026 44.119 1.00 37.98 C ATOM  940 C SER A 122 27.882 50.557 44.857 1.00 39.98 C ATOM  941 O SER A 122 27.950 50.914 46.037 1.00 37.20 O ATOM  942 CB SER A 122 29.647 51.086 43.155 1.00 38.15 C ATOM  943 OG SER A 122 30.806 50.621 42.481 1.00 36.97 O ATOM  944 N ILE A 123 26.747 50.600 44.169 1.00 42.51 N ATOM  945 CA ILE A 123 25.533 51.095 44.802 1.00 46.25 C ATOM  946 C ILE A 123 24.993 50.111 45.829 1.00 47.13 C ATOM  947 O ILE A 123 24.503 50.507 46.888 1.00 46.85 O ATOM  948 CB ILE A 123 24.463 51.434 43.751 1.00 47.26 C ATOM  949 CG1 ILE A 123 24.838 52.765 43.090 1.00 50.91 C ATOM  950 CG2 ILE A 123 23.084 51.506 44.392 1.00 47.45 C ATOM  951 CD1 ILE A 123 23.836 53.277 42.098 1.00 54.97 C ATOM  952 N ASP A 124 25.096 48.827 45.529 1.00 49.20 N ATOM  953 CA ASP A 124 24.630 47.819 46.467 1.00 52.74 C ATOM  954 C ASP A 124 25.502 47.921 47.717 1.00 54.58 C ATOM  955 O ASP A 124 25.087 47.545 48.810 1.00 55.49 O ATOM  956 CB ASP A 124 24.741 46.422 45.842 1.00 52.44 C ATOM  957 CG ASP A 124 24.404 45.313 46.819 1.00 54.83 C ATOM  958 OD1 ASP A 124 23.274 45.302 47.361 1.00 55.33 O ATOM  959 OD2 ASP A 124 25.275 44.446 47.042 1.00 54.45 O ATOM  960 N ALA A 125 26.707 48.455 47.550 1.00 57.11 N ATOM  961 CA ALA A 125 27.642 48.602 48.660 1.00 60.02 C ATOM  962 C ALA A 125 27.048 49.443 49.780 1.00 62.57 C ATOM  963 O ALA A 125 27.347 49.220 50.950 1.00 61.70 O ATOM  964 CB ALA A 125 28.947 49.222 48.179 1.00 58.07 C ATOM  965 N PHE A 126 26.217 50.417 49.431 1.00 65.62 N ATOM  966 CA PHE A 126 25.600 51.236 50.461 1.00 70.24 C ATOM  967 C PHE A 126 24.527 50.415 51.154 1.00 73.56 C ATOM  968 O PHE A 126 24.498 50.330 52.381 1.00 74.48 O ATOM  969 CB PHE A 126 24.978 52.494 49.866 1.00 69.43 C ATOM  970 CG PHE A 126 25.981 53.477 49.356 1.00 69.16 C ATOM  971 CD1 PHE A 126 26.601 53.285 48.127 1.00 69.83 C ATOM  972 CD2 PHE A 126 26.312 54.597 50.107 1.00 68.36 C ATOM  973 CE1 PHE A 126 27.539 54.200 47.649 1.00 70.13 C ATOM  974 CE2 PHE A 126 27.248 55.517 49.641 1.00 69.60 C ATOM  975 CZ PHE A 126 27.863 55.319 48.410 1.00 70.07 C ATOM  976 N LYS A 127 23.654 49.807 50.357 1.00 77.43 N ATOM  977 CA LYS A 127 22.572 48.974 50.875 1.00 80.53 C ATOM  978 C LYS A 127 22.998 48.235 52.138 1.00 82.15 C ATOM  979 O LYS A 127 22.474 48.481 53.225 1.00 82.37 O ATOM  980 CB LYS A 127 22.144 47.946 49.823 1.00 81.53 C ATOM  981 CG LYS A 127 21.483 48.530 48.588 1.00 83.56 C ATOM  982 CD LYS A 127 20.069 49.007 48.884 1.00 84.91 C ATOM  983 CE LYS A 127 19.376 49.490 47.618 1.00 85.48 C ATOM  984 NZ LYS A 127 17.966 49.903 47.871 1.00 86.48 N ATOM  985 N ASP A 128 23.961 47.334 51.980 1.00 84.12 N ATOM  986 CA ASP A 128 24.461 46.531 53.087 1.00 85.76 C ATOM  987 C ASP A 128 25.830 47.036 53.547 1.00 86.14 C ATOM  988 O ASP A 128 26.860 46.439 53.234 1.00 86.66 O ATOM  989 CB ASP A 128 24.551 45.067 52.641 1.00 87.18 C ATOM  990 CG ASP A 128 23.279 44.586 51.946 1.00 88.36 C ATOM  991 OD1 ASP A 128 22.226 44.474 52.614 1.00 87.93 O ATOM  992 OD2 ASP A 128 23.333 44.326 50.725 1.00 89.41 O ATOM  993 N PHE A 129 25.834 48.134 54.297 1.00 86.40 N ATOM  994 CA PHE A 129 27.075 48.730 54.780 1.00 87.11 C ATOM  995 C PHE A 129 26.903 49.423 56.131 1.00 89.71 C ATOM  996 O PHE A 129 26.196 50.427 56.232 1.00 90.14 O ATOM  997 CB PHE A 129 27.583 49.737 53.745 1.00 84.15 C ATOM  998 CG PHE A 129 28.741 50.573 54.213 1.00 81.11 C ATOM  999 CD1 PHE A 129 29.943 49.983 54.580 1.00 79.96 C ATOM 1000 CD2 PHE A 129 28.631 51.958 54.267 1.00 80.34 C ATOM 1001 CE1 PHE A 129 31.025 50.764 54.994 1.00 79.71 C ATOM 1002 CE2 PHE A 129 29.705 52.747 54.678 1.00 78.88 C ATOM 1003 CZ PHE A 129 30.903 52.150 55.042 1.00 78.87 C ATOM 1004 N VAL A 130 27.557 48.889 57.162 1.00 92.58 N ATOM 1005 CA VAL A 130 27.481 49.464 58.504 1.00 95.55 C ATOM 1006 C VAL A 130 28.826 49.438 59.224 1.00 97.26 C ATOM 1007 O VAL A 130 29.171 50.375 59.945 1.00 97.26 O ATOM 1008 CB VAL A 130 26.460 48.717 59.389 1.00 95.85 C ATOM 1009 CG1 VAL A 130 25.068 48.824 58.786 1.00 96.51 C ATOM 1010 CG2 VAL A 130 26.872 47.262 59.543 1.00 96.16 C ATOM 1011 N VAL A 131 29.579 48.360 59.029 1.00 99.84 N ATOM 1012 CA VAL A 131 30.882 48.210 59.668 1.00 102.46 C ATOM 1013 C VAL A 131 32.028 48.784 58.836 1.00 103.49 C ATOM 1014 O VAL A 131 32.706 48.060 58.104 1.00 103.21 O ATOM 1015 CB VAL A 131 31.184 46.719 59.985 1.00 102.88 C ATOM 1016 CG1 VAL A 131 30.277 46.235 61.104 1.00 103.34 C ATOM 1017 CG2 VAL A 131 30.980 45.861 58.743 1.00 103.19 C ATOM 1018 N ALA A 132 32.239 50.091 58.957 1.00 105.08 N ATOM 1019 CA ALA A 132 33.305 50.763 58.226 1.00 106.69 C ATOM 1020 C ALA A 132 34.662 50.287 58.740 1.00 107.70 C ATOM 1021 O ALA A 132 35.053 49.142 58.505 1.00 108.08 O ATOM 1022 CB ALA A 132 33.179 52.273 58.390 1.00 107.04 C ATOM 1023 N SER A 133 35.374 51.162 59.443 1.00 108.41 N ATOM 1024 CA SER A 133 36.683 50.814 59.985 1.00 108.93 C ATOM 1025 C SER A 133 36.553 49.949 61.233 1.00 109.08 C ATOM 1026 O SER A 133 37.146 48.873 61.316 1.00 109.42 O ATOM 1027 CB SER A 133 37.474 52.080 60.319 1.00 109.04 C ATOM 1028 OG SER A 133 37.762 52.822 59.149 1.00 109.34 O ATOM 1029 N ASP A 137 41.268 48.968 58.587 1.00 83.95 N ATOM 1030 CA ASP A 137 42.374 49.562 57.843 1.00 83.77 C ATOM 1031 C ASP A 137 42.267 49.218 56.364 1.00 81.65 C ATOM 1032 O ASP A 137 41.504 48.332 55.981 1.00 81.87 O ATOM 1033 CB ASP A 137 43.717 49.065 58.394 1.00 86.05 C ATOM 1034 CG ASP A 137 43.883 47.557 58.272 1.00 88.47 C ATOM 1035 OD1 ASP A 137 43.812 47.033 57.138 1.00 88.58 O ATOM 1036 OD2 ASP A 137 44.091 46.894 59.313 1.00 89.29 O ATOM 1037 N CYS A 138 43.040 49.917 55.538 1.00 78.93 N ATOM 1038 CA CYS A 138 43.023 49.683 54.096 1.00 76.20 C ATOM 1039 C CYS A 138 44.422 49.466 53.512 1.00 77.44 C ATOM 1040 O CYS A 138 44.569 49.241 52.307 1.00 77.09 O ATOM 1041 CB CYS A 138 42.353 50.862 53.382 1.00 70.43 C ATOM 1042 SG CYS A 138 40.648 51.212 53.925 1.00 63.65 S ATOM 1043 N VAL A 139 45.439 49.536 54.370 1.00 78.37 N ATOM 1044 CA VAL A 139 46.833 49.358 53.962 1.00 78.39 C ATOM 1045 C VAL A 139 47.356 50.580 53.213 1.00 78.35 C ATOM 1046 O VAL A 139 47.151 50.719 52.007 1.00 78.45 O ATOM 1047 CB VAL A 139 47.005 48.108 53.067 1.00 78.28 C ATOM 1048 CG1 VAL A 139 48.422 48.043 52.523 1.00 79.62 C ATOM 1049 CG2 VAL A 139 46.692 46.856 53.867 1.00 78.33 C TER 1050 VAL A 139 ATOM 1051 N GLY B 202 5.074 53.926 −9.864 1.00 55.94 N ATOM 1052 CA GLY B 202 5.956 53.732 −8.727 1.00 56.16 C ATOM 1053 C GLY B 202 7.260 53.075 −9.131 1.00 56.05 C ATOM 1054 O GLY B 202 7.265 52.063 −9.833 1.00 55.94 O ATOM 1055 N ILE B 203 8.373 53.652 −8.692 1.00 56.92 N ATOM 1056 CA ILE B 203 9.686 53.106 −9.017 1.00 57.39 C ATOM 1057 C ILE B 203 10.204 52.286 −7.842 1.00 59.41 C ATOM 1058 O ILE B 203 10.614 52.862 −6.828 1.00 60.09 O ATOM 1059 CB ILE B 203 10.706 54.226 −9.298 1.00 56.02 C ATOM 1060 CG1 ILE B 203 10.124 55.231 −10.295 1.00 55.36 C ATOM 1061 CG2 ILE B 203 12.004 53.619 −9.838 1.00 55.71 C ATOM 1062 CD1 ILE B 203 11.049 56.410 −10.594 1.00 53.98 C ATOM 1063 N CYS B 204 10.192 50.957 −7.978 1.00 60.84 N ATOM 1064 CA CYS B 204 10.667 50.061 −6.915 1.00 62.54 C ATOM 1065 C CYS B 204 10.340 50.704 −5.563 1.00 61.09 C ATOM 1066 O CYS B 204 11.195 50.815 −4.683 1.00 61.84 O ATOM 1067 CB CYS B 204 12.191 49.818 −7.068 1.00 66.33 C ATOM 1068 SG CYS B 204 13.033 48.997 −5.663 1.00 73.54 S ATOM 1069 N ARG B 205 9.092 51.148 −5.423 1.00 59.31 N ATOM 1070 CA ARG B 205 8.623 51.799 −4.200 1.00 57.61 C ATOM 1071 C ARG B 205 7.697 50.895 −3.390 1.00 58.14 C ATOM 1072 O ARG B 205 6.770 51.363 −2.723 1.00 58.84 O ATOM 1073 CB ARG B 205 7.897 53.103 −4.548 1.00 55.04 C ATOM 1074 CG ARG B 205 8.829 54.255 −4.882 1.00 53.30 C ATOM 1075 CD ARG B 205 9.663 54.623 −3.662 1.00 51.85 C ATOM 1076 NE ARG B 205 10.694 55.614 −3.959 1.00 51.10 N ATOM 1077 CZ ARG B 205 10.455 56.878 −4.304 1.00 52.18 C ATOM 1078 NH1 ARG B 205 9.207 57.326 −4.402 1.00 50.83 N ATOM 1079 NH2 ARG B 205 11.470 57.699 −4.549 1.00 51.90 N ATOM 1080 N ASN B 206 7.963 49.597 −3.457 1.00 57.68 N ATOM 1081 CA ASN B 206 7.177 48.600 −2.747 1.00 57.99 C ATOM 1082 C ASN B 206 7.799 48.464 −1.372 1.00 58.60 C ATOM 1083 O ASN B 206 8.941 48.009 −1.256 1.00 59.53 O ATOM 1084 CB ASN B 206 7.265 47.275 −3.490 1.00 58.87 C ATOM 1085 CG ASN B 206 7.246 47.465 −4.991 1.00 60.42 C ATOM 1086 OD1 ASN B 206 6.220 47.837 −5.568 1.00 60.92 O ATOM 1087 ND2 ASN B 206 8.393 47.234 −5.634 1.00 61.57 N ATOM 1088 N ARG B 207 7.054 48.859 −0.340 1.00 57.82 N ATOM 1089 CA ARG B 207 7.544 48.808 1.037 1.00 57.03 C ATOM 1090 C ARG B 207 8.912 49.498 1.053 1.00 58.08 C ATOM 1091 O ARG B 207 9.773 49.210 1.894 1.00 57.11 O ATOM 1092 CB ARG B 207 7.649 47.346 1.521 1.00 55.63 C ATOM 1093 CG ARG B 207 8.750 46.525 0.856 1.00 52.82 C ATOM 1094 CD ARG B 207 8.631 45.020 1.100 1.00 52.16 C ATOM 1095 NE ARG B 207 8.902 44.625 2.480 1.00 49.34 N ATOM 1096 CZ ARG B 207 9.331 43.414 2.827 1.00 50.30 C ATOM 1097 NH1 ARG B 207 9.544 42.494 1.892 1.00 51.49 N ATOM 1098 NH2 ARG B 207 9.533 43.112 4.104 1.00 51.05 N ATOM 1099 N VAL B 208 9.089 50.422 0.107 1.00 58.69 N ATOM 1100 CA VAL B 208 10.338 51.161 −0.043 1.00 59.57 C ATOM 1101 C VAL B 208 10.269 52.566 0.556 1.00 60.47 C ATOM 1102 O VAL B 208 10.764 53.535 −0.031 1.00 59.70 O ATOM 1103 CB VAL B 208 10.732 51.256 −1.535 1.00 58.68 C ATOM 1104 CG1 VAL B 208 12.100 51.912 −1.687 1.00 56.09 C ATOM 1105 CG2 VAL B 208 10.752 49.864 −2.142 1.00 56.94 C ATOM 1106 N THR B 209 9.648 52.674 1.727 1.00 61.79 N ATOM 1107 CA THR B 209 9.543 53.957 2.411 1.00 64.19 C ATOM 1108 C THR B 209 10.441 53.909 3.638 1.00 65.48 C ATOM 1109 O THR B 209 10.082 53.327 4.666 1.00 66.03 O ATOM 1110 CB THR B 209 8.096 54.249 2.850 1.00 64.54 C ATOM 1111 OG1 THR B 209 7.258 54.339 1.691 1.00 66.58 O ATOM 1112 CG2 THR B 209 8.025 55.563 3.619 1.00 64.63 C ATOM 1113 N ASN B 210 11.616 54.519 3.514 1.00 67.03 N ATOM 1114 CA ASN B 210 12.600 54.555 4.592 1.00 68.22 C ATOM 1115 C ASN B 210 12.085 55.139 5.907 1.00 69.19 C ATOM 1116 O ASN B 210 12.135 54.478 6.948 1.00 69.69 O ATOM 1117 CB ASN B 210 13.836 55.330 4.132 1.00 67.77 C ATOM 1118 CG ASN B 210 14.748 55.710 5.280 1.00 68.67 C ATOM 1119 OD1 ASN B 210 14.953 54.931 6.212 1.00 67.36 O ATOM 1120 ND2 ASN B 210 15.312 56.913 5.214 1.00 69.95 N ATOM 1121 N ASN B 211 11.599 56.376 5.862 1.00 69.70 N ATOM 1122 CA ASN B 211 11.089 57.040 7.059 1.00 69.97 C ATOM 1123 C ASN B 211 12.224 57.278 8.050 1.00 69.52 C ATOM 1124 O ASN B 211 12.468 56.470 8.950 1.00 69.57 O ATOM 1125 CB ASN B 211 10.000 56.188 7.707 1.00 70.79 C ATOM 1126 CG ASN B 211 8.873 55.870 6.750 1.00 71.27 C ATOM 1127 OD1 ASN B 211 8.127 56.757 6.334 1.00 71.14 O ATOM 1128 ND2 ASN B 211 8.751 54.601 6.385 1.00 71.65 N ATOM 1129 N VAL B 212 12.914 58.398 7.867 1.00 68.75 N ATOM 1130 CA VAL B 212 14.036 58.772 8.719 1.00 67.00 C ATOM 1131 C VAL B 212 13.647 59.074 10.168 1.00 65.19 C ATOM 1132 O VAL B 212 14.513 59.328 11.001 1.00 63.87 O ATOM 1133 CB VAL B 212 14.785 59.994 8.133 1.00 67.35 C ATOM 1134 CG1 VAL B 212 15.791 59.537 7.087 1.00 67.33 C ATOM 1135 CG2 VAL B 212 13.789 60.957 7.503 1.00 66.47 C ATOM 1136 N LYS B 213 12.350 59.049 10.465 1.00 63.78 N ATOM 1137 CA LYS B 213 11.880 59.307 11.827 1.00 61.90 C ATOM 1138 C LYS B 213 12.570 58.335 12.778 1.00 59.48 C ATOM 1139 O LYS B 213 13.009 58.715 13.866 1.00 58.25 O ATOM 1140 CB LYS B 213 10.360 59.119 11.922 1.00 63.24 C ATOM 1141 CG LYS B 213 9.551 60.117 11.096 1.00 66.28 C ATOM 1142 CD LYS B 213 8.053 59.861 11.206 1.00 66.69 C ATOM 1143 CE LYS B 213 7.264 60.822 10.327 1.00 66.77 C ATOM 1144 NZ LYS B 213 5.829 60.439 10.227 1.00 66.50 N ATOM 1145 N ASP B 214 12.664 57.079 12.352 1.00 56.30 N ATOM 1146 CA ASP B 214 13.302 56.043 13.152 1.00 53.09 C ATOM 1147 C ASP B 214 14.816 56.184 13.114 1.00 49.43 C ATOM 1148 O ASP B 214 15.497 55.934 14.107 1.00 48.27 O ATOM 1149 CB ASP B 214 12.897 54.660 12.642 1.00 55.83 C ATOM 1150 CG ASP B 214 11.399 54.413 12.750 1.00 57.66 C ATOM 1151 OD1 ASP B 214 10.834 54.665 13.838 1.00 57.31 O ATOM 1152 OD2 ASP B 214 10.793 53.961 11.751 1.00 58.37 O ATOM 1153 N VAL B 215 15.338 56.595 11.966 1.00 45.60 N ATOM 1154 CA VAL B 215 16.770 56.767 11.807 1.00 44.22 C ATOM 1155 C VAL B 215 17.346 57.816 12.758 1.00 43.86 C ATOM 1156 O VAL B 215 18.345 57.562 13.430 1.00 44.52 O ATOM 1157 CB VAL B 215 17.117 57.143 10.360 1.00 43.83 C ATOM 1158 CG1 VAL B 215 18.617 57.350 10.213 1.00 44.99 C ATOM 1159 CG2 VAL B 215 16.657 56.041 9.429 1.00 46.16 C ATOM 1160 N THR B 216 16.714 58.984 12.835 1.00 42.82 N ATOM 1161 CA THR B 216 17.217 60.035 13.712 1.00 41.68 C ATOM 1162 C THR B 216 17.180 59.558 15.155 1.00 40.38 C ATOM 1163 O THR B 216 18.121 59.782 15.919 1.00 40.92 O ATOM 1164 CB THR B 216 16.390 61.352 13.591 1.00 41.64 C ATOM 1165 OG1 THR B 216 15.206 61.258 14.387 1.00 42.85 O ATOM 1166 CG2 THR B 216 15.992 61.603 12.149 1.00 40.73 C ATOM 1167 N LYS B 217 16.090 58.892 15.520 1.00 39.71 N ATOM 1168 CA LYS B 217 15.932 58.371 16.871 1.00 38.63 C ATOM 1169 C LYS B 217 17.064 57.411 17.236 1.00 35.12 C ATOM 1170 O LYS B 217 17.544 57.413 18.369 1.00 32.67 O ATOM 1171 CB LYS B 217 14.590 57.646 17.004 1.00 42.48 C ATOM 1172 CG LYS B 217 13.393 58.572 16.969 1.00 48.85 C ATOM 1173 CD LYS B 217 12.093 57.817 17.224 1.00 50.93 C ATOM 1174 CE LYS B 217 10.903 58.768 17.218 1.00 52.56 C ATOM 1175 NZ LYS B 217 9.633 58.065 17.555 1.00 53.57 N ATOM 1176 N LEU B 218 17.477 56.592 16.271 1.00 32.67 N ATOM 1177 CA LEU B 218 18.551 55.622 16.482 1.00 32.18 C ATOM 1178 C LEU B 218 19.886 56.328 16.639 1.00 31.65 C ATOM 1179 O LEU B 218 20.659 56.006 17.536 1.00 30.79 O ATOM 1180 CB LEU B 218 18.638 54.648 15.306 1.00 30.41 C ATOM 1181 CG LEU B 218 19.718 53.570 15.339 1.00 26.12 C ATOM 1182 CD1 LEU B 218 19.499 52.659 16.520 1.00 26.45 C ATOM 1183 CD2 LEU B 218 19.671 52.771 14.039 1.00 28.84 C ATOM 1184 N VAL B 219 20.166 57.280 15.757 1.00 31.46 N ATOM 1185 CA VAL B 219 21.417 58.015 15.853 1.00 32.60 C ATOM 1186 C VAL B 219 21.466 58.673 17.242 1.00 32.42 C ATOM 1187 O VAL B 219 22.508 58.701 17.893 1.00 32.49 O ATOM 1188 CB VAL B 219 21.507 59.077 14.737 1.00 35.95 C ATOM 1189 CG1 VAL B 219 22.780 59.917 14.893 1.00 37.54 C ATOM 1190 CG2 VAL B 219 21.497 58.385 13.379 1.00 35.28 C ATOM 1191 N ALA B 220 20.318 59.171 17.691 1.00 30.69 N ATOM 1192 CA ALA B 220 20.186 59.809 19.002 1.00 31.19 C ATOM 1193 C ALA B 220 20.382 58.804 20.140 1.00 31.91 C ATOM 1194 O ALA B 220 20.742 59.174 21.265 1.00 30.98 O ATOM 1195 CB ALA B 220 18.801 60.440 19.125 1.00 28.27 C ATOM 1196 N ASN B 221 20.136 57.531 19.848 1.00 30.80 N ATOM 1197 CA ASN B 221 20.261 56.498 20.864 1.00 31.97 C ATOM 1198 C ASN B 221 21.549 55.694 20.723 1.00 31.15 C ATOM 1199 O ASN B 221 21.739 54.673 21.377 1.00 30.13 O ATOM 1200 CB ASN B 221 19.055 55.578 20.800 1.00 33.04 C ATOM 1201 CG ASN B 221 18.673 55.058 22.142 1.00 37.25 C ATOM 1202 OD1 ASN B 221 18.517 55.829 23.087 1.00 38.33 O ATOM 1203 ND2 ASN B 221 18.514 53.743 22.249 1.00 39.86 N ATOM 1204 N LEU B 222 22.425 56.178 19.856 1.00 30.64 N ATOM 1205 CA LEU B 222 23.709 55.557 19.609 1.00 31.59 C ATOM 1206 C LEU B 222 24.774 56.559 20.047 1.00 33.54 C ATOM 1207 O LEU B 222 24.679 57.753 19.748 1.00 34.13 O ATOM 1208 CB LEU B 222 23.858 55.266 18.118 1.00 31.84 C ATOM 1209 CG LEU B 222 23.960 53.842 17.562 1.00 32.43 C ATOM 1210 CD1 LEU B 222 23.326 52.794 18.478 1.00 29.84 C ATOM 1211 CD2 LEU B 222 23.292 53.866 16.202 1.00 31.79 C ATOM 1212 N PRO B 223 25.785 56.100 20.789 1.00 34.21 N ATOM 1213 CA PRO B 223 26.819 57.049 21.209 1.00 34.42 C ATOM 1214 C PRO B 223 27.514 57.665 19.989 1.00 35.75 C ATOM 1215 O PRO B 223 27.888 56.949 19.049 1.00 34.36 O ATOM 1216 CB PRO B 223 27.759 56.190 22.062 1.00 34.97 C ATOM 1217 CG PRO B 223 27.518 54.775 21.556 1.00 35.82 C ATOM 1218 CD PRO B 223 26.041 54.747 21.314 1.00 34.53 C ATOM 1219 N LYS B 224 27.660 58.991 19.998 1.00 35.36 N ATOM 1220 CA LYS B 224 28.309 59.711 18.897 1.00 38.46 C ATOM 1221 C LYS B 224 29.735 59.206 18.791 1.00 38.58 C ATOM 1222 O LYS B 224 30.443 59.479 17.829 1.00 39.76 O ATOM 1223 CB LYS B 224 28.344 61.216 19.182 1.00 40.17 C ATOM 1224 CG LYS B 224 27.035 61.801 19.670 1.00 44.14 C ATOM 1225 CD LYS B 224 27.237 63.221 20.168 1.00 47.87 C ATOM 1226 CE LYS B 224 25.980 63.755 20.843 1.00 51.17 C ATOM 1227 NZ LYS B 224 26.174 65.142 21.361 1.00 52.59 N ATOM 1228 N ASP B 225 30.132 58.468 19.815 1.00 40.23 N ATOM 1229 CA ASP B 225 31.456 57.890 19.951 1.00 41.59 C ATOM 1230 C ASP B 225 31.577 56.525 19.244 1.00 39.50 C ATOM 1231 O ASP B 225 32.676 56.097 18.888 1.00 37.57 O ATOM 1232 CB ASP B 225 31.726 57.712 21.448 1.00 44.75 C ATOM 1233 CG ASP B 225 33.193 57.637 21.777 1.00 49.61 C ATOM 1234 OD1 ASP B 225 33.918 56.837 21.145 1.00 54.59 O ATOM 1235 OD2 ASP B 225 33.620 58.376 22.687 1.00 52.53 O ATOM 1236 N TYR B 226 30.448 55.847 19.045 1.00 37.50 N ATOM 1237 CA TYR B 226 30.445 54.514 18.442 1.00 36.48 C ATOM 1238 C TYR B 226 30.892 54.451 16.991 1.00 35.68 C ATOM 1239 O TYR B 226 30.374 55.169 16.143 1.00 35.54 O ATOM 1240 CB TYR B 226 29.053 53.886 18.560 1.00 37.65 C ATOM 1241 CG TYR B 226 29.037 52.396 18.288 1.00 38.60 C ATOM 1242 CD1 TYR B 226 28.039 51.822 17.500 1.00 37.85 C ATOM 1243 CD2 TYR B 226 30.007 51.556 18.842 1.00 37.09 C ATOM 1244 CE1 TYR B 226 28.005 50.440 17.270 1.00 38.79 C ATOM 1245 CE2 TYR B 226 29.986 50.179 18.621 1.00 39.41 C ATOM 1246 CZ TYR B 226 28.981 49.626 17.833 1.00 38.69 C ATOM 1247 OH TYR B 226 28.957 48.268 17.607 1.00 39.90 O ATOM 1248 N MET B 227 31.838 53.562 16.706 1.00 36.10 N ATOM 1249 CA MET B 227 32.356 53.406 15.351 1.00 37.09 C ATOM 1250 C MET B 227 31.756 52.198 14.641 1.00 36.12 C ATOM 1251 O MET B 227 31.842 51.066 15.123 1.00 33.71 O ATOM 1252 CB MET B 227 33.881 53.290 15.382 1.00 41.32 C ATOM 1253 CG MET B 227 34.600 54.437 14.688 1.00 48.18 C ATOM 1254 SD MET B 227 33.881 56.053 15.088 1.00 54.24 S ATOM 1255 CE MET B 227 34.682 56.402 16.647 1.00 56.04 C ATOM 1256 N ILE B 228 31.156 52.454 13.481 1.00 35.08 N ATOM 1257 CA ILE B 228 30.521 51.416 12.683 1.00 33.44 C ATOM 1258 C ILE B 228 31.320 51.080 11.425 1.00 33.56 C ATOM 1259 O ILE B 228 31.733 51.971 10.687 1.00 32.95 O ATOM 1260 CB ILE B 228 29.107 51.859 12.262 1.00 31.75 C ATOM 1261 CG1 ILE B 228 28.248 52.077 13.509 1.00 30.42 C ATOM 1262 CG2 ILE B 228 28.493 50.832 11.320 1.00 30.01 C ATOM 1263 CD1 ILE B 228 26.900 52.710 13.224 1.00 28.35 C ATOM 1264 N THR B 229 31.513 49.789 11.172 1.00 33.75 N ATOM 1265 CA THR B 229 32.257 49.355 9.993 1.00 35.22 C ATOM 1266 C THR B 229 31.384 49.209 8.744 1.00 36.26 C ATOM 1267 O THR B 229 30.273 48.666 8.791 1.00 34.96 O ATOM 1268 CB THR B 229 32.970 48.018 10.248 1.00 36.26 C ATOM 1269 OG1 THR B 229 33.897 48.172 11.333 1.00 39.29 O ATOM 1270 CG2 THR B 229 33.718 47.566 8.995 1.00 35.93 C ATOM 1271 N LEU B 230 31.910 49.692 7.624 1.00 35.74 N ATOM 1272 CA LEU B 230 31.212 49.633 6.353 1.00 35.46 C ATOM 1273 C LEU B 230 32.210 49.587 5.190 1.00 37.16 C ATOM 1274 O LEU B 230 33.125 50.416 5.114 1.00 37.17 O ATOM 1275 CB LEU B 230 30.297 50.859 6.212 1.00 33.47 C ATOM 1276 CG LEU B 230 29.543 51.079 4.889 1.00 33.44 C ATOM 1277 CD1 LEU B 230 28.564 49.935 4.637 1.00 27.86 C ATOM 1278 CD2 LEU B 230 28.809 52.419 4.932 1.00 31.24 C ATOM 1279 N LYS B 231 32.054 48.605 4.302 1.00 38.67 N ATOM 1280 CA LYS B 231 32.927 48.512 3.134 1.00 41.23 C ATOM 1281 C LYS B 231 32.424 49.588 2.183 1.00 42.27 C ATOM 1282 O LYS B 231 31.504 49.364 1.398 1.00 41.26 O ATOM 1283 CB LYS B 231 32.829 47.133 2.481 1.00 41.80 C ATOM 1284 CG LYS B 231 33.541 46.035 3.257 1.00 45.00 C ATOM 1285 CD LYS B 231 33.579 44.737 2.459 1.00 48.11 C ATOM 1286 CE LYS B 231 34.274 43.619 3.231 1.00 50.40 C ATOM 1287 NZ LYS B 231 33.580 43.304 4.511 1.00 51.63 N ATOM 1288 N TYR B 232 33.043 50.760 2.283 1.00 44.81 N ATOM 1289 CA TYR B 232 32.683 51.943 1.508 1.00 47.65 C ATOM 1290 C TYR B 232 33.298 52.021 0.109 1.00 50.22 C ATOM 1291 O TYR B 232 34.508 51.822 −0.063 1.00 50.37 O ATOM 1292 CB TYR B 232 33.090 53.179 2.317 1.00 48.36 C ATOM 1293 CG TYR B 232 32.681 54.521 1.748 1.00 50.47 C ATOM 1294 CD1 TYR B 232 31.438 55.084 2.048 1.00 51.76 C ATOM 1295 CD2 TYR B 232 33.564 55.261 0.962 1.00 51.08 C ATOM 1296 CE1 TYR B 232 31.088 56.361 1.584 1.00 50.40 C ATOM 1297 CE2 TYR B 232 33.226 56.534 0.492 1.00 50.25 C ATOM 1298 CZ TYR B 232 31.992 57.079 0.809 1.00 51.25 C ATOM 1299 OH TYR B 232 31.677 58.350 0.369 1.00 50.44 O ATOM 1300 N VAL B 233 32.456 52.319 −0.883 1.00 51.48 N ATOM 1301 CA VAL B 233 32.911 52.472 −2.265 1.00 53.29 C ATOM 1302 C VAL B 233 33.562 53.856 −2.389 1.00 54.21 C ATOM 1303 O VAL B 233 32.896 54.884 −2.255 1.00 54.14 O ATOM 1304 CB VAL B 233 31.741 52.378 −3.272 1.00 53.48 C ATOM 1305 CG1 VAL B 233 32.276 52.433 −4.690 1.00 52.85 C ATOM 1306 CG2 VAL B 233 30.969 51.089 −3.060 1.00 54.00 C ATOM 1307 N PRO B 234 34.876 53.888 −2.658 1.00 55.55 N ATOM 1308 CA PRO B 234 35.736 55.064 −2.815 1.00 56.44 C ATOM 1309 C PRO B 234 35.161 56.459 −3.101 1.00 57.04 C ATOM 1310 O PRO B 234 35.372 57.379 −2.305 1.00 57.54 O ATOM 1311 CB PRO B 234 36.720 54.606 −3.874 1.00 57.14 C ATOM 1312 CG PRO B 234 36.989 53.204 −3.415 1.00 56.28 C ATOM 1313 CD PRO B 234 35.595 52.676 −3.100 1.00 55.40 C ATOM 1314 N GLY B 235 34.447 56.642 −4.208 1.00 56.12 N ATOM 1315 CA GLY B 235 33.943 57.979 −4.490 1.00 54.89 C ATOM 1316 C GLY B 235 32.469 58.134 −4.786 1.00 53.88 C ATOM 1317 O GLY B 235 32.083 58.925 −5.646 1.00 55.02 O ATOM 1318 N MET B 236 31.635 57.405 −4.062 1.00 53.22 N ATOM 1319 CA MET B 236 30.200 57.471 −4.283 1.00 52.92 C ATOM 1320 C MET B 236 29.595 58.845 −4.028 1.00 52.29 C ATOM 1321 O MET B 236 28.406 59.054 −4.250 1.00 51.46 O ATOM 1322 CB MET B 236 29.495 56.428 −3.419 1.00 53.98 C ATOM 1323 CG MET B 236 29.893 56.458 −1.957 1.00 55.72 C ATOM 1324 SD MET B 236 28.808 55.402 −0.984 1.00 58.44 S ATOM 1325 CE MET B 236 27.500 56.579 −0.565 1.00 54.06 C ATOM 1326 N ASP B 237 30.409 59.786 −3.567 1.00 53.17 N ATOM 1327 CA ASP B 237 29.912 61.130 −3.294 1.00 53.05 C ATOM 1328 C ASP B 237 29.905 62.043 −4.522 1.00 51.90 C ATOM 1329 O ASP B 237 29.208 63.058 −4.529 1.00 52.18 O ATOM 1330 CB ASP B 237 30.724 61.772 −2.168 1.00 54.57 C ATOM 1331 CG ASP B 237 32.211 61.560 −2.333 1.00 56.22 C ATOM 1332 OD1 ASP B 237 32.628 60.389 −2.453 1.00 56.92 O ATOM 1333 OD2 ASP B 237 32.962 62.557 −2.336 1.00 56.33 O ATOM 1334 N VAL B 238 30.661 61.676 −5.559 1.00 49.93 N ATOM 1335 CA VAL B 238 30.725 62.476 −6.788 1.00 47.50 C ATOM 1336 C VAL B 238 30.455 61.658 −8.047 1.00 46.36 C ATOM 1337 O VAL B 238 30.350 62.204 −9.141 1.00 44.99 O ATOM 1338 CB VAL B 238 32.105 63.155 −6.955 1.00 47.44 C ATOM 1339 CG1 VAL B 238 32.315 64.193 −5.855 1.00 46.51 C ATOM 1340 CG2 VAL B 238 33.209 62.103 −6.921 1.00 46.60 C ATOM 1341 N LEU B 239 30.343 60.346 −7.886 1.00 45.32 N ATOM 1342 CA LEU B 239 30.097 59.456 −9.009 1.00 44.11 C ATOM 1343 C LEU B 239 28.614 59.154 −9.221 1.00 42.87 C ATOM 1344 O LEU B 239 27.823 59.163 −8.275 1.00 41.17 O ATOM 1345 CB LEU B 239 30.866 58.150 −8.797 1.00 45.39 C ATOM 1346 CG LEU B 239 32.213 57.947 −9.500 1.00 47.31 C ATOM 1347 CD1 LEU B 239 32.895 59.280 −9.784 1.00 50.44 C ATOM 1348 CD2 LEU B 239 33.085 57.056 −8.633 1.00 47.46 C ATOM 1349 N PRO B 240 28.211 58.909 −10.481 1.00 42.22 N ATOM 1350 CA PRO B 240 26.802 58.602 −10.748 1.00 40.41 C ATOM 1351 C PRO B 240 26.413 57.361 −9.947 1.00 38.81 C ATOM 1352 O PRO B 240 27.230 56.461 −9.758 1.00 35.05 O ATOM 1353 CB PRO B 240 26.768 58.385 −12.265 1.00 40.21 C ATOM 1354 CG PRO B 240 28.185 58.015 −12.615 1.00 40.16 C ATOM 1355 CD PRO B 240 28.993 58.931 −11.730 1.00 42.24 C ATOM 1356 N SER B 241 25.170 57.328 −9.477 1.00 39.89 N ATOM 1357 CA SER B 241 24.683 56.229 −8.653 1.00 41.17 C ATOM 1358 C SER B 241 24.862 54.823 −9.217 1.00 41.84 C ATOM 1359 O SER B 241 25.099 53.887 −8.459 1.00 40.78 O ATOM 1360 CB SER B 241 23.211 56.456 −8.285 1.00 40.90 C ATOM 1361 OG SER B 241 22.370 56.370 −9.418 1.00 41.89 O ATOM 1362 N HIS B 242 24.769 54.662 −10.534 1.00 42.79 N ATOM 1363 CA HIS B 242 24.915 53.329 −11.106 1.00 44.00 C ATOM 1364 C HIS B 242 26.308 52.745 −10.861 1.00 44.18 C ATOM 1365 O HIS B 242 26.528 51.548 −11.051 1.00 44.48 O ATOM 1366 CB HIS B 242 24.609 53.337 −12.615 1.00 44.68 C ATOM 1367 CG HIS B 242 25.728 53.856 −13.463 1.00 45.88 C ATOM 1368 ND1 HIS B 242 25.938 55.201 −13.682 1.00 45.63 N ATOM 1369 CD2 HIS B 242 26.734 53.210 −14.100 1.00 45.13 C ATOM 1370 CE1 HIS B 242 27.028 55.359 −14.413 1.00 45.31 C ATOM 1371 NE2 HIS B 242 27.529 54.167 −14.679 1.00 44.52 N ATOM 1372 N CYS B 243 27.244 53.585 −10.436 1.00 44.41 N ATOM 1373 CA CYS B 243 28.610 53.134 −10.180 1.00 46.06 C ATOM 1374 C CYS B 243 28.830 52.503 −8.806 1.00 45.03 C ATOM 1375 O CYS B 243 29.813 51.795 −8.607 1.00 45.32 O ATOM 1376 CB CYS B 243 29.600 54.299 −10.302 1.00 50.08 C ATOM 1377 SG CYS B 243 29.818 55.061 −11.942 1.00 54.23 S ATOM 1378 N TRP B 244 27.930 52.751 −7.860 1.00 44.29 N ATOM 1379 CA TRP B 244 28.119 52.237 −6.503 1.00 43.92 C ATOM 1380 C TRP B 244 26.914 51.634 −5.792 1.00 44.54 C ATOM 1381 O TRP B 244 27.070 50.819 −4.881 1.00 44.86 O ATOM 1382 CB TRP B 244 28.656 53.356 −5.617 1.00 41.38 C ATOM 1383 CG TRP B 244 27.859 54.654 −5.700 1.00 40.51 C ATOM 1384 CD1 TRP B 244 28.097 55.721 −6.539 1.00 39.35 C ATOM 1385 CD2 TRP B 244 26.752 55.042 −4.872 1.00 38.13 C ATOM 1386 NE1 TRP B 244 27.213 56.743 −6.269 1.00 37.91 N ATOM 1387 CE2 TRP B 244 26.380 56.355 −5.254 1.00 37.29 C ATOM 1388 CE3 TRP B 244 26.040 54.409 −3.845 1.00 37.72 C ATOM 1389 CZ2 TRP B 244 25.334 57.042 −4.642 1.00 37.77 C ATOM 1390 CZ3 TRP B 244 24.994 55.096 −3.235 1.00 37.27 C ATOM 1391 CH2 TRP B 244 24.653 56.398 −3.635 1.00 39.15 C ATOM 1392 N ILE B 245 25.727 52.053 −6.207 1.00 43.54 N ATOM 1393 CA ILE B 245 24.472 51.626 −5.614 1.00 45.80 C ATOM 1394 C ILE B 245 24.233 50.133 −5.326 1.00 45.86 C ATOM 1395 O ILE B 245 23.612 49.797 −4.319 1.00 46.72 O ATOM 1396 CB ILE B 245 23.280 52.184 −6.451 1.00 47.09 C ATOM 1397 CG1 ILE B 245 22.333 52.971 −5.541 1.00 47.92 C ATOM 1398 CG2 ILE B 245 22.551 51.062 −7.179 1.00 47.16 C ATOM 1399 CD1 ILE B 245 21.883 52.218 −4.318 1.00 46.52 C ATOM 1400 N SER B 246 24.701 49.238 −6.187 1.00 45.14 N ATOM 1401 CA SER B 246 24.467 47.816 −5.950 1.00 45.76 C ATOM 1402 C SER B 246 25.338 47.305 −4.809 1.00 45.59 C ATOM 1403 O SER B 246 24.867 46.612 −3.907 1.00 43.82 O ATOM 1404 CB SER B 246 24.763 47.003 −7.207 1.00 45.52 C ATOM 1405 OG SER B 246 26.162 46.838 −7.370 1.00 51.00 O ATOM 1406 N GLU B 247 26.616 47.653 −4.864 1.00 45.29 N ATOM 1407 CA GLU B 247 27.578 47.244 −3.853 1.00 45.41 C ATOM 1408 C GLU B 247 27.260 47.850 −2.483 1.00 43.93 C ATOM 1409 O GLU B 247 27.327 47.170 −1.460 1.00 44.47 O ATOM 1410 CB GLU B 247 28.983 47.675 −4.285 1.00 46.51 C ATOM 1411 CG GLU B 247 30.072 47.322 −3.295 1.00 50.56 C ATOM 1412 CD GLU B 247 30.319 45.831 −3.220 1.00 52.10 C ATOM 1413 OE1 GLU B 247 31.108 45.396 −2.354 1.00 51.67 O ATOM 1414 OE2 GLU B 247 29.725 45.096 −4.037 1.00 54.23 O ATOM 1415 N MET B 248 26.914 49.130 −2.474 1.00 40.71 N ATOM 1416 CA MET B 248 26.621 49.826 −1.233 1.00 41.30 C ATOM 1417 C MET B 248 25.356 49.309 −0.552 1.00 39.73 C ATOM 1418 O MET B 248 25.319 49.149 0.670 1.00 39.87 O ATOM 1419 CB MET B 248 26.513 51.332 −1.505 1.00 41.78 C ATOM 1420 CG MET B 248 26.557 52.221 −0.264 1.00 43.87 C ATOM 1421 SD MET B 248 28.138 52.280 0.660 1.00 43.67 S ATOM 1422 CE MET B 248 29.247 51.363 −0.411 1.00 38.63 C ATOM 1423 N VAL B 249 24.317 49.050 −1.336 1.00 37.21 N ATOM 1424 CA VAL B 249 23.074 48.547 −0.776 1.00 35.20 C ATOM 1425 C VAL B 249 23.379 47.212 −0.107 1.00 36.30 C ATOM 1426 O VAL B 249 22.807 46.872 0.930 1.00 35.65 O ATOM 1427 CB VAL B 249 22.011 48.392 −1.887 1.00 36.29 C ATOM 1428 CG1 VAL B 249 20.977 47.367 −1.512 1.00 36.41 C ATOM 1429 CG2 VAL B 249 21.322 49.722 −2.110 1.00 32.75 C ATOM 1430 N VAL B 250 24.317 46.478 −0.693 1.00 35.39 N ATOM 1431 CA VAL B 250 24.738 45.184 −0.175 1.00 35.29 C ATOM 1432 C VAL B 250 25.599 45.302 1.088 1.00 35.84 C ATOM 1433 O VAL B 250 25.484 44.487 2.004 1.00 35.78 O ATOM 1434 CB VAL B 250 25.527 44.408 −1.244 1.00 33.99 C ATOM 1435 CG1 VAL B 250 26.122 43.136 −0.654 1.00 33.25 C ATOM 1436 CG2 VAL B 250 24.599 44.063 −2.403 1.00 35.34 C ATOM 1437 N GLN B 251 26.455 46.318 1.135 1.00 34.16 N ATOM 1438 CA GLN B 251 27.330 46.521 2.278 1.00 32.34 C ATOM 1439 C GLN B 251 26.570 47.124 3.438 1.00 30.64 C ATOM 1440 O GLN B 251 26.868 46.846 4.599 1.00 31.74 O ATOM 1441 CB GLN B 251 28.508 47.422 1.895 1.00 33.40 C ATOM 1442 CG GLN B 251 29.467 46.789 0.894 1.00 35.25 C ATOM 1443 CD GLN B 251 30.008 45.442 1.359 1.00 37.38 C ATOM 1444 OE1 GLN B 251 30.213 45.215 2.555 1.00 38.82 O ATOM 1445 NE2 GLN B 251 30.263 44.550 0.410 1.00 37.16 N ATOM 1446 N LEU B 252 25.592 47.962 3.131 1.00 29.22 N ATOM 1447 CA LEU B 252 24.788 48.553 4.187 1.00 30.07 C ATOM 1448 C LEU B 252 24.074 47.411 4.910 1.00 30.49 C ATOM 1449 O LEU B 252 24.083 47.338 6.137 1.00 31.62 O ATOM 1450 CB LEU B 252 23.775 49.541 3.595 1.00 26.58 C ATOM 1451 CG LEU B 252 24.396 50.889 3.162 1.00 29.74 C ATOM 1452 CD1 LEU B 252 23.367 51.781 2.452 1.00 25.72 C ATOM 1453 CD2 LEU B 252 24.940 51.602 4.403 1.00 28.99 C ATOM 1454 N SER B 253 23.475 46.512 4.135 1.00 29.43 N ATOM 1455 CA SER B 253 22.763 45.372 4.687 1.00 29.35 C ATOM 1456 C SER B 253 23.689 44.541 5.575 1.00 29.60 C ATOM 1457 O SER B 253 23.324 44.162 6.685 1.00 27.14 O ATOM 1458 CB SER B 253 22.216 44.501 3.559 1.00 29.62 C ATOM 1459 OG SER B 253 21.469 43.417 4.082 1.00 32.53 O ATOM 1460 N ASP B 254 24.897 44.278 5.094 1.00 29.62 N ATOM 1461 CA ASP B 254 25.847 43.494 5.871 1.00 31.92 C ATOM 1462 C ASP B 254 26.192 44.203 7.192 1.00 31.13 C ATOM 1463 O ASP B 254 26.277 43.575 8.248 1.00 25.96 O ATOM 1464 CB ASP B 254 27.130 43.271 5.070 1.00 35.93 C ATOM 1465 CG ASP B 254 28.066 42.273 5.737 1.00 41.42 C ATOM 1466 OD1 ASP B 254 29.303 42.391 5.568 1.00 43.83 O ATOM 1467 OD2 ASP B 254 27.559 41.356 6.423 1.00 46.70 O ATOM 1468 N SER B 255 26.399 45.513 7.131 1.00 28.26 N ATOM 1469 CA SER B 255 26.752 46.247 8.335 1.00 28.88 C ATOM 1470 C SER B 255 25.616 46.261 9.357 1.00 28.38 C ATOM 1471 O SER B 255 25.843 46.036 10.549 1.00 28.04 O ATOM 1472 CB SER B 255 27.165 47.682 7.985 1.00 28.35 C ATOM 1473 OG SER B 255 28.356 47.692 7.214 1.00 28.87 O ATOM 1474 N LEU B 256 24.397 46.512 8.890 1.00 26.63 N ATOM 1475 CA LEU B 256 23.257 46.563 9.787 1.00 26.15 C ATOM 1476 C LEU B 256 22.955 45.218 10.407 1.00 26.03 C ATOM 1477 O LEU B 256 22.582 45.138 11.572 1.00 26.78 O ATOM 1478 CB LEU B 256 22.024 47.095 9.060 1.00 23.91 C ATOM 1479 CG LEU B 256 22.081 48.604 8.804 1.00 25.22 C ATOM 1480 CD1 LEU B 256 20.923 49.019 7.915 1.00 25.03 C ATOM 1481 CD2 LEU B 256 22.038 49.358 10.134 1.00 23.13 C ATOM 1482 N THR B 257 23.121 44.166 9.623 1.00 27.10 N ATOM 1483 CA THR B 257 22.861 42.822 10.094 1.00 28.54 C ATOM 1484 C THR B 257 23.806 42.465 11.227 1.00 27.76 C ATOM 1485 O THR B 257 23.397 41.834 12.201 1.00 27.18 O ATOM 1486 CB THR B 257 23.012 41.797 8.948 1.00 30.71 C ATOM 1487 OG1 THR B 257 22.062 42.103 7.916 1.00 30.14 O ATOM 1488 CG2 THR B 257 22.758 40.372 9.461 1.00 30.87 C ATOM 1489 N ASP B 258 25.061 42.882 11.098 1.00 28.20 N ATOM 1490 CA ASP B 258 26.078 42.619 12.112 1.00 30.16 C ATOM 1491 C ASP B 258 25.849 43.377 13.414 1.00 29.71 C ATOM 1492 O ASP B 258 26.229 42.901 14.485 1.00 28.76 O ATOM 1493 CB ASP B 258 27.467 42.993 11.597 1.00 34.00 C ATOM 1494 CG ASP B 258 27.970 42.046 10.554 1.00 38.03 C ATOM 1495 OD1 ASP B 258 27.752 40.827 10.720 1.00 40.72 O ATOM 1496 OD2 ASP B 258 28.598 42.521 9.576 1.00 43.37 O ATOM 1497 N LEU B 259 25.265 44.565 13.318 1.00 29.27 N ATOM 1498 CA LEU B 259 25.002 45.382 14.502 1.00 31.85 C ATOM 1499 C LEU B 259 23.948 44.734 15.380 1.00 30.57 C ATOM 1500 O LEU B 259 23.878 44.994 16.585 1.00 27.66 O ATOM 1501 CB LEU B 259 24.521 46.784 14.106 1.00 34.32 C ATOM 1502 CG LEU B 259 25.565 47.720 13.506 1.00 36.30 C ATOM 1503 CD1 LEU B 259 24.940 49.089 13.226 1.00 38.89 C ATOM 1504 CD2 LEU B 259 26.727 47.858 14.483 1.00 38.73 C ATOM 1505 N LEU B 260 23.122 43.906 14.755 1.00 30.02 N ATOM 1506 CA LEU B 260 22.060 43.202 15.456 1.00 33.18 C ATOM 1507 C LEU B 260 22.669 42.436 16.621 1.00 33.45 C ATOM 1508 O LEU B 260 22.136 42.424 17.728 1.00 34.54 O ATOM 1509 CB LEU B 260 21.366 42.244 14.488 1.00 32.08 C ATOM 1510 CG LEU B 260 19.867 42.456 14.273 1.00 35.36 C ATOM 1511 CD1 LEU B 260 19.477 43.920 14.465 1.00 29.63 C ATOM 1512 CD2 LEU B 260 19.513 41.959 12.882 1.00 33.62 C ATOM 1513 N ASP B 261 23.807 41.813 16.346 1.00 35.20 N ATOM 1514 CA ASP B 261 24.550 41.030 17.326 1.00 37.38 C ATOM 1515 C ASP B 261 24.929 41.883 18.549 1.00 34.81 C ATOM 1516 O ASP B 261 25.082 41.358 19.650 1.00 36.03 O ATOM 1517 CB ASP B 261 25.834 40.495 16.665 1.00 40.33 C ATOM 1518 CG ASP B 261 26.245 39.132 17.183 1.00 46.67 C ATOM 1519 OD1 ASP B 261 27.295 38.623 16.727 1.00 49.65 O ATOM 1520 OD2 ASP B 261 25.525 38.560 18.035 1.00 50.57 O ATOM 1521 N LYS B 262 25.069 43.193 18.355 1.00 30.45 N ATOM 1522 CA LYS B 262 25.479 44.082 19.442 1.00 28.46 C ATOM 1523 C LYS B 262 24.379 44.578 20.367 1.00 26.76 C ATOM 1524 O LYS B 262 24.654 45.301 21.320 1.00 25.35 O ATOM 1525 CB LYS B 262 26.241 45.297 18.878 1.00 27.07 C ATOM 1526 CG LYS B 262 27.357 44.951 17.908 1.00 26.01 C ATOM 1527 CD LYS B 262 28.235 43.836 18.449 1.00 26.80 C ATOM 1528 CE LYS B 262 29.377 43.499 17.490 1.00 31.35 C ATOM 1529 NZ LYS B 262 28.856 43.052 16.172 1.00 35.54 N ATOM 1530 N PHE B 263 23.135 44.209 20.094 1.00 27.38 N ATOM 1531 CA PHE B 263 22.043 44.663 20.942 1.00 27.79 C ATOM 1532 C PHE B 263 21.155 43.523 21.406 1.00 28.66 C ATOM 1533 O PHE B 263 21.239 42.408 20.889 1.00 25.25 O ATOM 1534 CB PHE B 263 21.207 45.721 20.217 1.00 27.15 C ATOM 1535 CG PHE B 263 22.005 46.916 19.764 1.00 29.50 C ATOM 1536 CD1 PHE B 263 22.613 46.930 18.512 1.00 29.29 C ATOM 1537 CD2 PHE B 263 22.197 48.006 20.615 1.00 28.89 C ATOM 1538 CE1 PHE B 263 23.406 48.012 18.113 1.00 32.10 C ATOM 1539 CE2 PHE B 263 22.986 49.090 20.231 1.00 29.79 C ATOM 1540 CZ PHE B 263 23.593 49.096 18.981 1.00 31.21 C ATOM 1541 N SER B 264 20.323 43.813 22.405 1.00 29.66 N ATOM 1542 CA SER B 264 19.401 42.825 22.946 1.00 33.35 C ATOM 1543 C SER B 264 17.994 43.082 22.411 1.00 35.50 C ATOM 1544 O SER B 264 17.558 44.231 22.303 1.00 35.16 O ATOM 1545 CB SER B 264 19.413 42.875 24.474 1.00 33.43 C ATOM 1546 OG SER B 264 18.310 42.178 25.024 1.00 34.18 O ATOM 1547 N ASN B 265 17.306 41.998 22.066 1.00 38.20 N ATOM 1548 CA ASN B 265 15.952 42.036 21.528 1.00 42.52 C ATOM 1549 C ASN B 265 14.929 42.090 22.667 1.00 44.22 C ATOM 1550 O ASN B 265 13.727 41.959 22.449 1.00 44.33 O ATOM 1551 CB ASN B 265 15.734 40.791 20.648 1.00 47.43 C ATOM 1552 CG ASN B 265 14.377 40.769 19.969 1.00 52.30 C ATOM 1553 OD1 ASN B 265 13.347 40.580 20.618 1.00 55.95 O ATOM 1554 ND2 ASN B 265 14.368 40.958 18.654 1.00 55.04 N ATOM 1555 N ILE B 266 15.408 42.275 23.890 1.00 46.53 N ATOM 1556 CA ILE B 266 14.512 42.366 25.037 1.00 50.41 C ATOM 1557 C ILE B 266 14.555 43.783 25.583 1.00 51.79 C ATOM 1558 O ILE B 266 15.475 44.151 26.313 1.00 53.00 O ATOM 1559 CB ILE B 266 14.906 41.378 26.162 1.00 52.11 C ATOM 1560 CG1 ILE B 266 14.621 39.942 25.711 1.00 52.25 C ATOM 1561 CG2 ILE B 266 14.125 41.703 27.446 1.00 51.47 C ATOM 1562 CD1 ILE B 266 14.977 38.896 26.741 1.00 52.80 C ATOM 1563 N SER B 267 13.554 44.575 25.220 1.00 52.82 N ATOM 1564 CA SER B 267 13.479 45.960 25.655 1.00 53.92 C ATOM 1565 C SER B 267 12.101 46.529 25.332 1.00 54.57 C ATOM 1566 O SER B 267 11.650 46.470 24.184 1.00 55.28 O ATOM 1567 CB SER B 267 14.566 46.780 24.944 1.00 53.43 C ATOM 1568 OG SER B 267 14.486 48.159 25.265 1.00 53.30 O ATOM 1569 N GLU B 268 11.427 47.063 26.346 1.00 54.63 N ATOM 1570 CA GLU B 268 10.110 47.662 26.149 1.00 55.91 C ATOM 1571 C GLU B 268 10.305 49.051 25.546 1.00 55.23 C ATOM 1572 O GLU B 268 11.338 49.686 25.750 1.00 55.02 O ATOM 1573 CB GLU B 268 9.365 47.811 27.483 1.00 57.62 C ATOM 1574 CG GLU B 268 9.238 46.541 28.301 1.00 60.87 C ATOM 1575 CD GLU B 268 8.565 46.781 29.645 1.00 63.06 C ATOM 1576 OE1 GLU B 268 9.020 47.675 30.391 1.00 63.52 O ATOM 1577 OE2 GLU B 268 7.584 46.072 29.960 1.00 65.17 O ATOM 1578 N GLY B 269 9.307 49.520 24.808 1.00 55.14 N ATOM 1579 CA GLY B 269 9.387 50.842 24.214 1.00 53.65 C ATOM 1580 C GLY B 269 10.535 51.025 23.245 1.00 51.69 C ATOM 1581 O GLY B 269 10.726 50.214 22.339 1.00 52.57 O ATOM 1582 N LEU B 270 11.302 52.094 23.444 1.00 48.68 N ATOM 1583 CA LEU B 270 12.434 52.417 22.578 1.00 46.00 C ATOM 1584 C LEU B 270 13.481 51.300 22.540 1.00 43.42 C ATOM 1585 O LEU B 270 14.198 51.074 23.524 1.00 43.72 O ATOM 1586 CB LEU B 270 13.097 53.719 23.050 1.00 46.90 C ATOM 1587 CG LEU B 270 13.922 54.527 22.034 1.00 48.10 C ATOM 1588 CD1 LEU B 270 14.701 55.614 22.781 1.00 48.00 C ATOM 1589 CD2 LEU B 270 14.885 53.621 21.261 1.00 49.29 C ATOM 1590 N SER B 271 13.585 50.622 21.398 1.00 39.34 N ATOM 1591 CA SER B 271 14.549 49.534 21.246 1.00 33.02 C ATOM 1592 C SER B 271 15.455 49.723 20.043 1.00 29.95 C ATOM 1593 O SER B 271 14.979 49.829 18.916 1.00 30.47 O ATOM 1594 CB SER B 271 13.818 48.198 21.107 1.00 33.58 C ATOM 1595 OG SER B 271 14.740 47.135 20.920 1.00 29.31 O ATOM 1596 N ASN B 272 16.763 49.756 20.270 1.00 27.19 N ATOM 1597 CA ASN B 272 17.689 49.906 19.155 1.00 26.28 C ATOM 1598 C ASN B 272 17.677 48.657 18.270 1.00 24.35 C ATOM 1599 O ASN B 272 17.806 48.761 17.047 1.00 24.38 O ATOM 1600 CB ASN B 272 19.112 50.191 19.649 1.00 28.40 C ATOM 1601 CG ASN B 272 19.314 51.656 20.074 1.00 31.26 C ATOM 1602 OD1 ASN B 272 18.490 52.525 19.775 1.00 29.59 O ATOM 1603 ND2 ASN B 272 20.422 51.927 20.763 1.00 27.16 N ATOM 1604 N TYR B 273 17.526 47.480 18.879 1.00 22.77 N ATOM 1605 CA TYR B 273 17.478 46.233 18.105 1.00 22.69 C ATOM 1606 C TYR B 273 16.283 46.306 17.142 1.00 20.30 C ATOM 1607 O TYR B 273 16.387 45.988 15.959 1.00 18.57 O ATOM 1608 CB TYR B 273 17.305 45.005 19.029 1.00 19.03 C ATOM 1609 CG TYR B 273 17.499 43.665 18.325 1.00 19.58 C ATOM 1610 CD1 TYR B 273 18.711 42.976 18.410 1.00 21.34 C ATOM 1611 CD2 TYR B 273 16.475 43.098 17.555 1.00 21.61 C ATOM 1612 CE1 TYR B 273 18.905 41.749 17.739 1.00 21.50 C ATOM 1613 CE2 TYR B 273 16.654 41.870 16.879 1.00 20.21 C ATOM 1614 CZ TYR B 273 17.870 41.208 16.974 1.00 21.89 C ATOM 1615 OH TYR B 273 18.072 40.025 16.282 1.00 24.18 O ATOM 1616 N SER B 274 15.148 46.743 17.663 1.00 22.80 N ATOM 1617 CA SER B 274 13.927 46.832 16.863 1.00 27.21 C ATOM 1618 C SER B 274 14.050 47.772 15.667 1.00 27.36 C ATOM 1619 O SER B 274 13.613 47.449 14.563 1.00 30.53 O ATOM 1620 CB SER B 274 12.764 47.274 17.744 1.00 28.04 C ATOM 1621 OG SER B 274 11.648 47.587 16.945 1.00 36.14 O ATOM 1622 N ILE B 275 14.643 48.936 15.884 1.00 26.70 N ATOM 1623 CA ILE B 275 14.807 49.898 14.807 1.00 25.74 C ATOM 1624 C ILE B 275 15.759 49.382 13.737 1.00 28.05 C ATOM 1625 O ILE B 275 15.490 49.521 12.544 1.00 30.55 O ATOM 1626 CB ILE B 275 15.301 51.240 15.372 1.00 27.01 C ATOM 1627 CG1 ILE B 275 14.177 51.848 16.230 1.00 25.40 C ATOM 1628 CG2 ILE B 275 15.706 52.193 14.243 1.00 25.64 C ATOM 1629 CD1 ILE B 275 14.599 53.071 17.034 1.00 29.62 C ATOM 1630 N ILE B 276 16.861 48.767 14.156 1.00 27.36 N ATOM 1631 CA ILE B 276 17.828 48.242 13.210 1.00 26.58 C ATOM 1632 C ILE B 276 17.194 47.141 12.367 1.00 28.05 C ATOM 1633 O ILE B 276 17.449 47.048 11.158 1.00 26.42 O ATOM 1634 CB ILE B 276 19.077 47.682 13.940 1.00 27.08 C ATOM 1635 CG1 ILE B 276 19.794 48.818 14.676 1.00 29.78 C ATOM 1636 CG2 ILE B 276 20.012 47.018 12.946 1.00 21.94 C ATOM 1637 CD1 ILE B 276 20.973 48.376 15.530 1.00 31.10 C ATOM 1638 N ASP B 277 16.375 46.307 13.006 1.00 28.02 N ATOM 1639 CA ASP B 277 15.697 45.216 12.308 1.00 31.09 C ATOM 1640 C ASP B 277 14.875 45.762 11.134 1.00 31.45 C ATOM 1641 O ASP B 277 14.986 45.272 10.013 1.00 32.87 O ATOM 1642 CB ASP B 277 14.778 44.448 13.271 1.00 34.57 C ATOM 1643 CG ASP B 277 13.996 43.344 12.575 1.00 36.69 C ATOM 1644 OD1 ASP B 277 14.621 42.396 12.063 1.00 37.70 O ATOM 1645 OD2 ASP B 277 12.751 43.427 12.526 1.00 42.12 O ATOM 1646 N LYS B 278 14.054 46.775 11.394 1.00 31.81 N ATOM 1647 CA LYS B 278 13.241 47.388 10.346 1.00 33.40 C ATOM 1648 C LYS B 278 14.132 47.982 9.259 1.00 33.30 C ATOM 1649 O LYS B 278 13.841 47.849 8.075 1.00 33.52 O ATOM 1650 CB LYS B 278 12.348 48.484 10.938 1.00 34.87 C ATOM 1651 CG LYS B 278 11.222 47.948 11.806 1.00 39.50 C ATOM 1652 CD LYS B 278 10.764 48.949 12.865 1.00 44.74 C ATOM 1653 CE LYS B 278 9.850 48.261 13.896 1.00 47.34 C ATOM 1654 NZ LYS B 278 9.637 49.060 15.144 1.00 49.68 N ATOM 1655 N LEU B 279 15.227 48.623 9.662 1.00 33.17 N ATOM 1656 CA LEU B 279 16.136 49.219 8.694 1.00 33.76 C ATOM 1657 C LEU B 279 16.735 48.144 7.801 1.00 35.27 C ATOM 1658 O LEU B 279 16.949 48.367 6.611 1.00 35.16 O ATOM 1659 CB LEU B 279 17.254 49.994 9.397 1.00 31.81 C ATOM 1660 CG LEU B 279 16.830 51.213 10.221 1.00 31.76 C ATOM 1661 CD1 LEU B 279 18.076 51.978 10.657 1.00 27.74 C ATOM 1662 CD2 LEU B 279 15.910 52.117 9.396 1.00 27.79 C ATOM 1663 N VAL B 280 17.011 46.981 8.384 1.00 36.33 N ATOM 1664 CA VAL B 280 17.566 45.859 7.640 1.00 36.53 C ATOM 1665 C VAL B 280 16.589 45.355 6.575 1.00 36.86 C ATOM 1666 O VAL B 280 16.991 44.953 5.489 1.00 36.16 O ATOM 1667 CB VAL B 280 17.903 44.688 8.585 1.00 39.05 C ATOM 1668 CG1 VAL B 280 18.312 43.460 7.775 1.00 40.46 C ATOM 1669 CG2 VAL B 280 19.018 45.094 9.527 1.00 37.37 C ATOM 1670 N ASN B 281 15.298 45.380 6.884 1.00 37.81 N ATOM 1671 CA ASN B 281 14.303 44.910 5.937 1.00 37.92 C ATOM 1672 C ASN B 281 14.111 45.832 4.742 1.00 39.69 C ATOM 1673 O ASN B 281 13.937 45.358 3.623 1.00 40.54 O ATOM 1674 CB ASN B 281 12.968 44.680 6.638 1.00 36.79 C ATOM 1675 CG ASN B 281 13.007 43.487 7.570 1.00 35.96 C ATOM 1676 OD1 ASN B 281 13.696 42.501 7.305 1.00 34.67 O ATOM 1677 ND2 ASN B 281 12.255 43.563 8.660 1.00 35.46 N ATOM 1678 N ILE B 282 14.135 47.141 4.962 1.00 41.96 N ATOM 1679 CA ILE B 282 13.977 48.063 3.844 1.00 43.76 C ATOM 1680 C ILE B 282 15.178 47.930 2.908 1.00 43.59 C ATOM 1681 O ILE B 282 15.023 47.878 1.684 1.00 42.87 O ATOM 1682 CB ILE B 282 13.837 49.528 4.322 1.00 46.35 C ATOM 1683 CG1 ILE B 282 14.904 49.847 5.364 1.00 49.26 C ATOM 1684 CG2 ILE B 282 12.450 49.755 4.895 1.00 46.46 C ATOM 1685 CD1 ILE B 282 14.775 51.227 5.969 1.00 52.73 C ATOM 1686 N VAL B 283 16.369 47.834 3.490 1.00 42.61 N ATOM 1687 CA VAL B 283 17.591 47.701 2.707 1.00 44.18 C ATOM 1688 C VAL B 283 17.683 46.332 2.039 1.00 45.95 C ATOM 1689 O VAL B 283 18.330 46.180 1.005 1.00 44.64 O ATOM 1690 CB VAL B 283 18.836 47.902 3.586 1.00 44.07 C ATOM 1691 CG1 VAL B 283 20.078 47.992 2.729 1.00 45.78 C ATOM 1692 CG2 VAL B 283 18.682 49.152 4.404 1.00 47.56 C ATOM 1693 N ASP B 284 17.052 45.327 2.634 1.00 48.15 N ATOM 1694 CA ASP B 284 17.088 43.999 2.043 1.00 50.89 C ATOM 1695 C ASP B 284 16.085 43.925 0.905 1.00 51.42 C ATOM 1696 O ASP B 284 16.235 43.124 −0.014 1.00 50.07 O ATOM 1697 CB ASP B 284 16.816 42.928 3.102 1.00 52.73 C ATOM 1698 CG ASP B 284 18.063 42.590 3.910 1.00 54.77 C ATOM 1699 OD1 ASP B 284 19.064 43.328 3.782 1.00 53.52 O ATOM 1700 OD2 ASP B 284 18.048 41.596 4.671 1.00 56.89 O ATOM 1701 N ASP B 285 15.065 44.773 0.962 1.00 53.52 N ATOM 1702 CA ASP B 285 14.077 44.813 −0.103 1.00 56.78 C ATOM 1703 C ASP B 285 14.748 45.412 −1.336 1.00 57.85 C ATOM 1704 O ASP B 285 14.447 45.029 −2.466 1.00 57.90 O ATOM 1705 CB ASP B 285 12.872 45.664 0.303 1.00 57.84 C ATOM 1706 CG ASP B 285 11.864 44.888 1.126 1.00 60.65 C ATOM 1707 OD1 ASP B 285 11.413 43.820 0.658 1.00 62.40 O ATOM 1708 OD2 ASP B 285 11.515 45.344 2.235 1.00 62.92 O ATOM 1709 N LEU B 286 15.669 46.345 −1.106 1.00 59.05 N ATOM 1710 CA LEU B 286 16.389 46.993 −2.194 1.00 61.21 C ATOM 1711 C LEU B 286 17.308 46.003 −2.903 1.00 62.73 C ATOM 1712 O LEU B 286 17.385 45.991 −4.131 1.00 63.40 O ATOM 1713 CB LEU B 286 17.215 48.172 −1.667 1.00 59.77 C ATOM 1714 CG LEU B 286 16.469 49.304 −0.952 1.00 59.72 C ATOM 1715 CD1 LEU B 286 17.479 50.311 −0.430 1.00 60.06 C ATOM 1716 CD2 LEU B 286 15.485 49.975 −1.895 1.00 58.38 C ATOM 1717 N VAL B 287 18.003 45.173 −2.128 1.00 65.19 N ATOM 1718 CA VAL B 287 18.915 44.181 −2.695 1.00 67.52 C ATOM 1719 C VAL B 287 18.151 43.272 −3.651 1.00 69.85 C ATOM 1720 O VAL B 287 18.746 42.490 −4.390 1.00 70.28 O ATOM 1721 CB VAL B 287 19.587 43.321 −1.586 1.00 66.53 C ATOM 1722 CG1 VAL B 287 20.507 42.285 −2.208 1.00 65.22 C ATOM 1723 CG2 VAL B 287 20.383 44.211 −0.647 1.00 64.95 C ATOM 1724 N GLU B 288 16.826 43.387 −3.636 1.00 72.56 N ATOM 1725 CA GLU B 288 15.985 42.594 −4.521 1.00 75.05 C ATOM 1726 C GLU B 288 15.773 43.293 −5.863 1.00 76.15 C ATOM 1727 O GLU B 288 15.887 42.654 −6.905 1.00 76.95 O ATOM 1728 CB GLU B 288 14.631 42.303 −3.870 1.00 75.38 C ATOM 1729 CG GLU B 288 14.703 41.368 −2.676 1.00 76.07 C ATOM 1730 CD GLU B 288 13.334 40.869 −2.260 1.00 76.91 C ATOM 1731 OE1 GLU B 288 12.663 40.230 −3.100 1.00 76.61 O ATOM 1732 OE2 GLU B 288 12.928 41.116 −1.102 1.00 77.21 O ATOM 1733 N CYS B 289 15.465 44.592 −5.847 1.00 77.68 N ATOM 1734 CA CYS B 289 15.266 45.326 −7.102 1.00 79.66 C ATOM 1735 C CYS B 289 16.567 45.273 −7.896 1.00 81.37 C ATOM 1736 O CYS B 289 16.607 45.643 −9.069 1.00 82.35 O ATOM 1737 CB CYS B 289 14.862 46.798 −6.853 1.00 78.42 C ATOM 1738 SG CYS B 289 13.190 47.024 −6.149 1.00 78.81 S ATOM 1739 N VAL B 290 17.626 44.802 −7.244 1.00 83.34 N ATOM 1740 CA VAL B 290 18.939 44.678 −7.868 1.00 85.04 C ATOM 1741 C VAL B 290 19.114 43.291 −8.477 1.00 86.93 C ATOM 1742 O VAL B 290 19.836 43.121 −9.458 1.00 87.33 O ATOM 1743 CB VAL B 290 20.068 44.912 −6.840 1.00 84.62 C ATOM 1744 CG1 VAL B 290 21.422 44.610 −7.465 1.00 84.22 C ATOM 1745 CG2 VAL B 290 20.027 46.347 −6.348 1.00 84.06 C ATOM 1746 N LYS B 291 18.450 42.302 −7.888 1.00 89.27 N ATOM 1747 CA LYS B 291 18.538 40.931 −8.375 1.00 91.52 C ATOM 1748 C LYS B 291 18.122 40.793 −9.836 1.00 92.26 C ATOM 1749 O LYS B 291 18.958 40.870 −10.737 1.00 92.64 O ATOM 1750 CB LYS B 291 17.676 40.003 −7.518 1.00 92.27 C ATOM 1751 CG LYS B 291 18.450 39.217 −6.475 1.00 93.39 C ATOM 1752 CD LYS B 291 17.635 38.021 −6.007 1.00 94.40 C ATOM 1753 CE LYS B 291 18.452 37.076 −5.146 1.00 93.52 C ATOM 1754 NZ LYS B 291 17.667 35.850 −4.845 1.00 93.70 N ATOM 1755 N GLU B 292 16.829 40.583 −10.061 1.00 93.06 N ATOM 1756 CA GLU B 292 16.289 40.422 −11.407 1.00 93.90 C ATOM 1757 C GLU B 292 16.822 41.477 −12.370 1.00 94.28 C ATOM 1758 O GLU B 292 16.905 41.237 −13.575 1.00 94.59 O ATOM 1759 CB GLU B 292 14.764 40.479 −11.366 1.00 93.97 C ATOM 1760 N ASN B 293 17.180 42.639 −11.829 1.00 94.51 N ATOM 1761 CA ASN B 293 17.700 43.752 −12.620 1.00 94.89 C ATOM 1762 C ASN B 293 18.486 43.306 −13.847 1.00 95.25 C ATOM 1763 O ASN B 293 19.547 42.691 −13.732 1.00 94.68 O ATOM 1764 CB ASN B 293 18.569 44.647 −11.748 1.00 94.54 C ATOM 1765 N SER B 294 17.947 43.622 −15.021 1.00 96.10 N ATOM 1766 CA SER B 294 18.578 43.279 −16.291 1.00 96.82 C ATOM 1767 C SER B 294 19.260 44.516 −16.862 1.00 97.43 C ATOM 1768 O SER B 294 19.786 44.493 −17.976 1.00 97.54 O ATOM 1769 CB SER B 294 17.534 42.760 −17.272 1.00 96.87 C ATOM 1770 N SER B 295 19.234 45.599 −16.091 1.00 97.82 N ATOM 1771 CA SER B 295 19.850 46.851 −16.505 1.00 98.14 C ATOM 1772 C SER B 295 21.360 46.757 −16.330 1.00 98.75 C ATOM 1773 O SER B 295 21.849 46.322 −15.287 1.00 98.85 O ATOM 1774 CB SER B 295 19.297 48.007 −15.680 1.00 97.18 C ATOM 1775 N LYS B 296 22.094 47.157 −17.361 1.00 99.70 N ATOM 1776 CA LYS B 296 23.549 47.124 −17.320 1.00 100.08 C ATOM 1777 C LYS B 296 24.090 48.545 −17.201 1.00 100.40 C ATOM 1778 O LYS B 296 23.910 49.370 −18.099 1.00 100.26 O ATOM 1779 CB LYS B 296 24.095 46.454 −18.577 1.00 100.16 C ATOM 1780 N ASP B 297 24.747 48.826 −16.082 1.00 100.71 N ATOM 1781 CA ASP B 297 25.315 50.143 −15.840 1.00 101.31 C ATOM 1782 C ASP B 297 26.625 50.000 −15.070 1.00 101.82 C ATOM 1783 O ASP B 297 27.622 50.650 −15.392 1.00 101.90 O ATOM 1784 CB ASP B 297 24.327 50.997 −15.053 1.00 101.33 C ATOM 1785 N LEU B 298 26.607 49.137 −14.058 1.00 102.10 N ATOM 1786 CA LEU B 298 27.770 48.870 −13.217 1.00 102.11 C ATOM 1787 C LEU B 298 27.299 48.176 −11.949 1.00 102.30 C ATOM 1788 O LEU B 298 28.019 48.131 −10.952 1.00 102.51 O ATOM 1789 CB LEU B 298 28.489 50.171 −12.863 1.00 102.08 C ATOM 1790 N LYS B 299 26.081 47.641 −11.997 1.00 102.53 N ATOM 1791 CA LYS B 299 25.492 46.946 −10.855 1.00 102.73 C ATOM 1792 C LYS B 299 26.278 45.687 −10.495 1.00 103.02 C ATOM 1793 O LYS B 299 25.780 44.568 −10.633 1.00 103.10 O ATOM 1794 CB LYS B 299 24.039 46.591 −11.157 1.00 102.10 C ATOM 1795 N LYS B 300 27.508 45.877 −10.030 1.00 103.14 N ATOM 1796 CA LYS B 300 28.365 44.763 −9.650 1.00 103.42 C ATOM 1797 C LYS B 300 29.427 45.224 −8.656 1.00 103.57 C ATOM 1798 O LYS B 300 29.379 44.873 −7.475 1.00 103.46 O ATOM 1799 CB LYS B 300 29.026 44.173 −10.887 1.00 103.35 C ATOM 1800 N SER B 301 30.378 46.014 −9.149 1.00 103.66 N ATOM 1801 CA SER B 301 31.474 46.548 −8.342 1.00 103.79 C ATOM 1802 C SER B 301 32.583 45.521 −8.121 1.00 103.79 C ATOM 1803 O SER B 301 33.224 45.505 −7.069 1.00 103.66 O ATOM 1804 CB SER B 301 30.947 47.053 −6.996 1.00 103.60 C ATOM 1805 N PHE B 302 32.805 44.670 −9.120 1.00 103.61 N ATOM 1806 CA PHE B 302 33.839 43.640 −9.051 1.00 103.14 C ATOM 1807 C PHE B 302 33.752 42.815 −7.768 1.00 102.53 C ATOM 1808 O PHE B 302 32.978 41.859 −7.687 1.00 102.07 O ATOM 1809 CB PHE B 302 35.222 44.283 −9.172 1.00 103.18 C ATOM 1810 N LYS B 303 34.554 43.189 −6.772 1.00 101.84 N ATOM 1811 CA LYS B 303 34.577 42.495 −5.488 1.00 100.63 C ATOM 1812 C LYS B 303 33.991 43.369 −4.375 1.00 99.62 C ATOM 1813 O LYS B 303 32.952 44.003 −4.557 1.00 99.74 O ATOM 1814 CB LYS B 303 36.007 42.092 −5.144 1.00 100.68 C ATOM 1815 N SER B 304 34.657 43.398 −3.223 1.00 98.02 N ATOM 1816 CA SER B 304 34.189 44.197 −2.093 1.00 96.12 C ATOM 1817 C SER B 304 35.197 45.287 −1.746 1.00 94.26 C ATOM 1818 O SER B 304 36.399 45.035 −1.693 1.00 94.27 O ATOM 1819 CB SER B 304 33.957 43.306 −0.870 1.00 96.03 C ATOM 1820 OG SER B 304 35.168 42.716 −0.438 1.00 96.47 O ATOM 1821 N PRO B 305 34.713 46.517 −1.507 1.00 92.25 N ATOM 1822 CA PRO B 305 35.564 47.660 −1.163 1.00 90.03 C ATOM 1823 C PRO B 305 36.325 47.470 0.143 1.00 87.64 C ATOM 1824 O PRO B 305 36.170 46.462 0.832 1.00 87.52 O ATOM 1825 CB PRO B 305 34.571 48.818 −1.073 1.00 90.88 C ATOM 1826 CG PRO B 305 33.485 48.412 −2.014 1.00 91.99 C ATOM 1827 CD PRO B 305 33.317 46.952 −1.683 1.00 92.24 C ATOM 1828 N GLU B 306 37.149 48.458 0.469 1.00 84.58 N ATOM 1829 CA GLU B 306 37.944 48.447 1.687 1.00 80.75 C ATOM 1830 C GLU B 306 37.022 48.847 2.842 1.00 76.69 C ATOM 1831 O GLU B 306 36.143 49.693 2.677 1.00 75.73 O ATOM 1832 CB GLU B 306 39.095 49.451 1.540 1.00 82.18 C ATOM 1833 CG GLU B 306 40.088 49.503 2.690 1.00 83.86 C ATOM 1834 CD GLU B 306 41.032 50.696 2.582 1.00 85.10 C ATOM 1835 OE1 GLU B 306 41.781 50.786 1.584 1.00 85.38 O ATOM 1836 OE2 GLU B 306 41.020 51.553 3.494 1.00 85.08 O ATOM 1837 N PRO B 307 37.193 48.223 4.017 1.00 73.12 N ATOM 1838 CA PRO B 307 36.360 48.539 5.185 1.00 69.76 C ATOM 1839 C PRO B 307 36.742 49.878 5.824 1.00 66.56 C ATOM 1840 O PRO B 307 37.926 50.193 5.957 1.00 64.97 O ATOM 1841 CB PRO B 307 36.628 47.368 6.136 1.00 70.02 C ATOM 1842 CG PRO B 307 37.091 46.264 5.224 1.00 71.66 C ATOM 1843 CD PRO B 307 37.970 46.996 4.253 1.00 72.14 C ATOM 1844 N ARG B 308 35.742 50.663 6.217 1.00 63.07 N ATOM 1845 CA ARG B 308 35.998 51.948 6.860 1.00 59.50 C ATOM 1846 C ARG B 308 35.120 52.134 8.088 1.00 56.46 C ATOM 1847 O ARG B 308 34.031 51.566 8.183 1.00 55.95 O ATOM 1848 CB ARG B 308 35.745 53.109 5.896 1.00 60.12 C ATOM 1849 CG ARG B 308 36.675 53.175 4.704 1.00 62.24 C ATOM 1850 CD ARG B 308 36.430 54.452 3.914 1.00 64.63 C ATOM 1851 NE ARG B 308 37.145 54.461 2.640 1.00 67.72 N ATOM 1852 CZ ARG B 308 37.166 55.491 1.797 1.00 68.01 C ATOM 1853 NH1 ARG B 308 36.513 56.609 2.091 1.00 68.04 N ATOM 1854 NH2 ARG B 308 37.831 55.399 0.652 1.00 68.32 N ATOM 1855 N LEU B 309 35.603 52.934 9.030 1.00 52.29 N ATOM 1856 CA LEU B 309 34.857 53.212 10.244 1.00 48.71 C ATOM 1857 C LEU B 309 34.053 54.486 10.070 1.00 46.92 C ATOM 1858 O LEU B 309 34.495 55.419 9.398 1.00 47.41 O ATOM 1859 CB LEU B 309 35.809 53.358 11.429 1.00 47.87 C ATOM 1860 CG LEU B 309 36.441 52.060 11.931 1.00 47.25 C ATOM 1861 CD1 LEU B 309 37.403 52.377 13.069 1.00 48.09 C ATOM 1862 CD2 LEU B 309 35.352 51.098 12.399 1.00 45.50 C ATOM 1863 N PHE B 310 32.867 54.520 10.673 1.00 44.70 N ATOM 1864 CA PHE B 310 31.987 55.685 10.591 1.00 41.73 C ATOM 1865 C PHE B 310 31.218 55.854 11.889 1.00 40.76 C ATOM 1866 O PHE B 310 30.862 54.865 12.524 1.00 42.19 O ATOM 1867 CB PHE B 310 30.956 55.522 9.465 1.00 41.12 C ATOM 1868 CG PHE B 310 31.552 55.318 8.105 1.00 38.93 C ATOM 1869 CD1 PHE B 310 31.986 54.064 7.702 1.00 37.47 C ATOM 1870 CD2 PHE B 310 31.683 56.390 7.223 1.00 40.56 C ATOM 1871 CE1 PHE B 310 32.542 53.878 6.444 1.00 37.92 C ATOM 1872 CE2 PHE B 310 32.242 56.212 5.961 1.00 37.25 C ATOM 1873 CZ PHE B 310 32.671 54.955 5.573 1.00 36.90 C ATOM 1874 N THR B 311 30.955 57.100 12.281 1.00 38.12 N ATOM 1875 CA THR B 311 30.174 57.345 13.489 1.00 35.14 C ATOM 1876 C THR B 311 28.716 57.104 13.087 1.00 33.93 C ATOM 1877 O THR B 311 28.398 56.982 11.894 1.00 33.31 O ATOM 1878 CB THR B 311 30.296 58.803 14.007 1.00 34.64 C ATOM 1879 OG1 THR B 311 29.566 59.673 13.139 1.00 34.01 O ATOM 1880 CG2 THR B 311 31.753 59.251 14.063 1.00 34.36 C ATOM 1881 N PRO B 312 27.807 57.034 14.070 1.00 32.38 N ATOM 1882 CA PRO B 312 26.414 56.799 13.686 1.00 31.44 C ATOM 1883 C PRO B 312 25.847 57.830 12.720 1.00 31.83 C ATOM 1884 O PRO B 312 25.191 57.468 11.738 1.00 29.74 O ATOM 1885 CB PRO B 312 25.695 56.764 15.026 1.00 30.31 C ATOM 1886 CG PRO B 312 26.727 56.090 15.904 1.00 31.27 C ATOM 1887 CD PRO B 312 27.996 56.828 15.518 1.00 30.88 C ATOM 1888 N GLU B 313 26.092 59.109 12.968 1.00 32.84 N ATOM 1889 CA GLU B 313 25.552 60.102 12.048 1.00 36.95 C ATOM 1890 C GLU B 313 26.130 59.936 10.647 1.00 35.86 C ATOM 1891 O GLU B 313 25.399 60.028 9.666 1.00 37.73 O ATOM 1892 CB GLU B 313 25.768 61.533 12.572 1.00 40.35 C ATOM 1893 CG GLU B 313 27.158 61.866 13.072 1.00 48.07 C ATOM 1894 CD GLU B 313 28.160 62.071 11.956 1.00 53.14 C ATOM 1895 OE1 GLU B 313 27.739 62.435 10.835 1.00 56.07 O ATOM 1896 OE2 GLU B 313 29.373 61.893 12.208 1.00 56.39 O ATOM 1897 N GLU B 314 27.430 59.669 10.548 1.00 35.90 N ATOM 1898 CA GLU B 314 28.065 59.487 9.243 1.00 36.50 C ATOM 1899 C GLU B 314 27.489 58.270 8.507 1.00 36.42 C ATOM 1900 O GLU B 314 27.220 58.332 7.307 1.00 33.77 O ATOM 1901 CB GLU B 314 29.587 59.291 9.387 1.00 39.57 C ATOM 1902 CG GLU B 314 30.356 60.423 10.075 1.00 43.63 C ATOM 1903 CD GLU B 314 31.860 60.150 10.172 1.00 46.74 C ATOM 1904 OE1 GLU B 314 32.247 59.041 10.607 1.00 44.49 O ATOM 1905 OE2 GLU B 314 32.658 61.049 9.817 1.00 48.52 O ATOM 1906 N PHE B 315 27.313 57.164 9.232 1.00 34.16 N ATOM 1907 CA PHE B 315 26.803 55.931 8.637 1.00 32.79 C ATOM 1908 C PHE B 315 25.391 56.068 8.077 1.00 33.32 C ATOM 1909 O PHE B 315 25.111 55.653 6.946 1.00 32.68 O ATOM 1910 CB PHE B 315 26.818 54.797 9.670 1.00 30.68 C ATOM 1911 CG PHE B 315 26.395 53.459 9.112 1.00 30.52 C ATOM 1912 CD1 PHE B 315 27.344 52.569 8.595 1.00 28.74 C ATOM 1913 CD2 PHE B 315 25.049 53.085 9.105 1.00 28.69 C ATOM 1914 CE1 PHE B 315 26.960 51.331 8.086 1.00 27.98 C ATOM 1915 CE2 PHE B 315 24.650 51.844 8.596 1.00 26.95 C ATOM 1916 CZ PHE B 315 25.603 50.967 8.088 1.00 29.41 C ATOM 1917 N PHE B 316 24.497 56.652 8.860 1.00 33.65 N ATOM 1918 CA PHE B 316 23.130 56.777 8.405 1.00 36.80 C ATOM 1919 C PHE B 316 22.885 57.866 7.381 1.00 39.29 C ATOM 1920 O PHE B 316 21.802 57.948 6.804 1.00 40.21 O ATOM 1921 CB PHE B 316 22.195 56.888 9.608 1.00 35.12 C ATOM 1922 CG PHE B 316 22.153 55.627 10.421 1.00 34.42 C ATOM 1923 CD1 PHE B 316 23.028 55.441 11.491 1.00 33.83 C ATOM 1924 CD2 PHE B 316 21.312 54.578 10.049 1.00 32.73 C ATOM 1925 CE1 PHE B 316 23.072 54.222 12.176 1.00 35.74 C ATOM 1926 CE2 PHE B 316 21.346 53.353 10.723 1.00 31.66 C ATOM 1927 CZ PHE B 316 22.225 53.170 11.786 1.00 32.51 C ATOM 1928 N ARG B 317 23.890 58.703 7.147 1.00 40.85 N ATOM 1929 CA ARG B 317 23.758 59.723 6.122 1.00 42.36 C ATOM 1930 C ARG B 317 24.001 58.947 4.825 1.00 41.17 C ATOM 1931 O ARG B 317 23.232 59.056 3.871 1.00 41.74 O ATOM 1932 CB ARG B 317 24.799 60.832 6.319 1.00 45.58 C ATOM 1933 CG ARG B 317 24.458 61.797 7.460 1.00 51.23 C ATOM 1934 CD ARG B 317 25.622 62.740 7.790 1.00 54.05 C ATOM 1935 NE ARG B 317 25.270 63.743 8.798 1.00 54.75 N ATOM 1936 CZ ARG B 317 26.132 64.607 9.338 1.00 56.14 C ATOM 1937 NH1 ARG B 317 27.410 64.599 8.977 1.00 57.31 N ATOM 1938 NH2 ARG B 317 25.715 65.490 10.236 1.00 56.15 N ATOM 1939 N ILE B 318 25.055 58.133 4.816 1.00 39.36 N ATOM 1940 CA ILE B 318 25.391 57.306 3.657 1.00 38.03 C ATOM 1941 C ILE B 318 24.245 56.340 3.371 1.00 36.22 C ATOM 1942 O ILE B 318 24.029 55.926 2.232 1.00 36.42 O ATOM 1943 CB ILE B 318 26.676 56.476 3.911 1.00 39.68 C ATOM 1944 CG1 ILE B 318 27.919 57.346 3.707 1.00 40.60 C ATOM 1945 CG2 ILE B 318 26.723 55.270 2.973 1.00 37.16 C ATOM 1946 CD1 ILE B 318 27.986 58.564 4.591 1.00 44.51 C ATOM 1947 N PHE B 319 23.525 55.978 4.425 1.00 34.28 N ATOM 1948 CA PHE B 319 22.397 55.066 4.334 1.00 33.54 C ATOM 1949 C PHE B 319 21.210 55.724 3.615 1.00 34.34 C ATOM 1950 O PHE B 319 20.709 55.209 2.609 1.00 30.32 O ATOM 1951 CB PHE B 319 21.985 54.645 5.747 1.00 32.93 C ATOM 1952 CG PHE B 319 20.712 53.853 5.806 1.00 32.12 C ATOM 1953 CD1 PHE B 319 20.717 52.481 5.585 1.00 35.73 C ATOM 1954 CD2 PHE B 319 19.510 54.473 6.128 1.00 32.66 C ATOM 1955 CE1 PHE B 319 19.542 51.734 5.695 1.00 32.65 C ATOM 1956 CE2 PHE B 319 18.328 53.734 6.237 1.00 31.79 C ATOM 1957 CZ PHE B 319 18.347 52.364 6.022 1.00 32.56 C ATOM 1958 N ASN B 320 20.757 56.858 4.139 1.00 35.81 N ATOM 1959 CA ASN B 320 19.631 57.559 3.536 1.00 39.77 C ATOM 1960 C ASN B 320 19.920 57.913 2.083 1.00 41.47 C ATOM 1961 O ASN B 320 19.079 57.720 1.211 1.00 39.25 O ATOM 1962 CB ASN B 320 19.304 58.824 4.324 1.00 39.83 C ATOM 1963 CG ASN B 320 18.825 58.527 5.731 1.00 42.12 C ATOM 1964 OD1 ASN B 320 17.933 57.699 5.941 1.00 43.16 O ATOM 1965 ND2 ASN B 320 19.407 59.214 6.706 1.00 43.50 N ATOM 1966 N ARG B 321 21.119 58.420 1.823 1.00 45.27 N ATOM 1967 CA ARG B 321 21.498 58.780 0.464 1.00 50.92 C ATOM 1968 C ARG B 321 21.341 57.581 −0.461 1.00 51.05 C ATOM 1969 O ARG B 321 20.706 57.674 −1.510 1.00 50.54 O ATOM 1970 CB ARG B 321 22.946 59.269 0.436 1.00 54.83 C ATOM 1971 CG ARG B 321 23.177 60.518 1.268 1.00 61.05 C ATOM 1972 CD ARG B 321 24.652 60.702 1.601 1.00 65.80 C ATOM 1973 NE ARG B 321 24.847 61.701 2.650 1.00 69.86 N ATOM 1974 CZ ARG B 321 25.967 61.839 3.353 1.00 71.34 C ATOM 1975 NH1 ARG B 321 27.004 61.040 3.124 1.00 71.44 N ATOM 1976 NH2 ARG B 321 26.049 62.775 4.289 1.00 72.83 N ATOM 1977 N SER B 322 21.918 56.452 −0.060 1.00 52.87 N ATOM 1978 CA SER B 322 21.851 55.230 −0.855 1.00 53.43 C ATOM 1979 C SER B 322 20.407 54.836 −1.151 1.00 55.25 C ATOM 1980 O SER B 322 20.074 54.476 −2.281 1.00 55.67 O ATOM 1981 CB SER B 322 22.565 54.090 −0.128 1.00 52.66 C ATOM 1982 OG SER B 322 23.935 54.388 0.064 1.00 50.92 O ATOM 1983 N ILE B 323 19.552 54.900 −0.136 1.00 56.46 N ATOM 1984 CA ILE B 323 18.148 54.563 −0.319 1.00 58.62 C ATOM 1985 C ILE B 323 17.528 55.554 −1.292 1.00 60.36 C ATOM 1986 O ILE B 323 16.926 55.166 −2.292 1.00 60.43 O ATOM 1987 CB ILE B 323 17.380 54.619 1.017 1.00 59.22 C ATOM 1988 CG1 ILE B 323 17.757 53.408 1.873 1.00 58.94 C ATOM 1989 CG2 ILE B 323 15.879 54.662 0.765 1.00 58.59 C ATOM 1990 CD1 ILE B 323 17.075 53.382 3.210 1.00 59.07 C ATOM 1991 N ASP B 324 17.685 56.839 −0.991 1.00 62.51 N ATOM 1992 CA ASP B 324 17.157 57.896 −1.841 1.00 64.88 C ATOM 1993 C ASP B 324 17.688 57.746 −3.270 1.00 65.15 C ATOM 1994 O ASP B 324 17.095 58.260 −4.218 1.00 63.55 O ATOM 1995 CB ASP B 324 17.549 59.267 −1.277 1.00 67.65 C ATOM 1996 CG ASP B 324 16.784 59.626 −0.004 1.00 70.52 C ATOM 1997 OD1 ASP B 324 16.844 58.866 0.989 1.00 71.17 O ATOM 1998 OD2 ASP B 324 16.120 60.685 0.005 1.00 73.09 O ATOM 1999 N ALA B 325 18.800 57.029 −3.417 1.00 65.84 N ATOM 2000 CA ALA B 325 19.409 56.810 −4.726 1.00 68.05 C ATOM 2001 C ALA B 325 18.540 55.957 −5.648 1.00 69.79 C ATOM 2002 O ALA B 325 18.808 55.860 −6.845 1.00 70.12 O ATOM 2003 CB ALA B 325 20.778 56.168 −4.566 1.00 67.52 C ATOM 2004 N PHE B 326 17.506 55.332 −5.095 1.00 71.53 N ATOM 2005 CA PHE B 326 16.612 54.512 −5.901 1.00 73.81 C ATOM 2006 C PHE B 326 15.510 55.341 −6.538 1.00 76.59 C ATOM 2007 O PHE B 326 14.521 54.802 −7.031 1.00 77.23 O ATOM 2008 CB PHE B 326 15.994 53.398 −5.060 1.00 73.16 C ATOM 2009 CG PHE B 326 16.857 52.184 −4.953 1.00 72.21 C ATOM 2010 CD1 PHE B 326 18.058 52.229 −4.260 1.00 71.61 C ATOM 2011 CD2 PHE B 326 16.488 51.003 −5.583 1.00 72.42 C ATOM 2012 CE1 PHE B 326 18.882 51.116 −4.198 1.00 71.32 C ATOM 2013 CE2 PHE B 326 17.308 49.880 −5.528 1.00 72.69 C ATOM 2014 CZ PHE B 326 18.508 49.938 −4.834 1.00 71.79 C ATOM 2015 N LYS B 327 15.685 56.657 −6.515 1.00 79.77 N ATOM 2016 CA LYS B 327 14.725 57.579 −7.107 1.00 82.73 C ATOM 2017 C LYS B 327 15.459 58.374 −8.176 1.00 84.67 C ATOM 2018 O LYS B 327 14.960 58.570 −9.285 1.00 85.16 O ATOM 2019 CB LYS B 327 14.174 58.536 −6.047 1.00 83.44 C ATOM 2020 CG LYS B 327 13.281 59.630 −6.619 1.00 85.27 C ATOM 2021 CD LYS B 327 12.887 60.652 −5.562 1.00 86.20 C ATOM 2022 CE LYS B 327 12.049 61.772 −6.169 1.00 86.76 C ATOM 2023 NZ LYS B 327 11.690 62.816 −5.163 1.00 86.99 N ATOM 2024 N ASP B 328 16.656 58.824 −7.821 1.00 87.12 N ATOM 2025 CA ASP B 328 17.493 59.601 −8.720 1.00 89.44 C ATOM 2026 C ASP B 328 18.422 58.694 −9.523 1.00 89.84 C ATOM 2027 O ASP B 328 19.617 58.966 −9.647 1.00 89.93 O ATOM 2028 CB ASP B 328 18.311 60.617 −7.916 1.00 91.16 C ATOM 2029 CG ASP B 328 17.436 61.629 −7.194 1.00 92.98 C ATOM 2030 OD1 ASP B 328 16.764 62.428 −7.880 1.00 93.99 O ATOM 2031 OD2 ASP B 328 17.413 61.623 −5.944 1.00 93.57 O ATOM 2032 N PHE B 329 17.864 57.616 −10.063 1.00 90.47 N ATOM 2033 CA PHE B 329 18.635 56.669 −10.862 1.00 91.54 C ATOM 2034 C PHE B 329 17.788 56.160 −12.024 1.00 91.50 C ATOM 2035 O PHE B 329 17.420 54.984 −12.076 1.00 91.13 O ATOM 2036 CB PHE B 329 19.094 55.493 −9.995 1.00 92.88 C ATOM 2037 CG PHE B 329 19.963 54.497 −10.719 1.00 94.37 C ATOM 2038 CD1 PHE B 329 20.407 53.354 −10.068 1.00 95.79 C ATOM 2039 CD2 PHE B 329 20.331 54.692 −12.048 1.00 95.63 C ATOM 2040 CE1 PHE B 329 21.201 52.419 −10.725 1.00 96.80 C ATOM 2041 CE2 PHE B 329 21.123 53.765 −12.715 1.00 96.49 C ATOM 2042 CZ PHE B 329 21.559 52.625 −12.052 1.00 97.15 C ATOM 2043 N VAL B 330 17.489 57.056 −12.957 1.00 91.01 N ATOM 2044 CA VAL B 330 16.687 56.715 −14.123 1.00 90.86 C ATOM 2045 C VAL B 330 17.532 56.789 −15.395 1.00 90.35 C ATOM 2046 O VAL B 330 17.000 56.915 −16.500 1.00 90.30 O ATOM 2047 CB VAL B 330 15.477 57.673 −14.259 1.00 91.42 C ATOM 2048 CG1 VAL B 330 14.548 57.510 −13.063 1.00 91.85 C ATOM 2049 CG2 VAL B 330 15.959 59.117 −14.359 1.00 91.34 C ATOM 2050 N VAL B 331 18.849 56.700 −15.232 1.00 88.83 N ATOM 2051 CA VAL B 331 19.766 56.771 −16.364 1.00 87.12 C ATOM 2052 C VAL B 331 21.032 55.949 −16.132 1.00 85.40 C ATOM 2053 O VAL B 331 21.325 55.551 −15.004 1.00 85.03 O ATOM 2054 CB VAL B 331 20.168 58.237 −16.643 1.00 87.73 C ATOM 2055 CG1 VAL B 331 18.994 58.993 −17.249 1.00 88.14 C ATOM 2056 CG2 VAL B 331 20.600 58.911 −15.347 1.00 87.18 C ATOM 2057 N ALA B 332 21.776 55.698 −17.207 1.00 83.14 N ATOM 2058 CA ALA B 332 23.015 54.927 −17.128 1.00 81.00 C ATOM 2059 C ALA B 332 23.944 55.274 −18.288 1.00 79.56 C ATOM 2060 O ALA B 332 25.117 55.595 −18.086 1.00 78.95 O ATOM 2061 CB ALA B 332 22.706 53.436 −17.135 1.00 81.62 C ATOM 2062 N SER B 333 23.417 55.201 −19.505 1.00 77.72 N ATOM 2063 CA SER B 333 24.196 55.519 −20.696 1.00 75.21 C ATOM 2064 C SER B 333 24.292 57.035 −20.825 1.00 73.63 C ATOM 2065 O SER B 333 25.081 57.555 −21.618 1.00 72.74 O ATOM 2066 CB SER B 333 23.519 54.944 −21.941 1.00 74.54 C ATOM 2067 OG SER B 333 23.284 53.556 −21.797 1.00 74.58 O ATOM 2068 N GLU B 334 23.481 57.732 −20.032 1.00 71.81 N ATOM 2069 CA GLU B 334 23.440 59.191 −20.038 1.00 70.21 C ATOM 2070 C GLU B 334 24.158 59.803 −18.841 1.00 67.79 C ATOM 2071 O GLU B 334 23.853 60.922 −18.432 1.00 66.60 O ATOM 2072 CB GLU B 334 21.987 59.671 −20.057 1.00 71.91 C ATOM 2073 CG GLU B 334 21.201 59.220 −21.274 1.00 73.77 C ATOM 2074 CD GLU B 334 19.738 59.608 −21.199 1.00 75.72 C ATOM 2075 OE1 GLU B 334 19.039 59.128 −20.282 1.00 76.13 O ATOM 2076 OE2 GLU B 334 19.286 60.395 −22.057 1.00 77.49 O ATOM 2077 N THR B 335 25.106 59.067 −18.277 1.00 65.94 N ATOM 2078 CA THR B 335 25.866 59.566 −17.136 1.00 64.40 C ATOM 2079 C THR B 335 27.359 59.421 −17.398 1.00 63.02 C ATOM 2080 O THR B 335 27.773 58.942 −18.458 1.00 63.10 O ATOM 2081 CB THR B 335 25.515 58.810 −15.832 1.00 64.99 C ATOM 2082 OG1 THR B 335 25.922 57.441 −15.946 1.00 63.15 O ATOM 2083 CG2 THR B 335 24.016 58.874 −15.565 1.00 63.98 C ATOM 2084 N SER B 336 28.164 59.823 −16.423 1.00 60.77 N ATOM 2085 CA SER B 336 29.609 59.761 −16.557 1.00 59.57 C ATOM 2086 C SER B 336 30.201 58.391 −16.236 1.00 58.18 C ATOM 2087 O SER B 336 29.493 57.462 −15.848 1.00 56.96 O ATOM 2088 CB SER B 336 30.249 60.808 −15.650 1.00 60.02 C ATOM 2089 OG SER B 336 29.972 60.524 −14.291 1.00 61.00 O ATOM 2090 N ASP B 337 31.514 58.288 −16.406 1.00 56.54 N ATOM 2091 CA ASP B 337 32.246 57.064 −16.128 1.00 56.72 C ATOM 2092 C ASP B 337 32.198 56.783 −14.625 1.00 56.84 C ATOM 2093 O ASP B 337 31.476 57.451 −13.882 1.00 56.58 O ATOM 2094 CB ASP B 337 33.700 57.215 −16.588 1.00 55.51 C ATOM 2095 CG ASP B 337 34.432 58.327 −15.857 1.00 54.76 C ATOM 2096 OD1 ASP B 337 35.542 58.699 −16.292 1.00 55.99 O ATOM 2097 OD2 ASP B 337 33.904 58.828 −14.842 1.00 52.06 O ATOM 2098 N CYS B 338 32.975 55.804 −14.177 1.00 55.69 N ATOM 2099 CA CYS B 338 32.994 55.454 −12.764 1.00 57.24 C ATOM 2100 C CYS B 338 34.349 55.696 −12.110 1.00 57.23 C ATOM 2101 O CYS B 338 34.680 55.079 −11.099 1.00 56.86 O ATOM 2102 CB CYS B 338 32.580 53.993 −12.579 1.00 56.06 C ATOM 2103 SG CYS B 338 30.835 53.650 −12.996 1.00 59.59 S ATOM 2104 N VAL B 339 35.118 56.612 −12.686 1.00 57.28 N ATOM 2105 CA VAL B 339 36.438 56.950 −12.173 1.00 58.39 C ATOM 2106 C VAL B 339 36.526 58.443 −11.854 1.00 58.18 C ATOM 2107 O VAL B 339 35.728 59.237 −12.345 1.00 57.22 O ATOM 2108 CB VAL B 339 37.529 56.586 −13.211 1.00 59.55 C ATOM 2109 CG1 VAL B 339 38.908 56.959 −12.689 1.00 59.58 C ATOM 2110 CG2 VAL B 339 37.466 55.101 −13.522 1.00 60.35 C ATOM 2111 N VAL B 340 37.497 58.815 −11.024 1.00 58.73 N ATOM 2112 CA VAL B 340 37.704 60.207 −10.652 1.00 59.48 C ATOM 2113 C VAL B 340 39.150 60.612 −10.941 1.00 61.15 C ATOM 2114 O VAL B 340 40.067 60.225 −10.216 1.00 61.61 O ATOM 2115 CB VAL B 340 37.420 60.440 −9.151 1.00 58.62 C ATOM 2116 CG1 VAL B 340 37.637 61.912 −8.798 1.00 56.58 C ATOM 2117 CG2 VAL B 340 36.010 60.011 −8.818 1.00 57.68 C ATOM 2118 N SER B 341 39.345 61.390 −12.002 1.00 62.42 N ATOM 2119 CA SER B 341 40.674 61.858 −12.389 1.00 64.38 C ATOM 2120 C SER B 341 40.636 62.455 −13.790 1.00 65.42 C ATOM 2121 O SER B 341 40.753 61.734 −14.784 1.00 66.24 O ATOM 2122 CB SER B 341 41.681 60.707 −12.346 1.00 64.35 C TER 2123 SER B 341 ATOM 2124 N THR C 409 25.721 30.038 33.359 1.00 119.52 N ATOM 2125 CA THR C 409 24.769 31.115 33.121 1.00 119.16 C ATOM 2126 C THR C 409 24.295 31.124 31.671 1.00 118.62 C ATOM 2127 O THR C 409 25.071 30.866 30.750 1.00 118.27 O ATOM 2128 CB THR C 409 25.389 32.489 33.456 1.00 119.49 C ATOM 2129 OG1 THR C 409 25.640 32.569 34.863 1.00 119.51 O ATOM 2130 CG2 THR C 409 24.454 33.616 33.052 1.00 119.66 C ATOM 2131 N ASN C 410 23.011 31.417 31.484 1.00 117.91 N ATOM 2132 CA ASN C 410 22.409 31.476 30.157 1.00 116.50 C ATOM 2133 C ASN C 410 22.569 32.882 29.600 1.00 115.36 C ATOM 2134 O ASN C 410 21.656 33.702 29.701 1.00 115.48 O ATOM 2135 CB ASN C 410 20.935 31.116 30.238 1.00 116.84 C ATOM 2136 N ASN C 411 23.734 33.154 29.018 1.00 113.54 N ATOM 2137 CA ASN C 411 24.026 34.466 28.451 1.00 111.04 C ATOM 2138 C ASN C 411 23.019 34.864 27.380 1.00 108.27 C ATOM 2139 O ASN C 411 22.802 34.135 26.412 1.00 108.21 O ATOM 2140 CB ASN C 411 25.442 34.486 27.873 1.00 112.37 C ATOM 2141 CG ASN C 411 26.505 34.328 28.941 1.00 113.08 C ATOM 2142 OD1 ASN C 411 26.606 35.145 29.857 1.00 113.31 O ATOM 2143 ND2 ASN C 411 27.301 33.271 28.833 1.00 113.72 N ATOM 2144 N VAL C 412 22.412 36.032 27.571 1.00 104.37 N ATOM 2145 CA VAL C 412 21.410 36.554 26.651 1.00 99.13 C ATOM 2146 C VAL C 412 21.977 36.814 25.260 1.00 94.12 C ATOM 2147 O VAL C 412 22.346 37.938 24.915 1.00 94.18 O ATOM 2148 CB VAL C 412 20.787 37.854 27.205 1.00 100.42 C ATOM 2149 CG1 VAL C 412 19.645 38.317 26.309 1.00 100.54 C ATOM 2150 CG2 VAL C 412 20.291 37.615 28.621 1.00 100.43 C ATOM 2151 N LYS C 413 22.042 35.742 24.479 1.00 87.81 N ATOM 2152 CA LYS C 413 22.533 35.751 23.105 1.00 80.16 C ATOM 2153 C LYS C 413 21.637 34.732 22.408 1.00 74.79 C ATOM 2154 O LYS C 413 21.057 35.003 21.350 1.00 72.74 O ATOM 2155 CB LYS C 413 23.992 35.301 23.060 1.00 81.15 C ATOM 2156 N ASP C 414 21.540 33.554 23.025 1.00 67.32 N ATOM 2157 CA ASP C 414 20.687 32.486 22.535 1.00 58.95 C ATOM 2158 C ASP C 414 19.291 33.054 22.731 1.00 50.71 C ATOM 2159 O ASP C 414 18.411 32.926 21.877 1.00 48.37 O ATOM 2160 CB ASP C 414 20.842 31.235 23.405 1.00 64.38 C ATOM 2161 CG ASP C 414 22.196 30.571 23.249 1.00 68.30 C ATOM 2162 OD1 ASP C 414 22.477 30.055 22.140 1.00 69.88 O ATOM 2163 OD2 ASP C 414 22.973 30.563 24.235 1.00 69.38 O ATOM 2164 N VAL C 415 19.116 33.689 23.883 1.00 40.98 N ATOM 2165 CA VAL C 415 17.858 34.308 24.253 1.00 35.05 C ATOM 2166 C VAL C 415 17.410 35.298 23.173 1.00 34.05 C ATOM 2167 O VAL C 415 16.262 35.254 22.722 1.00 32.19 O ATOM 2168 CB VAL C 415 17.997 35.011 25.627 1.00 31.93 C ATOM 2169 CG1 VAL C 415 16.824 35.919 25.891 1.00 32.40 C ATOM 2170 CG2 VAL C 415 18.084 33.953 26.727 1.00 28.81 C ATOM 2171 N THR C 416 18.317 36.177 22.748 1.00 31.45 N ATOM 2172 CA THR C 416 17.995 37.152 21.717 1.00 29.58 C ATOM 2173 C THR C 416 17.517 36.432 20.456 1.00 29.53 C ATOM 2174 O THR C 416 16.511 36.813 19.855 1.00 26.91 O ATOM 2175 CB THR C 416 19.223 38.066 21.386 1.00 30.06 C ATOM 2176 OG1 THR C 416 19.345 39.083 22.390 1.00 30.21 O ATOM 2177 CG2 THR C 416 19.055 38.750 20.016 1.00 28.63 C ATOM 2178 N LYS C 417 18.238 35.388 20.061 1.00 29.46 N ATOM 2179 CA LYS C 417 17.868 34.611 18.880 1.00 29.39 C ATOM 2180 C LYS C 417 16.489 33.965 19.050 1.00 27.59 C ATOM 2181 O LYS C 417 15.664 33.995 18.136 1.00 28.30 C ATOM 2182 CB LYS C 417 18.903 33.509 18.617 1.00 30.97 C ATOM 2183 CG LYS C 417 19.825 33.786 17.439 1.00 34.65 C ATOM 2184 CD LYS C 417 20.818 34.894 17.729 1.00 36.75 C ATOM 2185 CE LYS C 417 22.175 34.311 18.094 1.00 40.95 C ATOM 2186 NZ LYS C 417 22.774 33.558 16.953 1.00 39.53 N ATOM 2187 N LEU C 418 16.251 33.377 20.219 1.00 23.37 N ATOM 2188 CA LEU C 418 14.983 32.715 20.495 1.00 22.30 C ATOM 2189 C LEU C 418 13.811 33.686 20.457 1.00 20.70 C ATOM 2190 O LEU C 418 12.722 33.338 20.017 1.00 21.55 C ATOM 2191 CB LEU C 418 15.038 32.026 21.860 1.00 19.71 C ATOM 2192 CG LEU C 418 13.758 31.375 22.391 1.00 20.40 C ATOM 2193 CD1 LEU C 418 13.230 30.356 21.403 1.00 15.96 C ATOM 2194 CD2 LEU C 418 14.051 30.703 23.733 1.00 16.28 C ATOM 2195 N VAL C 419 14.039 34.907 20.921 1.00 21.24 N ATOM 2196 CA VAL C 419 12.986 35.909 20.934 1.00 19.24 C ATOM 2197 C VAL C 419 12.647 36.402 19.525 1.00 18.54 C ATOM 2198 O VAL C 419 11.477 36.632 19.196 1.00 20.16 C ATOM 2199 CB VAL C 419 13.382 37.067 21.861 1.00 18.08 C ATOM 2200 CG1 VAL C 419 12.374 38.219 21.751 1.00 21.66 C ATOM 2201 CG2 VAL C 419 13.376 36.554 23.302 1.00 15.68 C ATOM 2202 N ALA C 420 13.672 36.533 18.693 1.00 15.15 N ATOM 2203 CA ALA C 420 13.508 36.963 17.317 1.00 17.52 C ATOM 2204 C ALA C 420 12.814 35.852 16.522 1.00 18.92 C ATOM 2205 O ALA C 420 12.155 36.123 15.518 1.00 20.02 O ATOM 2206 CB ALA C 420 14.886 37.273 16.699 1.00 16.86 C ATOM 2207 N ASN C 421 12.979 34.608 16.975 1.00 17.25 N ATOM 2208 CA ASN C 421 12.378 33.447 16.327 1.00 20.11 C ATOM 2209 C ASN C 421 11.025 32.989 16.861 1.00 18.94 C ATOM 2210 O ASN C 421 10.490 31.998 16.396 1.00 22.70 O ATOM 2211 CB ASN C 421 13.329 32.252 16.363 1.00 20.49 C ATOM 2212 CG ASN C 421 14.273 32.226 15.184 1.00 23.76 C ATOM 2213 OD1 ASN C 421 13.956 32.733 14.111 1.00 22.84 O ATOM 2214 ND2 ASN C 421 15.434 31.610 15.370 1.00 26.43 N ATOM 2215 N LEU C 422 10.485 33.684 17.850 1.00 21.69 N ATOM 2216 CA LEU C 422 9.165 33.347 18.402 1.00 21.52 C ATOM 2217 C LEU C 422 8.226 34.462 17.951 1.00 22.96 C ATOM 2218 O LEU C 422 8.628 35.627 17.929 1.00 22.14 O ATOM 2219 CB LEU C 422 9.204 33.318 19.930 1.00 17.36 C ATOM 2220 CG LEU C 422 9.994 32.173 20.569 1.00 19.51 C ATOM 2221 CD1 LEU C 422 10.204 32.467 22.063 1.00 16.94 C ATOM 2222 CD2 LEU C 422 9.237 30.842 20.358 1.00 15.76 C ATOM 2223 N PRO C 423 6.975 34.124 17.568 1.00 24.23 N ATOM 2224 CA PRO C 423 6.047 35.183 17.127 1.00 25.36 C ATOM 2225 C PRO C 423 5.772 36.202 18.228 1.00 25.17 C ATOM 2226 O PRO C 423 5.462 35.831 19.353 1.00 27.09 O ATOM 2227 CB PRO C 423 4.792 34.413 16.691 1.00 22.59 C ATOM 2228 CG PRO C 423 4.928 33.041 17.347 1.00 23.46 C ATOM 2229 CD PRO C 423 6.406 32.778 17.368 1.00 24.55 C ATOM 2230 N LYS C 424 5.903 37.484 17.898 1.00 27.84 N ATOM 2231 CA LYS C 424 5.699 38.562 18.870 1.00 29.74 C ATOM 2232 C LYS C 424 4.366 38.469 19.606 1.00 28.96 C ATOM 2233 O LYS C 424 4.251 38.908 20.744 1.00 25.75 O ATOM 2234 CB LYS C 424 5.783 39.927 18.191 1.00 29.72 C ATOM 2235 CG LYS C 424 7.117 40.251 17.574 1.00 37.16 C ATOM 2236 CD LYS C 424 6.952 41.363 16.524 1.00 40.32 C ATOM 2237 CE LYS C 424 8.218 41.569 15.698 1.00 42.47 C ATOM 2238 NZ LYS C 424 7.945 42.406 14.488 1.00 43.47 N ATOM 2239 N ASP C 425 3.360 37.902 18.957 1.00 28.50 N ATOM 2240 CA ASP C 425 2.059 37.791 19.590 1.00 32.00 C ATOM 2241 C ASP C 425 1.843 36.416 20.215 1.00 28.99 C ATOM 2242 O ASP C 425 0.725 36.053 20.534 1.00 29.58 O ATOM 2243 CB ASP C 425 0.951 38.097 18.569 1.00 32.89 C ATOM 2244 CG ASP C 425 0.984 37.156 17.385 1.00 36.03 C ATOM 2245 OD1 ASP C 425 2.071 36.612 17.101 1.00 34.79 O ATOM 2246 OD2 ASP C 425 −0.062 36.968 16.729 1.00 40.18 O ATOM 2247 N TYR C 426 2.910 35.647 20.388 1.00 28.20 N ATOM 2248 CA TYR C 426 2.769 34.326 20.996 1.00 27.47 C ATOM 2249 C TYR C 426 2.865 34.459 22.518 1.00 28.12 C ATOM 2250 O TYR C 426 3.865 34.949 23.044 1.00 31.37 O ATOM 2251 CB TYR C 426 3.861 33.378 20.478 1.00 26.08 C ATOM 2252 CG TYR C 426 3.674 31.949 20.945 1.00 26.36 C ATOM 2253 CD1 TYR C 426 2.494 31.256 20.671 1.00 24.85 C ATOM 2254 CD2 TYR C 426 4.653 31.302 21.688 1.00 24.72 C ATOM 2255 CE1 TYR C 426 2.295 29.961 21.130 1.00 25.05 C ATOM 2256 CE2 TYR C 426 4.461 29.997 22.151 1.00 23.79 C ATOM 2257 CZ TYR C 426 3.283 29.341 21.869 1.00 24.37 C ATOM 2258 OH TYR C 426 3.083 28.066 22.327 1.00 25.86 O ATOM 2259 N MET C 427 1.833 34.023 23.232 1.00 28.78 N ATOM 2260 CA MET C 427 1.830 34.132 24.686 1.00 28.41 C ATOM 2261 C MET C 427 2.356 32.893 25.398 1.00 27.73 C ATOM 2262 O MET C 427 2.018 31.767 25.059 1.00 25.73 O ATOM 2263 CB MET C 427 0.421 34.445 25.194 1.00 31.71 C ATOM 2264 CG MET C 427 −0.223 35.679 24.555 1.00 36.93 C ATOM 2265 SD MET C 427 0.761 37.196 24.702 1.00 41.33 S ATOM 2266 CE MET C 427 0.357 37.679 26.390 1.00 39.85 C ATOM 2267 N ILE C 428 3.185 33.124 26.406 1.00 27.81 N ATOM 2268 CA ILE C 428 3.768 32.052 27.196 1.00 26.77 C ATOM 2269 C ILE C 428 3.160 32.148 28.590 1.00 26.18 C ATOM 2270 O ILE C 428 3.040 33.233 29.145 1.00 24.71 O ATOM 2271 CB ILE C 428 5.305 32.216 27.295 1.00 28.58 C ATOM 2272 CG1 ILE C 428 5.927 32.138 25.893 1.00 27.33 C ATOM 2273 CG2 ILE C 428 5.889 31.165 28.238 1.00 26.23 C ATOM 2274 CD1 ILE C 428 7.422 32.453 25.850 1.00 25.32 C ATOM 2275 N THR C 429 2.769 31.011 29.149 1.00 26.38 N ATOM 2276 CA THR C 429 2.177 30.999 30.479 1.00 26.90 C ATOM 2277 C THR C 429 3.231 30.882 31.556 1.00 25.21 C ATOM 2278 O THR C 429 4.150 30.068 31.461 1.00 24.68 O ATOM 2279 CB THR C 429 1.209 29.811 30.676 1.00 28.90 C ATOM 2280 OG1 THR C 429 0.203 29.835 29.657 1.00 34.43 O ATOM 2281 CG2 THR C 429 0.536 29.910 32.047 1.00 30.79 C ATOM 2282 N LEU C 430 3.081 31.694 32.591 1.00 24.21 N ATOM 2283 CA LEU C 430 4.001 31.668 33.710 1.00 23.59 C ATOM 2284 C LEU C 430 3.270 32.006 35.007 1.00 25.18 C ATOM 2285 O LEU C 430 2.629 33.050 35.125 1.00 24.57 O ATOM 2286 CB LEU C 430 5.156 32.659 33.483 1.00 22.49 C ATOM 2287 CG LEU C 430 6.101 32.909 34.673 1.00 21.79 C ATOM 2288 CD1 LEU C 430 6.910 31.647 34.969 1.00 19.59 C ATOM 2289 CD2 LEU C 430 7.026 34.079 34.368 1.00 20.81 C ATOM 2290 N LYS C 431 3.347 31.102 35.973 1.00 26.18 N ATOM 2291 CA LYS C 431 2.737 31.349 37.267 1.00 29.32 C ATOM 2292 C LYS C 431 3.719 32.292 37.972 1.00 29.35 C ATOM 2293 O LYS C 431 4.625 31.868 38.692 1.00 28.17 O ATOM 2294 CB LYS C 431 2.564 30.035 38.034 1.00 31.78 C ATOM 2295 CG LYS C 431 1.679 28.986 37.322 1.00 30.55 C ATOM 2296 CD LYS C 431 1.500 27.732 38.201 1.00 33.93 C ATOM 2297 CE LYS C 431 0.721 26.599 37.514 1.00 34.68 C ATOM 2298 NZ LYS C 431 1.518 25.866 36.470 1.00 36.88 N ATOM 2299 N TYR C 432 3.530 33.581 37.710 1.00 31.52 N ATOM 2300 CA TYR C 432 4.352 34.664 38.240 1.00 33.55 C ATOM 2301 C TYR C 432 4.262 34.779 39.761 1.00 35.80 C ATOM 2302 O TYR C 432 3.169 34.748 40.330 1.00 36.29 O ATOM 2303 CB TYR C 432 3.905 35.982 37.588 1.00 34.63 C ATOM 2304 CG TYR C 432 4.649 37.223 38.040 1.00 36.39 C ATOM 2305 CD1 TYR C 432 5.912 37.532 37.531 1.00 36.97 C ATOM 2306 CD2 TYR C 432 4.098 38.080 38.993 1.00 35.09 C ATOM 2307 CE1 TYR C 432 6.610 38.666 37.965 1.00 37.33 C ATOM 2308 CE2 TYR C 432 4.786 39.212 39.433 1.00 34.43 C ATOM 2309 CZ TYR C 432 6.039 39.498 38.917 1.00 36.21 C ATOM 2310 OH TYR C 432 6.732 40.599 39.363 1.00 37.69 O ATOM 2311 N VAL C 433 5.417 34.909 40.411 1.00 36.29 N ATOM 2312 CA VAL C 433 5.486 35.055 41.862 1.00 35.95 C ATOM 2313 C VAL C 433 5.433 36.547 42.195 1.00 37.68 C ATOM 2314 O VAL C 433 6.337 37.303 41.846 1.00 37.86 O ATOM 2315 CB VAL C 433 6.799 34.455 42.421 1.00 36.60 C ATOM 2316 CG1 VAL C 433 6.947 34.777 43.906 1.00 31.64 C ATOM 2317 CG2 VAL C 433 6.805 32.956 42.199 1.00 35.80 C ATOM 2318 N PRO C 434 4.356 36.993 42.856 1.00 39.99 N ATOM 2319 CA PRO C 434 4.209 38.408 43.221 1.00 43.19 C ATOM 2320 C PRO C 434 5.296 38.906 44.160 1.00 45.66 C ATOM 2321 O PRO C 434 5.646 38.237 45.126 1.00 46.94 O ATOM 2322 CB PRO C 434 2.820 38.460 43.850 1.00 42.20 C ATOM 2323 CG PRO C 434 2.634 37.050 44.389 1.00 41.37 C ATOM 2324 CD PRO C 434 3.173 36.216 43.267 1.00 38.44 C ATOM 2325 N GLY C 435 5.828 40.086 43.867 1.00 48.42 N ATOM 2326 CA GLY C 435 6.875 40.653 44.694 1.00 51.65 C ATOM 2327 C GLY C 435 8.220 40.622 43.994 1.00 53.74 C ATOM 2328 O GLY C 435 9.183 41.234 44.451 1.00 54.21 O ATOM 2329 N MET C 436 8.267 39.905 42.875 1.00 55.58 N ATOM 2330 CA MET C 436 9.467 39.746 42.053 1.00 57.85 C ATOM 2331 C MET C 436 10.171 41.077 41.781 1.00 57.97 C ATOM 2332 O MET C 436 11.366 41.104 41.499 1.00 57.90 O ATOM 2333 CB MET C 436 9.073 39.086 40.716 1.00 60.24 C ATOM 2334 CG MET C 436 10.117 38.170 40.061 1.00 62.63 C ATOM 2335 SD MET C 436 11.294 38.958 38.921 1.00 66.70 S ATOM 2336 CE MET C 436 10.350 39.014 37.425 1.00 65.33 C ATOM 2337 N ASP C 437 9.435 42.179 41.884 1.00 58.78 N ATOM 2338 CA ASP C 437 10.000 43.494 41.596 1.00 59.01 C ATOM 2339 C ASP C 437 10.399 44.398 42.766 1.00 58.17 C ATOM 2340 O ASP C 437 11.122 45.370 42.564 1.00 58.63 O ATOM 2341 CB ASP C 437 9.056 44.253 40.652 1.00 59.84 C ATOM 2342 CG ASP C 437 7.672 44.451 41.239 1.00 61.99 C ATOM 2343 OD1 ASP C 437 7.187 43.548 41.953 1.00 62.11 O ATOM 2344 OD2 ASP C 437 7.058 45.507 40.971 1.00 63.72 O ATOM 2345 N VAL C 438 9.957 44.100 43.982 1.00 57.08 N ATOM 2346 CA VAL C 438 10.333 44.949 45.113 1.00 57.03 C ATOM 2347 C VAL C 438 10.929 44.203 46.306 1.00 56.72 C ATOM 2348 O VAL C 438 11.658 44.789 47.110 1.00 56.31 O ATOM 2349 CB VAL C 438 9.134 45.800 45.619 1.00 57.87 C ATOM 2350 CG1 VAL C 438 8.678 46.761 44.529 1.00 58.76 C ATOM 2351 CG2 VAL C 438 7.991 44.898 46.059 1.00 57.18 C ATOM 2352 N LEU C 439 10.625 42.916 46.425 1.00 55.85 N ATOM 2353 CA LEU C 439 11.146 42.132 47.534 1.00 55.27 C ATOM 2354 C LEU C 439 12.559 41.640 47.258 1.00 54.28 C ATOM 2355 O LEU C 439 12.969 41.499 46.104 1.00 53.11 O ATOM 2356 CB LEU C 439 10.243 40.924 47.816 1.00 55.76 C ATOM 2357 CG LEU C 439 8.888 41.175 48.477 1.00 56.88 C ATOM 2358 CD1 LEU C 439 8.011 42.009 47.559 1.00 59.05 C ATOM 2359 CD2 LEU C 439 8.218 39.851 48.783 1.00 56.52 C ATOM 2360 N PRO C 440 13.333 41.387 48.324 1.00 53.74 N ATOM 2361 CA PRO C 440 14.699 40.902 48.121 1.00 52.02 C ATOM 2362 C PRO C 440 14.682 39.494 47.528 1.00 50.04 C ATOM 2363 O PRO C 440 13.806 38.682 47.833 1.00 48.79 O ATOM 2364 CB PRO C 440 15.299 40.948 49.529 1.00 52.43 C ATOM 2365 CG PRO C 440 14.116 40.725 50.414 1.00 52.90 C ATOM 2366 CD PRO C 440 13.050 41.583 49.759 1.00 53.29 C ATOM 2367 N SER C 441 15.653 39.234 46.665 1.00 48.29 N ATOM 2368 CA SER C 441 15.818 37.957 45.984 1.00 46.16 C ATOM 2369 C SER C 441 15.447 36.715 46.802 1.00 44.55 C ATOM 2370 O SER C 441 14.661 35.887 46.361 1.00 41.81 O ATOM 2371 CB SER C 441 17.267 37.852 45.500 1.00 45.60 C ATOM 2372 OG SER C 441 17.634 36.516 45.230 1.00 52.84 O ATOM 2373 N HIS C 442 16.006 36.587 47.998 1.00 46.27 N ATOM 2374 CA HIS C 442 15.732 35.417 48.823 1.00 47.87 C ATOM 2375 C HIS C 442 14.251 35.235 49.123 1.00 47.05 C ATOM 2376 O HIS C 442 13.819 34.172 49.573 1.00 46.64 O ATOM 2377 CB HIS C 442 16.550 35.478 50.125 1.00 49.97 C ATOM 2378 CG HIS C 442 16.105 36.539 51.085 1.00 51.99 C ATOM 2379 ND1 HIS C 442 15.059 36.357 51.966 1.00 52.74 N ATOM 2380 CD2 HIS C 442 16.582 37.786 51.318 1.00 51.71 C ATOM 2381 CE1 HIS C 442 14.913 37.446 52.702 1.00 52.93 C ATOM 2382 NE2 HIS C 442 15.824 38.327 52.329 1.00 52.63 N ATOM 2383 N CYS C 443 13.467 36.270 48.861 1.00 46.79 N ATOM 2384 CA CYS C 443 12.042 36.181 49.113 1.00 47.55 C ATOM 2385 C CYS C 443 11.280 35.549 47.957 1.00 44.52 C ATOM 2386 O CYS C 443 10.168 35.066 48.156 1.00 44.07 O ATOM 2387 CB CYS C 443 11.449 37.564 49.396 1.00 52.06 C ATOM 2388 SG CYS C 443 11.991 38.314 50.959 1.00 59.63 S ATOM 2389 N TRP C 444 11.872 35.526 46.762 1.00 41.20 N ATOM 2390 CA TRP C 444 11.158 34.974 45.611 1.00 38.57 C ATOM 2391 C TRP C 444 11.831 34.011 44.615 1.00 36.90 C ATOM 2392 O TRP C 444 11.136 33.181 44.039 1.00 34.96 O ATOM 2393 CB TRP C 444 10.539 36.129 44.812 1.00 35.62 C ATOM 2394 CG TRP C 444 11.547 37.163 44.372 1.00 32.01 C ATOM 2395 CD1 TRP C 444 11.911 38.298 45.043 1.00 32.10 C ATOM 2396 CD2 TRP C 444 12.341 37.131 43.180 1.00 28.95 C ATOM 2397 NE1 TRP C 444 12.887 38.973 44.343 1.00 27.58 N ATOM 2398 CE2 TRP C 444 13.171 38.279 43.199 1.00 26.83 C ATOM 2399 CE3 TRP C 444 12.434 36.245 42.098 1.00 28.17 C ATOM 2400 CZ2 TRP C 444 14.082 38.560 42.182 1.00 25.62 C ATOM 2401 CZ3 TRP C 444 13.344 36.523 41.083 1.00 26.33 C ATOM 2402 CH2 TRP C 444 14.157 37.672 41.134 1.00 28.83 C ATOM 2403 N ILE C 445 13.143 34.110 44.388 1.00 36.37 N ATOM 2404 CA ILE C 445 13.792 33.226 43.408 1.00 37.21 C ATOM 2405 C ILE C 445 13.515 31.735 43.484 1.00 36.05 C ATOM 2406 O ILE C 445 13.457 31.075 42.449 1.00 35.39 O ATOM 2407 CB ILE C 445 15.343 33.377 43.367 1.00 40.95 C ATOM 2408 CG1 ILE C 445 15.898 33.609 44.772 1.00 41.41 C ATOM 2409 CG2 ILE C 445 15.735 34.437 42.348 1.00 41.56 C ATOM 2410 CD1 ILE C 445 15.849 32.377 45.652 1.00 40.58 C ATOM 2411 N SER C 446 13.359 31.194 44.686 1.00 35.89 N ATOM 2412 CA SER C 446 13.104 29.766 44.828 1.00 36.80 C ATOM 2413 C SER C 446 11.899 29.348 43.999 1.00 36.19 C ATOM 2414 O SER C 446 12.014 28.507 43.105 1.00 37.02 O ATOM 2415 CB SER C 446 12.870 29.404 46.297 1.00 39.47 C ATOM 2416 OG SER C 446 12.486 28.044 46.444 1.00 37.74 O ATOM 2417 N GLU C 447 10.744 29.933 44.292 1.00 33.96 N ATOM 2418 CA GLU C 447 9.532 29.606 43.551 1.00 32.24 C ATOM 2419 C GLU C 447 9.635 30.046 42.080 1.00 29.53 C ATOM 2420 O GLU C 447 9.181 29.339 41.183 1.00 28.78 O ATOM 2421 CB GLU C 447 8.309 30.266 44.211 1.00 34.77 C ATOM 2422 CG GLU C 447 6.975 29.899 43.567 1.00 39.16 C ATOM 2423 CD GLU C 447 6.655 28.416 43.690 1.00 42.43 C ATOM 2424 OE1 GLU C 447 5.783 27.919 42.945 1.00 43.28 O ATOM 2425 OE2 GLU C 447 7.275 27.744 44.541 1.00 46.08 O ATOM 2426 N MET C 448 10.240 31.201 41.825 1.00 27.08 N ATOM 2427 CA MET C 448 10.352 31.670 40.449 1.00 28.04 C ATOM 2428 C MET C 448 11.130 30.707 39.567 1.00 27.17 C ATOM 2429 O MET C 448 10.719 30.399 38.446 1.00 26.96 O ATOM 2430 CB MET C 448 11.009 33.047 40.381 1.00 28.47 C ATOM 2431 CG MET C 448 10.954 33.671 38.987 1.00 33.18 C ATOM 2432 SD MET C 448 9.381 34.531 38.559 1.00 40.53 S ATOM 2433 CE MET C 448 8.128 33.296 38.951 1.00 38.78 C ATOM 2434 N VAL C 449 12.264 30.248 40.073 1.00 25.81 N ATOM 2435 CA VAL C 449 13.104 29.322 39.339 1.00 26.02 C ATOM 2436 C VAL C 449 12.311 28.054 39.050 1.00 26.19 C ATOM 2437 O VAL C 449 12.356 27.520 37.936 1.00 27.20 O ATOM 2438 CB VAL C 449 14.398 29.025 40.150 1.00 28.96 C ATOM 2439 CG1 VAL C 449 14.830 27.598 39.989 1.00 30.72 C ATOM 2440 CG2 VAL C 449 15.506 29.964 39.682 1.00 28.33 C ATOM 2441 N VAL C 450 11.560 27.588 40.041 1.00 24.17 N ATOM 2442 CA VAL C 450 10.753 26.391 39.861 1.00 24.70 C ATOM 2443 C VAL C 450 9.697 26.627 38.788 1.00 24.32 C ATOM 2444 O VAL C 450 9.442 25.756 37.946 1.00 24.90 O ATOM 2445 CB VAL C 450 10.056 25.976 41.182 1.00 26.76 C ATOM 2446 CG1 VAL C 450 8.980 24.935 40.914 1.00 24.89 C ATOM 2447 CG2 VAL C 450 11.077 25.404 42.141 1.00 25.53 C ATOM 2448 N GLN C 451 9.094 27.809 38.802 1.00 23.10 N ATOM 2449 CA GLN C 451 8.063 28.114 37.819 1.00 21.98 C ATOM 2450 C GLN C 451 8.625 28.401 36.437 1.00 19.81 C ATOM 2451 O GLN C 451 7.993 28.077 35.437 1.00 21.40 O ATOM 2452 CB GLN C 451 7.196 29.283 38.294 1.00 22.86 C ATOM 2453 CG GLN C 451 6.279 28.940 39.480 1.00 24.71 C ATOM 2454 CD GLN C 451 5.431 27.670 39.270 1.00 25.91 C ATOM 2455 OE1 GLN C 451 5.034 27.346 38.152 1.00 24.23 O ATOM 2456 NE2 GLN C 451 5.139 26.965 40.362 1.00 23.67 N ATOM 2457 N LEU C 452 9.809 29.006 36.376 1.00 20.61 N ATOM 2458 CA LEU C 452 10.432 29.306 35.095 1.00 19.29 C ATOM 2459 C LEU C 452 10.823 27.985 34.454 1.00 21.21 C ATOM 2460 O LEU C 452 10.801 27.842 33.247 1.00 21.48 O ATOM 2461 CB LEU C 452 11.672 30.179 35.285 1.00 20.34 C ATOM 2462 CG LEU C 452 11.460 31.667 35.608 1.00 22.71 C ATOM 2463 CD1 LEU C 452 12.782 32.308 36.035 1.00 19.44 C ATOM 2464 CD2 LEU C 452 10.882 32.382 34.384 1.00 20.12 C ATOM 2465 N SER C 453 11.179 27.014 35.280 1.00 22.75 N ATOM 2466 CA SER C 453 11.559 25.702 34.784 1.00 23.36 C ATOM 2467 C SER C 453 10.345 25.013 34.175 1.00 21.69 C ATOM 2468 O SER C 453 10.426 24.423 33.102 1.00 22.03 C ATOM 2469 CB SER C 453 12.109 24.852 35.927 1.00 23.97 C ATOM 2470 OG SER C 453 12.431 23.548 35.475 1.00 30.62 O ATOM 2471 N ASP C 454 9.211 25.092 34.861 1.00 23.68 N ATOM 2472 CA ASP C 454 7.999 24.456 34.353 1.00 23.36 C ATOM 2473 C ASP C 454 7.540 25.068 33.026 1.00 23.44 C ATOM 2474 O ASP C 454 7.067 24.342 32.140 1.00 18.28 O ATOM 2475 CB ASP C 454 6.849 24.559 35.357 1.00 23.97 C ATOM 2476 CG ASP C 454 5.574 23.933 34.818 1.00 28.33 C ATOM 2477 OD1 ASP C 454 5.591 22.720 34.540 1.00 30.65 O ATOM 2478 OD2 ASP C 454 4.559 24.643 34.646 1.00 32.30 O ATOM 2479 N SER C 455 7.657 26.398 32.911 1.00 20.75 N ATOM 2480 CA SER C 455 7.250 27.105 31.693 1.00 22.16 C ATOM 2481 C SER C 455 8.123 26.745 30.504 1.00 19.56 C ATOM 2482 O SER C 455 7.617 26.526 29.402 1.00 18.40 O ATOM 2483 CB SER C 455 7.293 28.630 31.885 1.00 21.64 C ATOM 2484 OG SER C 455 6.236 29.060 32.720 1.00 24.44 O ATOM 2485 N LEU C 456 9.432 26.700 30.723 1.00 20.20 N ATOM 2486 CA LEU C 456 10.343 26.366 29.639 1.00 22.64 C ATOM 2487 C LEU C 456 10.101 24.929 29.182 1.00 22.40 C ATOM 2488 O LEU C 456 10.031 24.656 27.977 1.00 21.78 O ATOM 2489 CB LEU C 456 11.799 26.558 30.076 1.00 26.72 C ATOM 2490 CG LEU C 456 12.394 27.982 30.077 1.00 30.48 C ATOM 2491 CD1 LEU C 456 12.340 28.603 28.678 1.00 31.06 C ATOM 2492 CD2 LEU C 456 11.635 28.836 31.022 1.00 31.14 C ATOM 2493 N THR C 457 9.956 24.018 30.138 1.00 22.09 N ATOM 2494 CA THR C 457 9.707 22.618 29.810 1.00 27.16 C ATOM 2495 C THR C 457 8.389 22.472 29.049 1.00 27.09 C ATOM 2496 O THR C 457 8.306 21.682 28.109 1.00 29.28 O ATOM 2497 CB THR C 457 9.671 21.726 31.077 1.00 29.54 C ATOM 2498 OG1 THR C 457 10.934 21.797 31.748 1.00 34.82 O ATOM 2499 CG2 THR C 457 9.408 20.276 30.702 1.00 31.05 C ATOM 2500 N ASP C 458 7.361 23.221 29.444 1.00 25.79 N ATOM 2501 CA ASP C 458 6.087 23.149 28.731 1.00 25.04 C ATOM 2502 C ASP C 458 6.288 23.698 27.322 1.00 24.70 C ATOM 2503 O ASP C 458 5.719 23.198 26.357 1.00 23.65 O ATOM 2504 CB ASP C 458 5.003 24.004 29.399 1.00 26.32 C ATOM 2505 CG ASP C 458 4.630 23.524 30.782 1.00 27.77 C ATOM 2506 OD1 ASP C 458 4.830 22.333 31.084 1.00 31.33 O ATOM 2507 OD2 ASP C 458 4.111 24.348 31.567 1.00 28.00 O ATOM 2508 N LEU C 459 7.083 24.756 27.215 1.00 25.26 N ATOM 2509 CA LEU C 459 7.337 25.393 25.919 1.00 27.22 C ATOM 2510 C LEU C 459 8.099 24.451 24.982 1.00 28.01 C ATOM 2511 O LEU C 459 7.850 24.404 23.776 1.00 27.24 O ATOM 2512 CB LEU C 459 8.137 26.690 26.122 1.00 24.90 C ATOM 2513 CG LEU C 459 8.385 27.586 24.908 1.00 26.22 C ATOM 2514 CD1 LEU C 459 7.047 28.089 24.381 1.00 29.21 C ATOM 2515 CD2 LEU C 459 9.266 28.784 25.291 1.00 27.97 C ATOM 2516 N LEU C 460 9.024 23.689 25.551 1.00 29.41 N ATOM 2517 CA LEU C 460 9.831 22.770 24.764 1.00 30.45 C ATOM 2518 C LEU C 460 8.951 21.882 23.891 1.00 30.83 C ATOM 2519 O LEU C 460 9.204 21.730 22.697 1.00 32.84 O ATOM 2520 CB LEU C 460 10.691 21.921 25.700 1.00 29.64 C ATOM 2521 CG LEU C 460 11.838 21.136 25.083 1.00 28.50 C ATOM 2522 CD1 LEU C 460 12.846 22.088 24.450 1.00 24.94 C ATOM 2523 CD2 LEU C 460 12.495 20.312 26.177 1.00 28.74 C ATOM 2524 N ASP C 461 7.906 21.315 24.480 1.00 31.68 N ATOM 2525 CA ASP C 461 6.988 20.445 23.746 1.00 33.28 C ATOM 2526 C ASP C 461 6.234 21.096 22.581 1.00 31.27 C ATOM 2527 O ASP C 461 5.533 20.412 21.834 1.00 30.90 O ATOM 2528 CB ASP C 461 5.974 19.822 24.708 1.00 38.72 C ATOM 2529 CG ASP C 461 6.624 18.885 25.705 1.00 46.26 C ATOM 2530 OD1 ASP C 461 7.253 19.374 26.674 1.00 48.70 O ATOM 2531 OD2 ASP C 461 6.521 17.653 25.510 1.00 50.00 O ATOM 2532 N LYS C 462 6.359 22.408 22.425 1.00 27.57 N ATOM 2533 CA LYS C 462 5.680 23.080 21.327 1.00 25.35 C ATOM 2534 C LYS C 462 6.564 23.086 20.079 1.00 23.43 C ATOM 2535 O LYS C 462 6.146 23.532 19.019 1.00 24.64 O ATOM 2536 CB LYS C 462 5.324 24.518 21.716 1.00 24.71 C ATOM 2537 CG LYS C 462 4.388 24.630 22.919 1.00 25.36 C ATOM 2538 CD LYS C 462 3.081 23.877 22.675 1.00 29.01 C ATOM 2539 CE LYS C 462 2.079 24.115 23.800 1.00 31.24 C ATOM 2540 NZ LYS C 462 2.665 23.788 25.129 1.00 34.34 N ATOM 2541 N PHE C 463 7.781 22.580 20.214 1.00 23.53 N ATOM 2542 CA PHE C 463 8.726 22.543 19.101 1.00 25.78 C ATOM 2543 C PHE C 463 9.330 21.166 18.891 1.00 26.15 C ATOM 2544 O PHE C 463 9.116 20.259 19.690 1.00 22.61 O ATOM 2545 CB PHE C 463 9.871 23.544 19.334 1.00 25.16 C ATOM 2546 CG PHE C 463 9.401 24.955 19.555 1.00 25.81 C ATOM 2547 CD1 PHE C 463 9.080 25.403 20.834 1.00 25.56 C ATOM 2548 CD2 PHE C 463 9.218 25.813 18.479 1.00 21.79 C ATOM 2549 CE1 PHE C 463 8.581 26.681 21.037 1.00 21.95 C ATOM 2550 CE2 PHE C 463 8.719 27.095 18.671 1.00 23.55 C ATOM 2551 CZ PHE C 463 8.399 27.527 19.955 1.00 25.05 C ATOM 2552 N SER C 464 10.082 21.030 17.801 1.00 28.14 N ATOM 2553 CA SER C 464 10.765 19.791 17.481 1.00 32.33 C ATOM 2554 C SER C 464 12.166 20.179 17.031 1.00 32.53 C ATOM 2555 O SER C 464 12.357 21.206 16.388 1.00 34.11 O ATOM 2556 CB SER C 464 10.025 19.021 16.377 1.00 33.88 C ATOM 2557 OG SER C 464 10.234 19.586 15.099 1.00 37.24 O ATOM 2558 N ASN C 465 13.151 19.364 17.388 1.00 35.11 N ATOM 2559 CA ASN C 465 14.531 19.654 17.041 1.00 36.23 C ATOM 2560 C ASN C 465 14.801 19.559 15.541 1.00 38.36 C ATOM 2561 O ASN C 465 14.064 18.907 14.798 1.00 35.10 O ATOM 2562 CB ASN C 465 15.469 18.716 17.797 1.00 36.73 C ATOM 2563 CG ASN C 465 16.803 19.363 18.112 1.00 38.14 C ATOM 2564 OD1 ASN C 465 17.235 20.283 17.424 1.00 38.06 O ATOM 2565 ND2 ASN C 465 17.466 18.876 19.151 1.00 39.58 N ATOM 2566 N ILE C 466 15.868 20.225 15.111 1.00 41.35 N ATOM 2567 CA ILE C 466 16.273 20.254 13.711 1.00 45.74 C ATOM 2568 C ILE C 466 17.754 19.893 13.603 1.00 49.28 C ATOM 2569 O ILE C 466 18.561 20.290 14.449 1.00 49.27 O ATOM 2570 CB ILE C 466 16.052 21.655 13.114 1.00 45.87 C ATOM 2571 CG1 ILE C 466 14.573 22.030 13.223 1.00 46.31 C ATOM 2572 CG2 ILE C 466 16.517 21.688 11.668 1.00 46.14 C ATOM 2573 CD1 ILE C 466 14.243 23.442 12.767 1.00 46.65 C ATOM 2574 N SER C 467 18.108 19.154 12.555 1.00 51.80 N ATOM 2575 CA SER C 467 19.492 18.723 12.354 1.00 55.48 C ATOM 2576 C SER C 467 20.470 19.880 12.114 1.00 56.29 C ATOM 2577 O SER C 467 21.443 20.044 12.856 1.00 57.94 O ATOM 2578 CB SER C 467 19.561 17.732 11.188 1.00 56.27 C ATOM 2579 OG SER C 467 20.812 17.065 11.150 1.00 59.43 O ATOM 2580 N GLU C 468 20.217 20.676 11.078 1.00 56.47 N ATOM 2581 CA GLU C 468 21.085 21.810 10.766 1.00 56.36 C ATOM 2582 C GLU C 468 20.504 23.113 11.309 1.00 54.13 C ATOM 2583 O GLU C 468 19.343 23.432 11.055 1.00 55.55 O ATOM 2584 CB GLU C 468 21.257 21.951 9.253 1.00 58.77 C ATOM 2585 CG GLU C 468 21.898 20.764 8.562 1.00 63.85 C ATOM 2586 CD GLU C 468 21.942 20.944 7.053 1.00 66.73 C ATOM 2587 OE1 GLU C 468 20.860 20.938 6.422 1.00 67.58 O ATOM 2588 OE2 GLU C 468 23.055 21.102 6.500 1.00 67.99 O ATOM 2589 N GLY C 469 21.309 23.862 12.055 1.00 50.79 N ATOM 2590 CA GLY C 469 20.842 25.131 12.586 1.00 47.17 C ATOM 2591 C GLY C 469 20.508 25.143 14.065 1.00 45.11 C ATOM 2592 O GLY C 469 20.180 24.108 14.649 1.00 44.06 O ATOM 2593 N LEU C 470 20.589 26.325 14.670 1.00 41.53 N ATOM 2594 CA LEU C 470 20.282 26.483 16.085 1.00 39.49 C ATOM 2595 C LEU C 470 18.775 26.660 16.302 1.00 36.77 C ATOM 2596 O LEU C 470 18.283 27.779 16.444 1.00 38.40 O ATOM 2597 CB LEU C 470 21.028 27.688 16.653 1.00 40.94 C ATOM 2598 CG LEU C 470 20.817 27.897 18.152 1.00 44.12 C ATOM 2599 CD1 LEU C 470 21.261 26.630 18.898 1.00 45.02 C ATOM 2600 CD2 LEU C 470 21.587 29.121 18.629 1.00 41.73 C ATOM 2601 N SER C 471 18.063 25.539 16.343 1.00 31.88 N ATOM 2602 CA SER C 471 16.620 25.505 16.525 1.00 27.37 C ATOM 2603 C SER C 471 16.139 26.114 17.835 1.00 24.48 C ATOM 2604 O SER C 471 16.896 26.240 18.796 1.00 24.37 O ATOM 2605 CB SER C 471 16.130 24.055 16.462 1.00 27.40 C ATOM 2606 OG SER C 471 16.464 23.358 17.658 1.00 23.30 O ATOM 2607 N ASN C 472 14.864 26.480 17.874 1.00 22.24 N ATOM 2608 CA ASN C 472 14.288 27.036 19.095 1.00 22.64 C ATOM 2609 C ASN C 472 14.289 25.927 20.135 1.00 20.43 C ATOM 2610 O ASN C 472 14.493 26.166 21.323 1.00 19.53 O ATOM 2611 CB ASN C 472 12.852 27.518 18.854 1.00 20.78 C ATOM 2612 CG ASN C 472 12.795 28.860 18.139 1.00 21.60 C ATOM 2613 OD1 ASN C 472 11.747 29.262 17.624 1.00 25.78 O ATOM 2614 ND2 ASN C 472 13.912 29.563 18.118 1.00 21.36 N ATOM 2615 N TYR C 473 14.062 24.705 19.674 1.00 21.65 N ATOM 2616 CA TYR C 473 14.039 23.551 20.562 1.00 20.71 C ATOM 2617 C TYR C 473 15.352 23.414 21.344 1.00 19.56 C ATOM 2618 O TYR C 473 15.355 23.365 22.585 1.00 17.41 O ATOM 2619 CB TYR C 473 13.786 22.275 19.753 1.00 22.94 C ATOM 2620 CG TYR C 473 13.765 21.026 20.598 1.00 24.69 C ATOM 2621 CD1 TYR C 473 12.580 20.570 21.166 1.00 25.55 C ATOM 2622 CD2 TYR C 473 14.940 20.329 20.872 1.00 25.72 C ATOM 2623 CE1 TYR C 473 12.559 19.454 21.991 1.00 27.45 C ATOM 2624 CE2 TYR C 473 14.930 19.213 21.695 1.00 30.34 C ATOM 2625 CZ TYR C 473 13.735 18.784 22.253 1.00 28.31 C ATOM 2626 OH TYR C 473 13.722 17.700 23.101 1.00 34.15 O ATOM 2627 N SER C 474 16.475 23.365 20.636 1.00 20.25 N ATOM 2628 CA SER C 474 17.757 23.212 21.331 1.00 23.68 C ATOM 2629 C SER C 474 18.106 24.402 22.224 1.00 22.92 C ATOM 2630 O SER C 474 18.703 24.227 23.290 1.00 23.47 O ATOM 2631 CB SER C 474 18.894 22.932 20.336 1.00 23.74 C ATOM 2632 OG SER C 474 19.008 23.954 19.372 1.00 33.18 O ATOM 2633 N ILE C 475 17.732 25.610 21.810 1.00 22.40 N ATOM 2634 CA ILE C 475 18.004 26.785 22.638 1.00 20.76 C ATOM 2635 C ILE C 475 17.202 26.653 23.925 1.00 21.49 C ATOM 2636 O ILE C 475 17.721 26.876 25.025 1.00 19.81 O ATOM 2637 CB ILE C 475 17.582 28.102 21.956 1.00 21.73 C ATOM 2638 CG1 ILE C 475 18.446 28.365 20.727 1.00 19.99 C ATOM 2639 CG2 ILE C 475 17.707 29.265 22.940 1.00 19.73 C ATOM 2640 CD1 ILE C 475 18.116 29.694 20.032 1.00 24.22 C ATOM 2641 N ILE C 476 15.933 26.280 23.800 1.00 21.24 N ATOM 2642 CA ILE C 476 15.104 26.129 24.997 1.00 20.97 C ATOM 2643 C ILE C 476 15.642 24.986 25.853 1.00 20.70 C ATOM 2644 O ILE C 476 15.673 25.079 27.084 1.00 19.30 O ATOM 2645 CB ILE C 476 13.619 25.815 24.654 1.00 21.79 C ATOM 2646 CG1 ILE C 476 12.958 27.026 24.002 1.00 22.13 C ATOM 2647 CG2 ILE C 476 12.860 25.435 25.925 1.00 16.53 C ATOM 2648 CD1 ILE C 476 11.744 26.657 23.170 1.00 21.09 C ATOM 2649 N ASP C 477 16.061 23.907 25.200 1.00 23.82 N ATOM 2650 CA ASP C 477 16.578 22.740 25.918 1.00 25.99 C ATOM 2651 C ASP C 477 17.739 23.163 26.820 1.00 26.65 C ATOM 2652 O ASP C 477 17.831 22.725 27.966 1.00 27.58 O ATOM 2653 CB ASP C 477 17.027 21.670 24.925 1.00 30.12 C ATOM 2654 CG ASP C 477 17.187 20.295 25.568 1.00 36.38 C ATOM 2655 OD1 ASP C 477 17.789 19.407 24.919 1.00 39.97 O ATOM 2656 OD2 ASP C 477 16.707 20.094 26.708 1.00 36.57 O ATOM 2657 N LYS C 478 18.612 24.030 26.317 1.00 27.68 N ATOM 2658 CA LYS C 478 19.736 24.519 27.119 1.00 29.23 C ATOM 2659 C LYS C 478 19.227 25.353 28.300 1.00 29.75 C ATOM 2660 O LYS C 478 19.727 25.230 29.427 1.00 31.70 O ATOM 2661 CB LYS C 478 20.673 25.398 26.284 1.00 30.85 C ATOM 2662 CG LYS C 478 21.161 24.782 24.983 1.00 38.41 C ATOM 2663 CD LYS C 478 22.194 23.690 25.197 1.00 42.83 C ATOM 2664 CE LYS C 478 22.812 23.268 23.867 1.00 46.03 C ATOM 2665 NZ LYS C 478 23.965 22.340 24.062 1.00 50.46 N ATOM 2666 N LEU C 479 18.244 26.213 28.053 1.00 27.40 N ATOM 2667 CA LEU C 479 17.719 27.045 29.135 1.00 28.07 C ATOM 2668 C LEU C 479 17.145 26.193 30.258 1.00 24.73 C ATOM 2669 O LEU C 479 17.341 26.498 31.434 1.00 22.84 O ATOM 2670 CB LEU C 479 16.655 28.020 28.611 1.00 26.25 C ATOM 2671 CG LEU C 479 17.165 29.012 27.560 1.00 31.77 C ATOM 2672 CD1 LEU C 479 16.070 30.035 27.264 1.00 31.46 C ATOM 2673 CD2 LEU C 479 18.437 29.712 28.056 1.00 29.08 C ATOM 2674 N VAL C 480 16.449 25.121 29.889 1.00 26.01 N ATOM 2675 CA VAL C 480 15.858 24.200 30.861 1.00 26.10 C ATOM 2676 C VAL C 480 16.934 23.591 31.754 1.00 28.41 C ATOM 2677 O VAL C 480 16.794 23.536 32.981 1.00 30.02 O ATOM 2678 CB VAL C 480 15.101 23.033 30.150 1.00 27.48 C ATOM 2679 CG1 VAL C 480 14.709 21.944 31.174 1.00 22.70 C ATOM 2680 CG2 VAL C 480 13.847 23.573 29.438 1.00 22.45 C ATOM 2681 N ASN C 481 18.015 23.134 31.138 1.00 29.31 N ATOM 2682 CA ASN C 481 19.091 22.523 31.904 1.00 31.74 C ATOM 2683 C ASN C 481 19.737 23.501 32.855 1.00 32.23 C ATOM 2684 O ASN C 481 20.096 23.137 33.968 1.00 34.43 O ATOM 2685 CB ASN C 481 20.135 21.926 30.968 1.00 31.52 C ATOM 2686 CG ASN C 481 19.678 20.618 30.381 1.00 36.47 C ATOM 2687 OD1 ASN C 481 19.393 19.673 31.118 1.00 37.95 O ATOM 2688 ND2 ASN C 481 19.592 20.549 29.050 1.00 38.74 N ATOM 2689 N ILE C 482 19.890 24.745 32.424 1.00 31.94 N ATOM 2690 CA ILE C 482 20.473 25.739 33.296 1.00 32.92 C ATOM 2691 C ILE C 482 19.513 26.004 34.445 1.00 33.63 C ATOM 2692 O ILE C 482 19.916 26.019 35.612 1.00 33.56 O ATOM 2693 CB ILE C 482 20.737 27.064 32.550 1.00 35.61 C ATOM 2694 CG1 ILE C 482 21.821 26.853 31.489 1.00 36.13 C ATOM 2695 CG2 ILE C 482 21.172 28.145 33.544 1.00 37.84 C ATOM 2696 CD1 ILE C 482 22.014 28.027 30.560 1.00 35.81 C ATOM 2697 N VAL C 483 18.235 26.194 34.125 1.00 33.38 N ATOM 2698 CA VAL C 483 17.268 26.490 35.170 1.00 34.28 C ATOM 2699 C VAL C 483 17.063 25.317 36.115 1.00 34.62 C ATOM 2700 O VAL C 483 16.742 25.518 37.283 1.00 31.29 O ATOM 2701 CB VAL C 483 15.911 26.951 34.586 1.00 35.64 C ATOM 2702 CG1 VAL C 483 14.940 27.255 35.710 1.00 36.63 C ATOM 2703 CG2 VAL C 483 16.109 28.199 33.745 1.00 36.55 C ATOM 2704 N ASP C 484 17.240 24.096 35.616 1.00 36.84 N ATOM 2705 CA ASP C 484 17.106 22.922 36.473 1.00 39.62 C ATOM 2706 C ASP C 484 18.272 22.892 37.450 1.00 38.62 C ATOM 2707 O ASP C 484 18.115 22.499 38.603 1.00 39.47 O ATOM 2708 CB ASP C 484 17.099 21.629 35.658 1.00 42.89 C ATOM 2709 CG ASP C 484 15.742 21.319 35.072 1.00 47.18 C ATOM 2710 OD1 ASP C 484 14.742 21.900 35.549 1.00 50.05 O ATOM 2711 OD2 ASP C 484 15.673 20.483 34.143 1.00 52.07 O ATOM 2712 N ASP C 485 19.446 23.303 36.988 1.00 38.05 N ATOM 2713 CA ASP C 485 20.607 23.337 37.865 1.00 40.50 C ATOM 2714 C ASP C 485 20.321 24.271 39.035 1.00 41.55 C ATOM 2715 O ASP C 485 20.628 23.949 40.186 1.00 42.39 O ATOM 2716 CB ASP C 485 21.843 23.830 37.117 1.00 42.31 C ATOM 2717 CG ASP C 485 22.286 22.873 36.036 1.00 46.90 C ATOM 2718 OD1 ASP C 485 21.953 21.672 36.148 1.00 46.07 O ATOM 2719 OD2 ASP C 485 22.974 23.316 35.086 1.00 47.88 O ATOM 2720 N LEU C 486 19.735 25.427 38.730 1.00 41.28 N ATOM 2721 CA LEU C 486 19.388 26.415 39.746 1.00 42.01 C ATOM 2722 C LEU C 486 18.341 25.867 40.703 1.00 41.60 C ATOM 2723 O LEU C 486 18.346 26.190 41.888 1.00 40.42 O ATOM 2724 CB LEU C 486 18.857 27.691 39.091 1.00 41.85 C ATOM 2725 CG LEU C 486 19.868 28.389 38.185 1.00 43.42 C ATOM 2726 CD1 LEU C 486 19.212 29.559 37.452 1.00 43.01 C ATOM 2727 CD2 LEU C 486 21.042 28.856 39.034 1.00 42.44 C ATOM 2728 N VAL C 487 17.440 25.039 40.190 1.00 42.89 N ATOM 2729 CA VAL C 487 16.413 24.465 41.045 1.00 45.33 C ATOM 2730 C VAL C 487 17.095 23.559 42.063 1.00 48.13 C ATOM 2731 O VAL C 487 16.747 23.581 43.248 1.00 46.85 O ATOM 2732 CB VAL C 487 15.377 23.647 40.241 1.00 43.87 C ATOM 2733 CG1 VAL C 487 14.393 22.976 41.185 1.00 40.38 C ATOM 2734 CG2 VAL C 487 14.637 24.553 39.285 1.00 43.12 C ATOM 2735 N GLU C 488 18.074 22.779 41.605 1.00 50.31 N ATOM 2736 CA GLU C 488 18.808 21.883 42.498 1.00 54.58 C ATOM 2737 C GLU C 488 19.626 22.667 43.527 1.00 56.13 C ATOM 2738 O GLU C 488 19.730 22.262 44.678 1.00 56.58 O ATOM 2739 CB GLU C 488 19.755 20.965 41.712 1.00 56.04 C ATOM 2740 CG GLU C 488 19.088 20.057 40.682 1.00 59.98 C ATOM 2741 CD GLU C 488 19.720 18.669 40.620 1.00 62.60 C ATOM 2742 OE1 GLU C 488 19.446 17.861 41.533 1.00 61.75 O ATOM 2743 OE2 GLU C 488 20.493 18.385 39.671 1.00 63.45 O ATOM 2744 N CYS C 489 20.204 23.787 43.107 1.00 59.19 N ATOM 2745 CA CYS C 489 21.023 24.614 43.991 1.00 62.50 C ATOM 2746 C CYS C 489 20.217 25.331 45.065 1.00 64.25 C ATOM 2747 O CYS C 489 20.748 25.686 46.117 1.00 62.95 O ATOM 2748 CB CYS C 489 21.784 25.651 43.175 1.00 64.14 C ATOM 2749 SG CYS C 489 22.738 24.935 41.835 1.00 70.99 S ATOM 2750 N VAL C 490 18.938 25.557 44.788 1.00 66.42 N ATOM 2751 CA VAL C 490 18.065 26.231 45.736 1.00 68.53 C ATOM 2752 C VAL C 490 17.555 25.246 46.785 1.00 70.15 C ATOM 2753 O VAL C 490 17.107 25.650 47.858 1.00 70.55 O ATOM 2754 CB VAL C 490 16.864 26.885 45.012 1.00 69.36 C ATOM 2755 CG1 VAL C 490 15.909 27.505 46.023 1.00 69.33 C ATOM 2756 CG2 VAL C 490 17.365 27.948 44.043 1.00 68.45 C ATOM 2757 N LYS C 491 17.638 23.955 46.473 1.00 71.74 N ATOM 2758 CA LYS C 491 17.183 22.911 47.387 1.00 73.62 C ATOM 2759 C LYS C 491 18.264 22.538 48.396 1.00 75.55 C ATOM 2760 O LYS C 491 18.383 21.376 48.785 1.00 75.66 O ATOM 2761 CB LYS C 491 16.755 21.681 46.603 1.00 72.92 C ATOM 2762 N GLU C 492 19.042 23.535 48.814 1.00 78.00 N ATOM 2763 CA GLU C 492 20.121 23.351 49.782 1.00 79.84 C ATOM 2764 C GLU C 492 21.012 24.589 49.802 1.00 81.20 C ATOM 2765 O GLU C 492 22.126 24.564 49.283 1.00 81.52 O ATOM 2766 CB GLU C 492 20.951 22.119 49.425 1.00 80.18 C ATOM 2767 N ASN C 493 20.518 25.669 50.401 1.00 83.14 N ATOM 2768 CA ASN C 493 21.277 26.916 50.481 1.00 84.85 C ATOM 2769 C ASN C 493 21.948 27.097 51.845 1.00 86.58 C ATOM 2770 O ASN C 493 23.088 26.670 52.050 1.00 86.98 O ATOM 2771 CB ASN C 493 20.362 28.100 50.190 1.00 84.61 C ATOM 2772 N SER C 494 21.238 27.736 52.772 1.00 88.38 N ATOM 2773 CA SER C 494 21.759 27.980 54.116 1.00 89.76 C ATOM 2774 C SER C 494 20.629 27.992 55.145 1.00 90.86 C ATOM 2775 O SER C 494 20.509 27.076 55.961 1.00 91.08 O ATOM 2776 CB SER C 494 22.509 29.309 54.150 1.00 89.25 C ATOM 2777 N SER C 495 19.808 29.037 55.095 1.00 91.91 N ATOM 2778 CA SER C 495 18.678 29.195 56.006 1.00 92.32 C ATOM 2779 C SER C 495 17.985 30.529 55.729 1.00 92.84 C ATOM 2780 O SER C 495 16.815 30.720 56.075 1.00 92.80 O ATOM 2781 CB SER C 495 19.159 29.141 57.455 1.00 91.90 C ATOM 2782 N LYS C 496 18.718 31.445 55.102 1.00 92.97 N ATOM 2783 CA LYS C 496 18.194 32.766 54.770 1.00 92.97 C ATOM 2784 C LYS C 496 17.581 32.773 53.372 1.00 92.72 C ATOM 2785 O LYS C 496 18.022 33.512 52.488 1.00 92.28 O ATOM 2786 CB LYS C 496 19.309 33.808 54.859 1.00 93.19 C ATOM 2787 N ASP C 497 16.563 31.939 53.183 1.00 92.13 N ATOM 2788 CA ASP C 497 15.865 31.833 51.908 1.00 92.02 C ATOM 2789 C ASP C 497 14.435 31.359 52.156 1.00 92.20 C ATOM 2790 O ASP C 497 14.203 30.458 52.964 1.00 92.35 O ATOM 2791 CB ASP C 497 16.593 30.858 50.989 1.00 91.57 C ATOM 2792 N LEU C 498 13.478 31.970 51.464 1.00 92.05 N ATOM 2793 CA LEU C 498 12.075 31.605 51.622 1.00 91.73 C ATOM 2794 C LEU C 498 11.645 30.576 50.580 1.00 91.81 C ATOM 2795 O LEU C 498 11.058 30.924 49.555 1.00 92.52 O ATOM 2796 CB LEU C 498 11.198 32.850 51.521 1.00 91.53 C ATOM 2797 N LYS C 499 11.941 29.308 50.845 1.00 91.61 N ATOM 2798 CA LYS C 499 11.579 28.233 49.930 1.00 91.43 C ATOM 2799 C LYS C 499 10.117 27.847 50.133 1.00 91.66 C ATOM 2800 O LYS C 499 9.603 26.949 49.466 1.00 91.71 O ATOM 2801 CB LYS C 499 12.478 27.025 50.159 1.00 90.82 C ATOM 2802 N LYS C 500 9.455 28.538 51.056 1.00 92.00 N ATOM 2803 CA LYS C 500 8.050 28.282 51.362 1.00 92.42 C ATOM 2804 C LYS C 500 7.141 28.565 50.165 1.00 92.65 C ATOM 2805 O LYS C 500 7.499 28.274 49.020 1.00 93.28 O ATOM 2806 CB LYS C 500 7.618 29.126 52.559 1.00 92.24 C ATOM 2807 N SER C 501 5.968 29.133 50.439 1.00 92.35 N ATOM 2808 CA SER C 501 4.985 29.453 49.404 1.00 91.78 C ATOM 2809 C SER C 501 4.381 28.168 48.836 1.00 91.55 C ATOM 2810 O SER C 501 3.246 28.167 48.348 1.00 90.99 O ATOM 2811 CB SER C 501 5.637 30.273 48.284 1.00 91.58 C ATOM 2812 N PHE C 502 5.149 27.081 48.917 1.00 91.35 N ATOM 2813 CA PHE C 502 4.736 25.767 48.425 1.00 90.43 C ATOM 2814 C PHE C 502 4.320 25.841 46.961 1.00 89.44 C ATOM 2815 O PHE C 502 5.155 25.771 46.058 1.00 89.03 O ATOM 2816 CB PHE C 502 3.584 25.227 49.274 1.00 90.98 C ATOM 2817 N LYS C 503 3.019 25.976 46.740 1.00 88.39 N ATOM 2818 CA LYS C 503 2.464 26.081 45.400 1.00 87.51 C ATOM 2819 C LYS C 503 1.156 26.860 45.503 1.00 86.08 C ATOM 2820 O LYS C 503 0.238 26.451 46.220 1.00 86.05 O ATOM 2821 CB LYS C 503 2.202 24.691 44.814 1.00 88.05 C ATOM 2822 CG LYS C 503 1.839 24.711 43.336 1.00 88.57 C ATOM 2823 CD LYS C 503 1.419 23.338 42.832 1.00 88.37 C ATOM 2824 CE LYS C 503 0.106 22.899 43.452 1.00 87.87 C ATOM 2825 NZ LYS C 503 −0.417 21.679 42.790 1.00 87.78 N ATOM 2826 N SER C 504 1.083 27.987 44.800 1.00 83.62 N ATOM 2827 CA SER C 504 −0.109 28.826 44.821 1.00 80.69 C ATOM 2828 C SER C 504 −0.033 30.080 43.944 1.00 77.49 C ATOM 2829 O SER C 504 −0.748 31.050 44.190 1.00 78.09 O ATOM 2830 CB SER C 504 −0.423 29.238 46.266 1.00 82.35 C ATOM 2831 OG SER C 504 0.708 29.822 46.895 1.00 83.35 O ATOM 2832 N PRO C 505 0.830 30.087 42.914 1.00 73.98 N ATOM 2833 CA PRO C 505 0.891 31.293 42.082 1.00 70.42 C ATOM 2834 C PRO C 505 −0.127 31.246 40.945 1.00 66.52 C ATOM 2835 O PRO C 505 −0.414 30.176 40.411 1.00 66.27 O ATOM 2836 CB PRO C 505 2.326 31.277 41.581 1.00 70.47 C ATOM 2837 CG PRO C 505 2.546 29.816 41.349 1.00 73.11 C ATOM 2838 CD PRO C 505 1.926 29.160 42.571 1.00 73.18 C ATOM 2839 N GLU C 506 −0.672 32.402 40.579 1.00 62.89 N ATOM 2840 CA GLU C 506 −1.659 32.459 39.504 1.00 60.06 C ATOM 2841 C GLU C 506 −0.999 32.543 38.125 1.00 56.43 C ATOM 2842 O GLU C 506 −0.067 33.321 37.909 1.00 53.61 O ATOM 2843 CB GLU C 506 −2.597 33.657 39.686 1.00 60.85 C ATOM 2844 CG GLU C 506 −2.055 34.963 39.137 1.00 63.66 C ATOM 2845 CD GLU C 506 −3.083 36.074 39.155 1.00 66.22 C ATOM 2846 OE1 GLU C 506 −4.181 35.889 38.591 1.00 66.44 O ATOM 2847 OE2 GLU C 506 −2.791 37.141 39.732 1.00 69.61 O ATOM 2848 N PRO C 507 −1.483 31.730 37.174 1.00 53.50 N ATOM 2849 CA PRO C 507 −0.959 31.696 35.808 1.00 50.59 C ATOM 2850 C PRO C 507 −1.172 33.025 35.096 1.00 47.75 C ATOM 2851 O PRO C 507 −2.249 33.617 35.170 1.00 47.48 O ATOM 2852 CB PRO C 507 −1.762 30.569 35.155 1.00 51.01 C ATOM 2853 CG PRO C 507 −2.109 29.678 36.309 1.00 52.55 C ATOM 2854 CD PRO C 507 −2.491 30.672 37.371 1.00 52.89 C ATOM 2855 N ARG C 508 −0.142 33.497 34.408 1.00 43.60 N ATOM 2856 CA ARG C 508 −0.245 34.750 33.675 1.00 39.58 C ATOM 2857 C ARG C 508 0.357 34.575 32.294 1.00 35.30 C ATOM 2858 O ARG C 508 1.231 33.738 32.102 1.00 31.03 O ATOM 2859 CB ARG C 508 0.471 35.870 34.427 1.00 40.31 C ATOM 2860 CG ARG C 508 −0.213 36.255 35.716 1.00 44.11 C ATOM 2861 CD ARG C 508 0.431 37.486 36.326 1.00 48.76 C ATOM 2862 NE ARG C 508 0.731 38.514 35.328 1.00 47.99 N ATOM 2863 CZ ARG C 508 1.181 39.729 35.631 1.00 50.50 C ATOM 2864 NH1 ARG C 508 1.371 40.059 36.904 1.00 50.11 N ATOM 2865 NH2 ARG C 508 1.457 40.609 34.670 1.00 49.02 N ATOM 2866 N LEU C 509 −0.126 35.362 31.339 1.00 32.29 N ATOM 2867 CA LEU C 509 0.359 35.294 29.965 1.00 31.11 C ATOM 2868 C LEU C 509 1.333 36.427 29.663 1.00 28.63 C ATOM 2869 O LEU C 509 1.058 37.603 29.941 1.00 24.90 O ATOM 2870 CB LEU C 509 −0.810 35.359 28.978 1.00 31.46 C ATOM 2871 CG LEU C 509 −1.865 34.252 29.051 1.00 34.91 C ATOM 2872 CD1 LEU C 509 −2.915 34.504 27.975 1.00 34.69 C ATOM 2873 CD2 LEU C 509 −1.217 32.878 28.873 1.00 33.71 C ATOM 2874 N PHE C 510 2.471 36.058 29.085 1.00 24.62 N ATOM 2875 CA PHE C 510 3.498 37.025 28.742 1.00 22.42 C ATOM 2876 C PHE C 510 3.965 36.840 27.304 1.00 22.59 C ATOM 2877 O PHE C 510 3.922 35.730 26.756 1.00 21.95 C ATOM 2878 CB PHE C 510 4.716 36.862 29.659 1.00 20.32 C ATOM 2879 CG PHE C 510 4.406 36.967 31.114 1.00 19.85 C ATOM 2880 CD1 PHE C 510 3.987 35.850 31.834 1.00 21.32 C ATOM 2881 CD2 PHE C 510 4.546 38.188 31.782 1.00 24.49 C ATOM 2882 CE1 PHE C 510 3.714 35.940 33.195 1.00 19.00 C ATOM 2883 CE2 PHE C 510 4.273 38.294 33.153 1.00 23.56 C ATOM 2884 CZ PHE C 510 3.857 37.162 33.859 1.00 24.09 C ATOM 2885 N THR C 511 4.408 37.933 26.691 1.00 21.70 N ATOM 2886 CA THR C 511 4.946 37.873 25.338 1.00 20.39 C ATOM 2887 C THR C 511 6.326 37.241 25.515 1.00 18.81 C ATOM 2888 O THR C 511 6.872 37.228 26.620 1.00 18.27 O ATOM 2889 CB THR C 511 5.156 39.274 24.770 1.00 21.47 C ATOM 2890 OG1 THR C 511 6.103 39.966 25.597 1.00 25.55 O ATOM 2891 CG2 THR C 511 3.841 40.058 24.746 1.00 23.54 C ATOM 2892 N PRO C 512 6.912 36.704 24.440 1.00 20.33 N ATOM 2893 CA PRO C 512 8.240 36.102 24.617 1.00 21.52 C ATOM 2894 C PRO C 512 9.239 37.093 25.237 1.00 22.84 C ATOM 2895 O PRO C 512 10.008 36.750 26.134 1.00 23.45 O ATOM 2896 CB PRO C 512 8.607 35.689 23.198 1.00 20.44 C ATOM 2897 CG PRO C 512 7.223 35.291 22.624 1.00 18.41 C ATOM 2898 CD PRO C 512 6.364 36.422 23.098 1.00 19.58 C ATOM 2899 N GLU C 513 9.199 38.330 24.770 1.00 24.25 N ATOM 2900 CA GLU C 513 10.091 39.378 25.261 1.00 26.40 C ATOM 2901 C GLU C 513 9.920 39.624 26.762 1.00 26.10 C ATOM 2902 O GLU C 513 10.906 39.771 27.500 1.00 25.11 C ATOM 2903 CB GLU C 513 9.822 40.669 24.489 1.00 29.08 C ATOM 2904 CG GLU C 513 10.850 41.753 24.712 1.00 35.84 C ATOM 2905 CD GLU C 513 10.469 43.040 24.011 1.00 41.11 C ATOM 2906 OE1 GLU C 513 10.021 42.961 22.841 1.00 40.55 C ATOM 2907 OE2 GLU C 513 10.623 44.121 24.626 1.00 43.50 O ATOM 2908 N GLU C 514 8.664 39.682 27.202 1.00 26.40 N ATOM 2909 CA GLU C 514 8.324 39.886 28.606 1.00 25.38 C ATOM 2910 C GLU C 514 8.777 38.681 29.433 1.00 23.79 C ATOM 2911 O GLU C 514 9.386 38.831 30.501 1.00 23.81 O ATOM 2912 CB GLU C 514 6.807 40.069 28.755 1.00 29.33 C ATOM 2913 CG GLU C 514 6.315 41.527 28.727 1.00 33.14 C ATOM 2914 CD GLU C 514 4.861 41.672 28.261 1.00 33.03 C ATOM 2915 OE1 GLU C 514 4.007 40.829 28.611 1.00 31.80 O ATOM 2916 OE2 GLU C 514 4.568 42.649 27.542 1.00 38.85 O ATOM 2917 N PHE C 515 8.479 37.484 28.941 1.00 21.59 N ATOM 2918 CA PHE C 515 8.859 36.270 29.660 1.00 19.64 C ATOM 2919 C PHE C 515 10.360 36.198 29.901 1.00 17.78 C ATOM 2920 O PHE C 515 10.808 35.987 31.026 1.00 17.87 O ATOM 2921 CB PHE C 515 8.415 35.018 28.890 1.00 18.51 C ATOM 2922 CG PHE C 515 8.822 33.730 29.550 1.00 20.90 C ATOM 2923 CD1 PHE C 515 8.068 33.197 30.596 1.00 19.79 C ATOM 2924 CD2 PHE C 515 9.972 33.053 29.141 1.00 21.28 C ATOM 2925 CE1 PHE C 515 8.445 32.010 31.226 1.00 16.33 C ATOM 2926 CE2 PHE C 515 10.361 31.859 29.766 1.00 21.22 C ATOM 2927 CZ PHE C 515 9.597 31.339 30.807 1.00 20.73 C ATOM 2928 N PHE C 516 11.151 36.381 28.852 1.00 18.00 N ATOM 2929 CA PHE C 516 12.593 36.296 29.035 1.00 20.74 C ATOM 2930 C PHE C 516 13.251 37.427 29.813 1.00 22.35 C ATOM 2931 O PHE C 516 14.369 37.273 30.288 1.00 23.89 O ATOM 2932 CB PHE C 516 13.272 36.053 27.692 1.00 19.59 C ATOM 2933 CG PHE C 516 13.052 34.667 27.182 1.00 21.15 C ATOM 2934 CD1 PHE C 516 12.038 34.398 26.259 1.00 19.55 C ATOM 2935 CD2 PHE C 516 13.795 33.603 27.702 1.00 21.51 C ATOM 2936 CE1 PHE C 516 11.766 33.090 25.862 1.00 22.18 C ATOM 2937 CE2 PHE C 516 13.533 32.287 27.313 1.00 21.46 C ATOM 2938 CZ PHE C 516 12.516 32.027 26.390 1.00 18.99 C ATOM 2939 N ARG C 517 12.548 38.545 29.972 1.00 25.99 N ATOM 2940 CA ARG C 517 13.058 39.674 30.756 1.00 27.38 C ATOM 2941 C ARG C 517 12.968 39.224 32.218 1.00 27.00 C ATOM 2942 O ARG C 517 13.789 39.594 33.061 1.00 27.39 O ATOM 2943 CB ARG C 517 12.187 40.924 30.547 1.00 25.75 C ATOM 2944 CG ARG C 517 12.627 42.145 31.360 1.00 30.62 C ATOM 2945 CD ARG C 517 11.810 43.412 31.008 1.00 32.07 C ATOM 2946 NE ARG C 517 11.927 43.761 29.592 1.00 37.76 N ATOM 2947 CZ ARG C 517 10.896 43.869 28.754 1.00 40.99 C ATOM 2948 NH1 ARG C 517 9.658 43.663 29.188 1.00 41.55 N ATOM 2949 NH2 ARG C 517 11.100 44.161 27.473 1.00 41.63 N ATOM 2950 N ILE C 518 11.948 38.424 32.509 1.00 25.97 N ATOM 2951 CA ILE C 518 11.752 37.897 33.850 1.00 22.48 C ATOM 2952 C ILE C 518 12.750 36.756 34.045 1.00 22.93 C ATOM 2953 O ILE C 518 13.337 36.616 35.111 1.00 24.47 O ATOM 2954 CB ILE C 518 10.314 37.394 34.020 1.00 22.76 C ATOM 2955 CG1 ILE C 518 9.360 38.592 34.014 1.00 21.65 C ATOM 2956 CG2 ILE C 518 10.178 36.567 35.298 1.00 17.95 C ATOM 2957 CD1 ILE C 518 7.884 38.197 33.877 1.00 23.44 C ATOM 2958 N PHE C 519 12.938 35.951 33.004 1.00 22.45 N ATOM 2959 CA PHE C 519 13.895 34.848 33.032 1.00 23.48 C ATOM 2960 C PHE C 519 15.262 35.437 33.393 1.00 26.08 C ATOM 2961 O PHE C 519 15.886 35.047 34.388 1.00 26.78 O ATOM 2962 CB PHE C 519 13.969 34.194 31.647 1.00 22.04 C ATOM 2963 CG PHE C 519 15.114 33.228 31.479 1.00 23.71 C ATOM 2964 CD1 PHE C 519 14.985 31.889 31.864 1.00 23.22 C ATOM 2965 CD2 PHE C 519 16.326 33.657 30.938 1.00 21.19 C ATOM 2966 CE1 PHE C 519 16.049 30.998 31.713 1.00 21.76 C ATOM 2967 CE2 PHE C 519 17.397 32.779 30.783 1.00 21.63 C ATOM 2968 CZ PHE C 519 17.261 31.443 31.171 1.00 23.53 C ATOM 2969 N ASN C 520 15.712 36.388 32.581 1.00 26.37 N ATOM 2970 CA ASN C 520 17.002 37.043 32.784 1.00 28.23 C ATOM 2971 C ASN C 520 17.169 37.639 34.165 1.00 29.17 C ATOM 2972 O ASN C 520 18.227 37.507 34.788 1.00 30.03 O ATOM 2973 CB ASN C 520 17.195 38.183 31.786 1.00 26.87 C ATOM 2974 CG ASN C 520 17.631 37.711 30.442 1.00 26.27 C ATOM 2975 OD1 ASN C 520 17.659 38.489 29.495 1.00 32.70 O ATOM 2976 ND2 ASN C 520 17.975 36.435 30.335 1.00 26.28 N ATOM 2977 N ARG C 521 16.141 38.338 34.623 1.00 29.19 N ATOM 2978 CA ARG C 521 16.209 38.973 35.926 1.00 32.82 C ATOM 2979 C ARG C 521 16.368 37.912 37.014 1.00 33.74 C ATOM 2980 O ARG C 521 17.122 38.108 37.974 1.00 33.01 O ATOM 2981 CB ARG C 521 14.958 39.820 36.161 1.00 33.12 C ATOM 2982 CG ARG C 521 15.070 40.788 37.325 1.00 39.00 C ATOM 2983 CD ARG C 521 13.914 41.782 37.299 1.00 45.11 C ATOM 2984 NE ARG C 521 13.822 42.459 36.003 1.00 51.59 N ATOM 2985 CZ ARG C 521 14.702 43.352 35.547 1.00 53.90 C ATOM 2986 NH1 ARG C 521 15.755 43.697 36.285 1.00 53.08 N ATOM 2987 NH2 ARG C 521 14.535 43.892 34.341 1.00 52.06 N ATOM 2988 N SER C 522 15.681 36.781 36.848 1.00 33.44 N ATOM 2989 CA SER C 522 15.759 35.702 37.825 1.00 34.99 C ATOM 2990 C SER C 522 17.150 35.074 37.814 1.00 38.06 C ATOM 2991 O SER C 522 17.710 34.800 38.872 1.00 36.91 O ATOM 2992 CB SER C 522 14.694 34.633 37.539 1.00 33.27 C ATOM 2993 OG SER C 522 13.387 35.186 37.572 1.00 28.25 O ATOM 2994 N ILE C 523 17.706 34.849 36.623 1.00 41.24 N ATOM 2995 CA ILE C 523 19.042 34.265 36.513 1.00 44.88 C ATOM 2996 C ILE C 523 20.053 35.232 37.132 1.00 47.92 C ATOM 2997 O ILE C 523 20.921 34.824 37.905 1.00 46.65 O ATOM 2998 CB ILE C 523 19.420 33.959 35.024 1.00 44.62 C ATOM 2999 CG1 ILE C 523 19.259 32.462 34.740 1.00 43.86 C ATOM 3000 CG2 ILE C 523 20.874 34.354 34.735 1.00 43.36 C ATOM 3001 CD1 ILE C 523 17.872 31.937 34.937 1.00 43.79 C ATOM 3002 N ASP C 524 19.927 36.512 36.797 1.00 51.02 N ATOM 3003 CA ASP C 524 20.815 37.536 37.336 1.00 56.14 C ATOM 3004 C ASP C 524 20.646 37.669 38.847 1.00 58.19 C ATOM 3005 O ASP C 524 21.623 37.653 39.595 1.00 58.67 O ATOM 3006 CB ASP C 524 20.532 38.889 36.675 1.00 57.90 C ATOM 3007 CG ASP C 524 21.483 39.191 35.524 1.00 61.27 C ATOM 3008 OD1 ASP C 524 21.759 38.275 34.717 1.00 61.38 O ATOM 3009 OD2 ASP C 524 21.945 40.351 35.422 1.00 62.25 O ATOM 3010 N ALA C 525 19.398 37.800 39.287 1.00 61.09 N ATOM 3011 CA ALA C 525 19.091 37.949 40.705 1.00 63.58 C ATOM 3012 C ALA C 525 19.268 36.637 41.449 1.00 65.20 C ATOM 3013 O ALA C 525 18.631 36.402 42.475 1.00 65.19 O ATOM 3014 CB ALA C 525 17.667 38.458 40.880 1.00 64.99 C ATOM 3015 N PHE C 526 20.125 35.777 40.915 1.00 67.33 N ATOM 3016 CA PHE C 526 20.404 34.492 41.535 1.00 69.35 C ATOM 3017 C PHE C 526 21.797 34.596 42.141 1.00 70.48 C ATOM 3018 O PHE C 526 22.145 33.875 43.076 1.00 71.00 O ATOM 3019 CB PHE C 526 20.348 33.377 40.490 1.00 69.78 C ATOM 3020 CG PHE C 526 20.536 32.011 41.062 1.00 70.50 C ATOM 3021 CD1 PHE C 526 21.810 31.529 41.341 1.00 70.53 C ATOM 3022 CD2 PHE C 526 19.436 31.218 41.367 1.00 71.41 C ATOM 3023 CE1 PHE C 526 21.987 30.276 41.920 1.00 70.93 C ATOM 3024 CE2 PHE C 526 19.602 29.962 41.946 1.00 71.39 C ATOM 3025 CZ PHE C 526 20.881 29.491 42.223 1.00 71.33 C ATOM 3026 N LYS C 527 22.577 35.527 41.603 1.00 71.19 N ATOM 3027 CA LYS C 527 23.938 35.784 42.056 1.00 71.55 C ATOM 3028 C LYS C 527 24.080 37.277 42.371 1.00 70.63 C ATOM 3029 O LYS C 527 23.788 37.731 43.481 1.00 70.51 O ATOM 3030 CB LYS C 527 24.923 35.378 40.955 1.00 72.89 C ATOM 3031 CG LYS C 527 24.520 35.863 39.557 1.00 74.66 C ATOM 3032 CD LYS C 527 25.500 35.400 38.482 1.00 75.46 C ATOM 3033 CE LYS C 527 25.039 35.801 37.080 1.00 75.93 C ATOM 3034 NZ LYS C 527 24.995 37.279 36.867 1.00 75.87 N ATOM 3035 N ASP C 528 24.539 38.015 41.366 1.00 69.13 N ATOM 3036 CA ASP C 528 24.734 39.461 41.396 1.00 68.02 C ATOM 3037 C ASP C 528 24.981 40.243 42.687 1.00 66.87 C ATOM 3038 O ASP C 528 26.018 40.086 43.333 1.00 66.97 O ATOM 3039 CB ASP C 528 23.588 40.129 40.631 1.00 68.86 C ATOM 3040 CG ASP C 528 23.707 39.940 39.135 1.00 70.61 C ATOM 3041 OD1 ASP C 528 23.897 38.787 38.697 1.00 73.33 O ATOM 3042 OD2 ASP C 528 23.611 40.941 38.394 1.00 72.34 O ATOM 3043 N PHE C 529 24.018 41.092 43.044 1.00 65.50 N ATOM 3044 CA PHE C 529 24.132 41.995 44.197 1.00 62.92 C ATOM 3045 C PHE C 529 22.753 42.435 44.704 1.00 62.89 C ATOM 3046 O PHE C 529 22.271 41.972 45.744 1.00 60.70 O ATOM 3047 CB PHE C 529 24.910 43.223 43.722 1.00 59.24 C ATOM 3048 CG PHE C 529 24.861 43.402 42.223 1.00 54.32 C ATOM 3049 CD1 PHE C 529 23.632 43.532 41.561 1.00 53.79 C ATOM 3050 CD2 PHE C 529 26.026 43.334 41.457 1.00 52.93 C ATOM 3051 CE1 PHE C 529 23.562 43.584 40.155 1.00 51.16 C ATOM 3052 CE2 PHE C 529 25.973 43.385 40.048 1.00 51.37 C ATOM 3053 CZ PHE C 529 24.738 43.508 39.397 1.00 50.72 C ATOM 3054 N VAL C 530 22.164 43.362 43.944 1.00 62.87 N ATOM 3055 CA VAL C 530 20.843 43.962 44.159 1.00 62.88 C ATOM 3056 C VAL C 530 20.321 44.182 45.584 1.00 62.22 C ATOM 3057 O VAL C 530 20.044 43.233 46.322 1.00 62.00 O ATOM 3058 CB VAL C 530 19.749 43.182 43.368 1.00 62.92 C ATOM 3059 CG1 VAL C 530 18.449 43.993 43.332 1.00 62.70 C ATOM 3060 CG2 VAL C 530 20.233 42.889 41.953 1.00 63.00 C ATOM 3061 N VAL C 531 20.175 45.458 45.937 1.00 61.98 N ATOM 3062 CA VAL C 531 19.655 45.895 47.235 1.00 62.79 C ATOM 3063 C VAL C 531 20.097 45.061 48.452 1.00 63.46 C ATOM 3064 O VAL C 531 21.066 44.295 48.387 1.00 62.89 O ATOM 3065 CB VAL C 531 18.090 45.964 47.182 1.00 62.86 C ATOM 3066 CG1 VAL C 531 17.532 46.734 48.382 1.00 61.05 C ATOM 3067 CG2 VAL C 531 17.648 46.632 45.878 1.00 60.79 C ATOM 3068 N ALA C 532 19.377 45.239 49.561 1.00 64.26 N ATOM 3069 CA ALA C 532 19.643 44.550 50.822 1.00 64.32 C ATOM 3070 C ALA C 532 19.598 43.036 50.673 1.00 64.57 C ATOM 3071 O ALA C 532 18.581 42.404 50.966 1.00 64.60 O ATOM 3072 CB ALA C 532 18.634 44.998 51.876 1.00 63.34 C ATOM 3073 N SER C 533 20.714 42.464 50.227 1.00 65.18 N ATOM 3074 CA SER C 533 20.824 41.024 50.029 1.00 65.29 C ATOM 3075 C SER C 533 20.772 40.247 51.344 1.00 65.38 C ATOM 3076 O SER C 533 21.684 40.342 52.171 1.00 65.59 O ATOM 3077 CB SER C 533 22.129 40.690 49.296 1.00 64.84 C ATOM 3078 OG SER C 533 23.259 41.063 50.069 1.00 65.94 O ATOM 3079 N GLU C 534 19.696 39.484 51.527 1.00 65.95 N ATOM 3080 CA GLU C 534 19.506 38.661 52.718 1.00 65.76 C ATOM 3081 C GLU C 534 19.243 39.481 53.975 1.00 66.75 C ATOM 3082 O GLU C 534 19.342 38.965 55.089 1.00 67.37 O ATOM 3083 CB GLU C 534 20.734 37.782 52.930 1.00 65.02 C ATOM 3084 CG GLU C 534 21.167 37.039 51.676 1.00 64.99 C ATOM 3085 CD GLU C 534 22.532 36.403 51.828 1.00 64.29 C ATOM 3086 OE1 GLU C 534 22.681 35.521 52.700 1.00 65.53 O ATOM 3087 OE2 GLU C 534 23.454 36.791 51.080 1.00 64.02 O ATOM 3088 N THR C 535 18.908 40.757 53.803 1.00 67.44 N ATOM 3089 CA THR C 535 18.637 41.614 54.950 1.00 68.00 C ATOM 3090 C THR C 535 17.165 41.545 55.332 1.00 68.22 C ATOM 3091 O THR C 535 16.756 40.678 56.104 1.00 68.54 O ATOM 3092 CB THR C 535 19.008 43.088 54.666 1.00 67.35 C ATOM 3093 OG1 THR C 535 20.403 43.179 54.347 1.00 67.95 O ATOM 3094 CG2 THR C 535 18.725 43.952 55.891 1.00 67.69 C ATOM 3095 N SER C 536 16.372 42.458 54.786 1.00 69.72 N ATOM 3096 CA SER C 536 14.946 42.495 55.083 1.00 71.58 C ATOM 3097 C SER C 536 14.277 41.143 54.839 1.00 72.98 C ATOM 3098 O SER C 536 14.316 40.601 53.731 1.00 72.00 O ATOM 3099 CB SER C 536 14.255 43.588 54.254 1.00 70.94 C ATOM 3100 OG SER C 536 14.513 43.434 52.870 1.00 71.43 O ATOM 3101 N ASP C 537 13.673 40.605 55.896 1.00 75.05 N ATOM 3102 CA ASP C 537 12.979 39.324 55.839 1.00 76.57 C ATOM 3103 C ASP C 537 11.798 39.383 54.873 1.00 76.67 C ATOM 3104 O ASP C 537 11.556 40.407 54.228 1.00 76.41 O ATOM 3105 CB ASP C 537 12.486 38.949 57.236 1.00 78.26 C ATOM 3106 CG ASP C 537 11.586 40.013 57.839 1.00 79.16 C ATOM 3107 OD1 ASP C 537 10.455 40.193 57.339 1.00 81.11 O ATOM 3108 OD2 ASP C 537 12.014 40.676 58.809 1.00 79.18 O ATOM 3109 N CYS C 538 11.055 38.286 54.784 1.00 76.63 N ATOM 3110 CA CYS C 538 9.914 38.230 53.880 1.00 76.72 C ATOM 3111 C CYS C 538 8.594 38.162 54.640 1.00 78.73 C ATOM 3112 O CYS C 538 8.361 37.248 55.432 1.00 79.12 O ATOM 3113 CB CYS C 538 10.057 37.025 52.948 1.00 72.63 C ATOM 3114 SG CYS C 538 11.753 36.812 52.310 1.00 67.17 S ATOM 3115 N VAL C 539 7.734 39.144 54.388 1.00 80.68 N ATOM 3116 CA VAL C 539 6.433 39.228 55.040 1.00 82.30 C ATOM 3117 C VAL C 539 5.325 38.748 54.109 1.00 82.61 C ATOM 3118 O VAL C 539 4.232 38.402 54.557 1.00 83.44 O ATOM 3119 CB VAL C 539 6.130 40.680 55.469 1.00 82.60 C ATOM 3120 CG1 VAL C 539 4.789 40.748 56.187 1.00 83.10 C ATOM 3121 CG2 VAL C 539 7.249 41.197 56.358 1.00 83.03 C TER 3122 VAL C 539 ATOM 3123 N THR D 609 9.249 28.401 −7.677 1.00 104.80 N ATOM 3124 CA THR D 609 9.697 27.034 −7.441 1.00 104.82 C ATOM 3125 C THR D 609 10.982 27.017 −6.632 1.00 104.32 C ATOM 3126 O THR D 609 12.058 27.291 −7.165 1.00 104.68 O ATOM 3127 CB THR D 609 9.955 26.295 −8.763 1.00 105.25 C ATOM 3128 OG1 THR D 609 8.723 26.158 −9.480 1.00 106.41 O ATOM 3129 CG2 THR D 609 10.544 24.916 −8.499 1.00 105.53 C ATOM 3130 N ASN D 610 10.871 26.689 −5.348 1.00 103.19 N ATOM 3131 CA ASN D 610 12.049 26.644 −4.494 1.00 101.47 C ATOM 3132 C ASN D 610 11.835 25.834 −3.214 1.00 99.54 C ATOM 3133 O ASN D 610 11.326 24.712 −3.253 1.00 99.25 O ATOM 3134 CB ASN D 610 12.490 28.070 −4.146 1.00 102.29 C ATOM 3135 CG ASN D 610 13.967 28.158 −3.805 1.00 103.02 C ATOM 3136 OD1 ASN D 610 14.436 27.541 −2.848 1.00 103.61 O ATOM 3137 ND2 ASN D 610 14.710 28.931 −4.592 1.00 103.09 N ATOM 3138 N ASN D 611 12.225 26.423 −2.087 1.00 97.01 N ATOM 3139 CA ASN D 611 12.128 25.792 −0.774 1.00 93.50 C ATOM 3140 C ASN D 611 10.939 24.875 −0.529 1.00 90.18 C ATOM 3141 O ASN D 611 9.862 25.040 −1.103 1.00 90.09 O ATOM 3142 CB ASN D 611 12.170 26.857 0.324 1.00 94.97 C ATOM 3143 CG ASN D 611 13.502 27.574 0.385 1.00 95.78 C ATOM 3144 OD1 ASN D 611 14.553 26.944 0.507 1.00 95.59 O ATOM 3145 ND2 ASN D 611 13.466 28.901 0.304 1.00 96.69 N ATOM 3146 N VAL D 612 11.174 23.907 0.350 1.00 85.29 N ATOM 3147 CA VAL D 612 10.198 22.909 0.760 1.00 80.19 C ATOM 3148 C VAL D 612 10.842 22.227 1.960 1.00 75.88 C ATOM 3149 O VAL D 612 10.165 21.708 2.844 1.00 74.52 O ATOM 3150 CB VAL D 612 9.935 21.873 −0.358 1.00 81.35 C ATOM 3151 CG1 VAL D 612 11.238 21.205 −0.772 1.00 82.50 C ATOM 3152 CG2 VAL D 612 8.925 20.839 0.118 1.00 80.43 C ATOM 3153 N LYS D 613 12.170 22.243 1.975 1.00 71.51 N ATOM 3154 CA LYS D 613 12.933 21.670 3.072 1.00 67.34 C ATOM 3155 C LYS D 613 12.999 22.749 4.149 1.00 62.33 C ATOM 3156 O LYS D 613 13.083 22.450 5.339 1.00 61.50 O ATOM 3157 CB LYS D 613 14.343 21.297 2.613 1.00 69.74 C ATOM 3158 CG LYS D 613 15.170 22.469 2.107 1.00 72.74 C ATOM 3159 CD LYS D 613 16.618 22.067 1.847 1.00 74.87 C ATOM 3160 CE LYS D 613 17.369 21.759 3.144 1.00 76.97 C ATOM 3161 NZ LYS D 613 16.829 20.579 3.884 1.00 77.27 N ATOM 3162 N ASP D 614 12.973 24.006 3.715 1.00 56.07 N ATOM 3163 CA ASP D 614 12.984 25.137 4.639 1.00 49.70 C ATOM 3164 C ASP D 614 11.604 25.175 5.282 1.00 44.24 C ATOM 3165 O ASP D 614 11.444 25.616 6.419 1.00 40.58 O ATOM 3166 CB ASP D 614 13.248 26.446 3.886 1.00 51.87 C ATOM 3167 CG ASP D 614 14.726 26.831 3.870 1.00 53.98 C ATOM 3168 OD1 ASP D 614 15.580 25.965 4.162 1.00 56.47 O ATOM 3169 OD2 ASP D 614 15.034 28.003 3.557 1.00 56.08 O ATOM 3170 N VAL D 615 10.609 24.697 4.537 1.00 38.54 N ATOM 3171 CA VAL D 615 9.247 24.656 5.036 1.00 35.71 C ATOM 3172 C VAL D 615 9.154 23.643 6.175 1.00 33.47 C ATOM 3173 O VAL D 615 8.494 23.903 7.177 1.00 31.02 O ATOM 3174 CB VAL D 615 8.237 24.282 3.928 1.00 34.45 C ATOM 3175 CG1 VAL D 615 6.851 24.119 4.523 1.00 31.21 C ATOM 3176 CG2 VAL D 615 8.221 25.363 2.848 1.00 32.22 C ATOM 3177 N THR D 616 9.823 22.501 6.037 1.00 31.98 N ATOM 3178 CA THR D 616 9.786 21.503 7.102 1.00 32.69 C ATOM 3179 C THR D 616 10.533 22.047 8.318 1.00 30.76 C ATOM 3180 O THR D 616 10.155 21.793 9.460 1.00 30.94 O ATOM 3181 CB THR D 616 10.428 20.162 6.672 1.00 35.33 C ATOM 3182 OG1 THR D 616 11.846 20.328 6.547 1.00 41.34 O ATOM 3183 CG2 THR D 616 9.852 19.699 5.334 1.00 35.34 C ATOM 3184 N LYS D 617 11.589 22.816 8.076 1.00 29.35 N ATOM 3185 CA LYS D 617 12.344 23.393 9.180 1.00 29.05 C ATOM 3186 C LYS D 617 11.499 24.469 9.849 1.00 26.16 C ATOM 3187 O LYS D 617 11.512 24.613 11.068 1.00 25.52 O ATOM 3188 CB LYS D 617 13.660 24.007 8.684 1.00 31.88 C ATOM 3189 CG LYS D 617 14.657 22.995 8.131 1.00 36.84 C ATOM 3190 CD LYS D 617 15.973 23.669 7.729 1.00 40.64 C ATOM 3191 CE LYS D 617 16.962 22.657 7.167 1.00 42.08 C ATOM 3192 NZ LYS D 617 18.285 23.281 6.866 1.00 47.70 N ATOM 3193 N LEU D 618 10.761 25.219 9.042 1.00 23.72 N ATOM 3194 CA LEU D 618 9.913 26.274 9.562 1.00 23.58 C ATOM 3195 C LEU D 618 8.825 25.676 10.458 1.00 22.78 C ATOM 3196 O LEU D 618 8.595 26.150 11.565 1.00 22.16 O ATOM 3197 CB LEU D 618 9.277 27.050 8.404 1.00 25.27 C ATOM 3198 CG LEU D 618 8.511 28.330 8.742 1.00 22.16 C ATOM 3199 CD1 LEU D 618 9.457 29.310 9.442 1.00 25.36 C ATOM 3200 CD2 LEU D 618 7.941 28.948 7.474 1.00 21.74 C ATOM 3201 N VAL D 619 8.153 24.634 9.981 1.00 21.60 N ATOM 3202 CA VAL D 619 7.111 24.014 10.780 1.00 21.20 C ATOM 3203 C VAL D 619 7.722 23.610 12.114 1.00 19.91 C ATOM 3204 O VAL D 619 7.151 23.880 13.177 1.00 21.08 O ATOM 3205 CB VAL D 619 6.510 22.772 10.072 1.00 22.52 C ATOM 3206 CG1 VAL D 619 5.569 22.012 11.020 1.00 20.69 C ATOM 3207 CG2 VAL D 619 5.761 23.208 8.828 1.00 22.01 C ATOM 3208 N ALA D 620 8.898 22.995 12.058 1.00 19.29 N ATOM 3209 CA ALA D 620 9.593 22.559 13.271 1.00 22.19 C ATOM 3210 C ALA D 620 9.941 23.708 14.212 1.00 21.87 C ATOM 3211 O ALA D 620 9.997 23.527 15.431 1.00 22.55 O ATOM 3212 CB ALA D 620 10.882 21.791 12.900 1.00 22.64 C ATOM 3213 N ASN D 621 10.180 24.886 13.642 1.00 20.77 N ATOM 3214 CA ASN D 621 10.545 26.044 14.429 1.00 21.13 C ATOM 3215 C ASN D 621 9.398 26.989 14.776 1.00 22.18 C ATOM 3216 O ASN D 621 9.635 28.126 15.172 1.00 25.05 O ATOM 3217 CB ASN D 621 11.658 26.814 13.721 1.00 21.85 C ATOM 3218 CG ASN D 621 12.794 27.178 14.664 1.00 23.02 C ATOM 3219 OD1 ASN D 621 13.183 26.377 15.522 1.00 22.74 O ATOM 3220 ND2 ASN D 621 13.341 28.381 14.506 1.00 24.14 N ATOM 3221 N LEU D 622 8.161 26.524 14.626 1.00 20.56 N ATOM 3222 CA LEU D 622 6.988 27.328 14.965 1.00 20.70 C ATOM 3223 C LEU D 622 6.262 26.587 16.081 1.00 19.87 C ATOM 3224 O LEU D 622 6.276 25.357 16.109 1.00 20.57 O ATOM 3225 CB LEU D 622 6.076 27.504 13.739 1.00 19.75 C ATOM 3226 CG LEU D 622 6.608 28.485 12.679 1.00 20.96 C ATOM 3227 CD1 LEU D 622 5.782 28.448 11.379 1.00 18.20 C ATOM 3228 CD2 LEU D 622 6.600 29.879 13.291 1.00 21.02 C ATOM 3229 N PRO D 623 5.645 27.317 17.038 1.00 17.52 N ATOM 3230 CA PRO D 623 4.947 26.611 18.119 1.00 20.47 C ATOM 3231 C PRO D 623 3.795 25.789 17.543 1.00 22.37 C ATOM 3232 O PRO D 623 3.043 26.292 16.697 1.00 19.83 O ATOM 3233 CB PRO D 623 4.435 27.740 19.016 1.00 18.11 C ATOM 3234 CG PRO D 623 5.272 28.928 18.638 1.00 17.91 C ATOM 3235 CD PRO D 623 5.440 28.770 17.153 1.00 16.64 C ATOM 3236 N LYS D 624 3.668 24.538 17.994 1.00 21.53 N ATOM 3237 CA LYS D 624 2.596 23.661 17.521 1.00 26.57 C ATOM 3238 C LYS D 624 1.207 24.258 17.776 1.00 27.64 C ATOM 3239 O LYS D 624 0.252 23.910 17.093 1.00 30.00 O ATOM 3240 CB LYS D 624 2.665 22.282 18.204 1.00 25.86 C ATOM 3241 CG LYS D 624 3.908 21.478 17.876 1.00 31.06 C ATOM 3242 CD LYS D 624 3.932 20.129 18.594 1.00 31.72 C ATOM 3243 CE LYS D 624 5.322 19.472 18.497 1.00 33.07 C ATOM 3244 NZ LYS D 624 5.356 18.078 19.056 1.00 31.48 N ATOM 3245 N ASP D 625 1.085 25.149 18.756 1.00 28.70 N ATOM 3246 CA ASP D 625 −0.221 25.724 19.052 1.00 30.74 C ATOM 3247 C ASP D 625 −0.429 27.166 18.560 1.00 30.14 C ATOM 3248 O ASP D 625 −1.396 27.828 18.933 1.00 29.70 O ATOM 3249 CB ASP D 625 −0.527 25.596 20.562 1.00 30.51 C ATOM 3250 CG ASP D 625 0.474 26.333 21.439 1.00 34.32 C ATOM 3251 OD1 ASP D 625 1.687 26.271 21.158 1.00 33.59 O ATOM 3252 OD2 ASP D 625 0.046 26.964 22.432 1.00 40.39 O ATOM 3253 N TYR D 626 0.465 27.648 17.705 1.00 29.06 N ATOM 3254 CA TYR D 626 0.308 28.988 17.171 1.00 27.36 C ATOM 3255 C TYR D 626 −0.647 28.868 15.976 1.00 28.81 C ATOM 3256 O TYR D 626 −0.432 28.055 15.078 1.00 29.03 O ATOM 3257 CB TYR D 626 1.657 29.530 16.724 1.00 27.84 C ATOM 3258 CG TYR D 626 1.641 30.989 16.344 1.00 24.37 C ATOM 3259 CD1 TYR D 626 1.307 31.969 17.270 1.00 24.30 C ATOM 3260 CD2 TYR D 626 1.999 31.389 15.062 1.00 25.35 C ATOM 3261 CE1 TYR D 626 1.338 33.326 16.922 1.00 22.03 C ATOM 3262 CE2 TYR D 626 2.029 32.719 14.706 1.00 21.86 C ATOM 3263 CZ TYR D 626 1.705 33.684 15.635 1.00 22.40 C ATOM 3264 OH TYR D 626 1.793 35.010 15.270 1.00 26.81 O ATOM 3265 N MET D 627 −1.712 29.660 15.979 1.00 27.81 N ATOM 3266 CA MET D 627 −2.692 29.614 14.902 1.00 27.77 C ATOM 3267 C MET D 627 −2.414 30.687 13.879 1.00 26.69 C ATOM 3268 O MET D 627 −2.155 31.847 14.229 1.00 27.26 O ATOM 3269 CB MET D 627 −4.111 29.795 15.449 1.00 29.13 C ATOM 3270 CG MET D 627 −4.483 28.783 16.530 1.00 33.45 C ATOM 3271 SD MET D 627 −4.081 27.094 16.044 1.00 39.63 S ATOM 3272 CE MET D 627 −5.527 26.652 15.050 1.00 38.53 C ATOM 3273 N ILE D 628 −2.451 30.292 12.612 1.00 24.67 N ATOM 3274 CA ILE D 628 −2.219 31.221 11.522 1.00 25.62 C ATOM 3275 C ILE D 628 −3.526 31.385 10.757 1.00 26.27 C ATOM 3276 O ILE D 628 −4.167 30.395 10.386 1.00 22.16 O ATOM 3277 CB ILE D 628 −1.144 30.692 10.547 1.00 25.29 C ATOM 3278 CG1 ILE D 628 0.138 30.346 11.315 1.00 26.17 C ATOM 3279 CG2 ILE D 628 −0.851 31.753 9.485 1.00 25.31 C ATOM 3280 CD1 ILE D 628 1.186 29.612 10.487 1.00 22.59 C ATOM 3281 N THR D 629 −3.912 32.633 10.515 1.00 28.09 N ATOM 3282 CA THR D 629 −5.144 32.912 9.779 1.00 31.02 C ATOM 3283 C THR D 629 −4.949 32.944 8.271 1.00 30.20 C ATOM 3284 O THR D 629 −3.988 33.518 7.755 1.00 27.82 O ATOM 3285 CB THR D 629 −5.756 34.250 10.162 1.00 32.14 C ATOM 3286 OG1 THR D 629 −5.718 34.408 11.582 1.00 37.56 O ATOM 3287 CG2 THR D 629 −7.202 34.295 9.697 1.00 36.14 C ATOM 3288 N LEU D 630 −5.898 32.341 7.574 1.00 30.44 N ATOM 3289 CA LEU D 630 −5.866 32.271 6.131 1.00 32.20 C ATOM 3290 C LEU D 630 −7.297 32.212 5.629 1.00 34.56 C ATOM 3291 O LEU D 630 −8.097 31.390 6.092 1.00 33.39 O ATOM 3292 CB LEU D 630 −5.113 31.002 5.670 1.00 28.93 C ATOM 3293 CG LEU D 630 −5.202 30.639 4.177 1.00 27.21 C ATOM 3294 CD1 LEU D 630 −4.440 31.676 3.365 1.00 22.63 C ATOM 3295 CD2 LEU D 630 −4.641 29.232 3.916 1.00 25.04 C ATOM 3296 N LYS D 631 −7.629 33.088 4.692 1.00 37.84 N ATOM 3297 CA LYS D 631 −8.963 33.058 4.118 1.00 42.10 C ATOM 3298 C LYS D 631 −8.918 31.896 3.135 1.00 44.08 C ATOM 3299 O LYS D 631 −8.337 31.993 2.054 1.00 41.39 O ATOM 3300 CB LYS D 631 −9.276 34.379 3.418 1.00 42.62 C ATOM 3301 CG LYS D 631 −9.395 35.528 4.403 1.00 44.88 C ATOM 3302 CD LYS D 631 −9.531 36.864 3.707 1.00 47.80 C ATOM 3303 CE LYS D 631 −9.388 37.990 4.711 1.00 49.65 C ATOM 3304 NZ LYS D 631 −9.271 39.314 4.048 1.00 54.29 N ATOM 3305 N TYR D 632 −9.500 30.782 3.558 1.00 48.07 N ATOM 3306 CA TYR D 632 −9.534 29.566 2.771 1.00 53.34 C ATOM 3307 C TYR D 632 −10.583 29.681 1.665 1.00 55.29 C ATOM 3308 O TYR D 632 −11.699 30.154 1.899 1.00 55.86 O ATOM 3309 CB TYR D 632 −9.865 28.389 3.691 1.00 57.34 C ATOM 3310 CG TYR D 632 −9.485 27.026 3.154 1.00 61.63 C ATOM 3311 CD1 TYR D 632 −8.150 26.674 2.976 1.00 62.09 C ATOM 3312 CD2 TYR D 632 −10.462 26.077 2.850 1.00 64.00 C ATOM 3313 CE1 TYR D 632 −7.795 25.414 2.513 1.00 64.69 C ATOM 3314 CE2 TYR D 632 −10.117 24.810 2.383 1.00 65.21 C ATOM 3315 CZ TYR D 632 −8.781 24.485 2.218 1.00 65.98 C ATOM 3316 OH TYR D 632 −8.430 23.239 1.748 1.00 66.91 O ATOM 3317 N VAL D 633 −10.217 29.260 0.458 1.00 56.89 N ATOM 3318 CA VAL D 633 −11.136 29.296 −0.675 1.00 58.30 C ATOM 3319 C VAL D 633 −12.053 28.073 −0.623 1.00 59.02 C ATOM 3320 O VAL D 633 −11.609 26.969 −0.320 1.00 58.72 O ATOM 3321 CB VAL D 633 −10.363 29.322 −2.019 1.00 58.62 C ATOM 3322 CG1 VAL D 633 −11.200 28.713 −3.130 1.00 59.35 C ATOM 3323 CG2 VAL D 633 −10.009 30.757 −2.378 1.00 57.39 C ATOM 3324 N PRO D 634 −13.350 28.264 −0.920 1.00 61.02 N ATOM 3325 CA PRO D 634 −14.383 27.223 −0.923 1.00 62.30 C ATOM 3326 C PRO D 634 −13.921 25.775 −1.086 1.00 62.35 C ATOM 3327 O PRO D 634 −13.371 25.184 −0.155 1.00 62.18 O ATOM 3328 CB PRO D 634 −15.302 27.677 −2.048 1.00 62.26 C ATOM 3329 CG PRO D 634 −15.345 29.157 −1.802 1.00 63.32 C ATOM 3330 CD PRO D 634 −13.881 29.509 −1.511 1.00 62.09 C ATOM 3331 N GLY D 635 −14.154 25.202 −2.262 1.00 62.41 N ATOM 3332 CA GLY D 635 −13.767 23.818 −2.482 1.00 64.17 C ATOM 3333 C GLY D 635 −12.385 23.654 −3.073 1.00 64.49 C ATOM 3334 O GLY D 635 −12.181 22.822 −3.962 1.00 64.76 O ATOM 3335 N MET D 636 −11.433 24.434 −2.566 1.00 64.65 N ATOM 3336 CA MET D 636 −10.062 24.402 −3.065 1.00 64.78 C ATOM 3337 C MET D 636 −9.326 23.086 −2.823 1.00 64.92 C ATOM 3338 O MET D 636 −8.104 23.031 −2.953 1.00 65.98 O ATOM 3339 CB MET D 636 −9.242 25.537 −2.446 1.00 65.11 C ATOM 3340 CG MET D 636 −8.795 25.268 −1.013 1.00 65.13 C ATOM 3341 SD MET D 636 −7.160 25.975 −0.639 1.00 67.60 S ATOM 3342 CE MET D 636 −6.056 24.678 −1.286 1.00 63.14 C ATOM 3343 N ASP D 637 −10.046 22.029 −2.469 1.00 64.44 N ATOM 3344 CA ASP D 637 −9.382 20.754 −2.230 1.00 64.50 C ATOM 3345 C ASP D 637 −9.855 19.712 −3.229 1.00 63.89 C ATOM 3346 O ASP D 637 −9.095 18.826 −3.620 1.00 63.15 O ATOM 3347 CB ASP D 637 −9.662 20.263 −0.808 1.00 65.45 C ATOM 3348 CG ASP D 637 −10.970 19.508 −0.702 1.00 66.50 C ATOM 3349 OD1 ASP D 637 −11.989 20.007 −1.229 1.00 67.34 O ATOM 3350 OD2 ASP D 637 −10.979 18.418 −0.087 1.00 67.32 O ATOM 3351 N VAL D 638 −11.113 19.827 −3.643 1.00 64.62 N ATOM 3352 CA VAL D 638 −11.693 18.880 −4.588 1.00 65.92 C ATOM 3353 C VAL D 638 −11.757 19.406 −6.020 1.00 69.41 C ATOM 3354 O VAL D 638 −11.298 18.737 −6.948 1.00 69.69 O ATOM 3355 CB VAL D 638 −13.114 18.455 −4.147 1.00 62.82 C ATOM 3356 CG1 VAL D 638 −13.034 17.657 −2.857 1.00 61.12 C ATOM 3357 CG2 VAL D 638 −13.997 19.681 −3.957 1.00 60.81 C ATOM 3358 N LEU D 639 −12.327 20.595 −6.201 1.00 73.26 N ATOM 3359 CA LEU D 639 −12.439 21.184 −7.530 1.00 78.29 C ATOM 3360 C LEU D 639 −11.082 21.251 −8.225 1.00 86.56 C ATOM 3361 O LEU D 639 −10.036 21.192 −7.575 1.00 86.40 O ATOM 3362 CB LEU D 639 −13.046 22.588 −7.446 1.00 73.68 C ATOM 3363 CG LEU D 639 −14.565 22.684 −7.275 1.00 69.04 C ATOM 3364 CD1 LEU D 639 −14.983 22.060 −5.955 1.00 66.96 C ATOM 3365 CD2 LEU D 639 −14.986 24.148 −7.336 1.00 66.40 C ATOM 3366 N PRO D 640 −11.083 21.379 −9.562 1.00 90.46 N ATOM 3367 CA PRO D 640 −9.840 21.451 −10.334 1.00 96.88 C ATOM 3368 C PRO D 640 −8.972 22.651 −9.965 1.00 101.73 C ATOM 3369 O PRO D 640 −9.476 23.684 −9.522 1.00 102.12 O ATOM 3370 CB PRO D 640 −10.339 21.518 −11.774 1.00 97.23 C ATOM 3371 CG PRO D 640 −11.635 22.257 −11.637 1.00 96.90 C ATOM 3372 CD PRO D 640 −12.251 21.575 −10.440 1.00 92.55 C ATOM 3373 N SER D 641 −7.665 22.499 −10.156 1.00 105.53 N ATOM 3374 CA SER D 641 −6.705 23.553 −9.854 1.00 109.37 C ATOM 3375 C SER D 641 −6.828 24.693 −10.861 1.00 110.52 C ATOM 3376 O SER D 641 −5.826 25.215 −11.353 1.00 111.81 O ATOM 3377 CB SER D 641 −5.281 22.990 −9.888 1.00 111.58 C ATOM 3378 OG SER D 641 −4.914 22.597 −11.198 1.00 114.18 O ATOM 3379 N HIS D 642 −8.066 25.066 −11.166 1.00 110.97 N ATOM 3380 CA HIS D 642 −8.343 26.142 −12.107 1.00 110.40 C ATOM 3381 C HIS D 642 −9.260 27.140 −11.423 1.00 108.41 C ATOM 3382 O HIS D 642 −9.047 28.350 −11.491 1.00 108.42 O ATOM 3383 CB HIS D 642 −9.027 25.587 −13.357 1.00 112.21 C ATOM 3384 CG HIS D 642 −8.258 24.495 −14.030 1.00 113.95 C ATOM 3385 ND1 HIS D 642 −6.974 24.669 −14.499 1.00 114.98 N ATOM 3386 CD2 HIS D 642 −8.591 23.213 −14.313 1.00 114.86 C ATOM 3387 CE1 HIS D 642 −6.548 23.542 −15.042 1.00 115.59 C ATOM 3388 NE2 HIS D 642 −7.511 22.643 −14.942 1.00 115.50 N ATOM 3389 N CYS D 643 −10.285 26.616 −10.763 1.00 105.86 N ATOM 3390 CA CYS D 643 −11.241 27.445 −10.049 1.00 102.95 C ATOM 3391 C CYS D 643 −10.504 28.309 −9.031 1.00 100.68 C ATOM 3392 O CYS D 643 −10.472 29.535 −9.152 1.00 100.62 O ATOM 3393 CB CYS D 643 −12.275 26.563 −9.342 1.00 103.59 C ATOM 3394 SG CYS D 643 −13.485 25.768 −10.448 1.00 102.50 S ATOM 3395 N TRP D 644 −9.908 27.663 −8.033 1.00 97.42 N ATOM 3396 CA TRP D 644 −9.167 28.377 −7.000 1.00 93.72 C ATOM 3397 C TRP D 644 −7.741 28.703 −7.445 1.00 90.99 C ATOM 3398 O TRP D 644 −7.532 29.219 −8.542 1.00 91.82 O ATOM 3399 CB TRP D 644 −9.144 27.564 −5.698 1.00 93.17 C ATOM 3400 CG TRP D 644 −8.830 26.110 −5.874 1.00 92.17 C ATOM 3401 CD1 TRP D 644 −9.645 25.153 −6.409 1.00 92.07 C ATOM 3402 CD2 TRP D 644 −7.613 25.446 −5.516 1.00 91.66 C ATOM 3403 NE1 TRP D 644 −9.011 23.934 −6.405 1.00 91.70 N ATOM 3404 CE2 TRP D 644 −7.762 24.085 −5.864 1.00 91.39 C ATOM 3405 CE3 TRP D 644 −6.409 25.868 −4.935 1.00 91.54 C ATOM 3406 CZ2 TRP D 644 −6.752 23.142 −5.651 1.00 91.23 C ATOM 3407 CZ3 TRP D 644 −5.402 24.929 −4.723 1.00 91.15 C ATOM 3408 CH2 TRP D 644 −5.582 23.581 −5.081 1.00 91.44 C ATOM 3409 N ILE D 645 −6.771 28.404 −6.588 1.00 87.01 N ATOM 3410 CA ILE D 645 −5.364 28.668 −6.873 1.00 82.82 C ATOM 3411 C ILE D 645 −5.059 30.145 −7.063 1.00 79.68 C ATOM 3412 O ILE D 645 −4.244 30.714 −6.338 1.00 78.71 O ATOM 3413 CB ILE D 645 −4.881 27.907 −8.121 1.00 83.33 C ATOM 3414 CG1 ILE D 645 −4.632 26.444 −7.761 1.00 83.90 C ATOM 3415 CG2 ILE D 645 −3.609 28.546 −8.668 1.00 83.53 C ATOM 3416 CD1 ILE D 645 −3.919 25.666 −8.839 1.00 85.34 C ATOM 3417 N SER D 646 −5.697 30.763 −8.049 1.00 76.22 N ATOM 3418 CA SER D 646 −5.477 32.176 −8.308 1.00 72.36 C ATOM 3419 C SER D 646 −5.791 32.968 −7.044 1.00 68.74 C ATOM 3420 O SER D 646 −5.033 33.854 −6.651 1.00 67.25 O ATOM 3421 CB SER D 646 −6.364 32.652 −9.457 1.00 73.20 C ATOM 3422 OG SER D 646 −6.150 34.028 −9.719 1.00 72.80 O ATOM 3423 N GLU D 647 −6.907 32.636 −6.404 1.00 65.08 N ATOM 3424 CA GLU D 647 −7.306 33.317 −5.181 1.00 62.17 C ATOM 3425 C GLU D 647 −6.456 32.834 −4.007 1.00 59.05 C ATOM 3426 O GLU D 647 −5.992 33.633 −3.193 1.00 56.23 O ATOM 3427 CB GLU D 647 −8.788 33.067 −4.894 1.00 63.15 C ATOM 3428 CG GLU D 647 −9.310 33.796 −3.662 1.00 66.05 C ATOM 3429 CD GLU D 647 −9.198 35.310 −3.773 1.00 68.11 C ATOM 3430 OE1 GLU D 647 −9.806 35.891 −4.699 1.00 69.38 O ATOM 3431 OE2 GLU D 647 −8.504 35.918 −2.929 1.00 68.44 O ATOM 3432 N MET D 648 −6.250 31.523 −3.925 1.00 56.89 N ATOM 3433 CA MET D 648 −5.442 30.963 −2.852 1.00 55.25 C ATOM 3434 C MET D 648 −4.088 31.644 −2.788 1.00 53.08 C ATOM 3435 O MET D 648 −3.683 32.139 −1.737 1.00 53.75 O ATOM 3436 CB MET D 648 −5.237 29.468 −3.050 1.00 55.54 C ATOM 3437 CG MET D 648 −6.100 28.619 −2.147 1.00 60.03 C ATOM 3438 SD MET D 648 −5.943 29.094 −0.401 1.00 63.69 S ATOM 3439 CE MET D 648 −7.335 30.206 −0.245 1.00 58.42 C ATOM 3440 N VAL D 649 −3.391 31.667 −3.919 1.00 49.36 N ATOM 3441 CA VAL D 649 −2.077 32.285 −3.988 1.00 46.89 C ATOM 3442 C VAL D 649 −2.086 33.707 −3.437 1.00 44.43 C ATOM 3443 O VAL D 649 −1.139 34.121 −2.774 1.00 44.35 O ATOM 3444 CB VAL D 649 −1.541 32.275 −5.437 1.00 47.15 C ATOM 3445 CG1 VAL D 649 −0.321 33.168 −5.554 1.00 49.44 C ATOM 3446 CG2 VAL D 649 −1.166 30.847 −5.831 1.00 47.73 C ATOM 3447 N VAL D 650 −3.153 34.454 −3.705 1.00 41.65 N ATOM 3448 CA VAL D 650 −3.261 35.817 −3.199 1.00 38.93 C ATOM 3449 C VAL D 650 −3.440 35.780 −1.688 1.00 36.51 C ATOM 3450 O VAL D 650 −2.888 36.611 −0.966 1.00 38.35 O ATOM 3451 CB VAL D 650 −4.468 36.562 −3.818 1.00 40.92 C ATOM 3452 CG1 VAL D 650 −4.664 37.924 −3.131 1.00 36.92 C ATOM 3453 CG2 VAL D 650 −4.249 36.741 −5.306 1.00 39.66 C ATOM 3454 N GLN D 651 −4.220 34.814 −1.219 1.00 34.68 N ATOM 3455 CA GLN D 651 −4.477 34.652 0.206 1.00 35.25 C ATOM 3456 C GLN D 651 −3.260 34.147 0.977 1.00 33.77 C ATOM 3457 O GLN D 651 −3.045 34.530 2.122 1.00 33.36 O ATOM 3458 CB GLN D 651 −5.654 33.704 0.423 1.00 35.38 C ATOM 3459 CG GLN D 651 −6.992 34.289 −0.005 1.00 39.24 C ATOM 3460 CD GLN D 651 −7.201 35.707 0.514 1.00 39.71 C ATOM 3461 OE1 GLN D 651 −6.848 36.026 1.651 1.00 41.62 O ATOM 3462 NE2 GLN D 651 −7.779 36.562 −0.320 1.00 41.54 N ATOM 3463 N LEU D 652 −2.473 33.282 0.350 1.00 32.28 N ATOM 3464 CA LEU D 652 −1.278 32.749 0.989 1.00 32.03 C ATOM 3465 C LEU D 652 −0.255 33.850 1.164 1.00 31.64 C ATOM 3466 O LEU D 652 0.453 33.899 2.160 1.00 32.05 O ATOM 3467 CB LEU D 652 −0.671 31.636 0.143 1.00 31.97 C ATOM 3468 CG LEU D 652 −1.391 30.298 0.254 1.00 30.73 C ATOM 3469 CD1 LEU D 652 −0.879 29.344 −0.811 1.00 30.88 C ATOM 3470 CD2 LEU D 652 −1.164 29.740 1.649 1.00 30.69 C ATOM 3471 N SER D 653 −0.180 34.740 0.188 1.00 32.28 N ATOM 3472 CA SER D 653 0.767 35.831 0.264 1.00 34.28 C ATOM 3473 C SER D 653 0.393 36.792 1.390 1.00 35.52 C ATOM 3474 O SER D 653 1.260 37.317 2.083 1.00 35.54 O ATOM 3475 CB SER D 653 0.819 36.568 −1.074 1.00 34.23 C ATOM 3476 OG SER D 653 1.768 37.617 −1.021 1.00 35.34 O ATOM 3477 N ASP D 654 −0.899 37.036 1.576 1.00 37.08 N ATOM 3478 CA ASP D 654 −1.315 37.931 2.647 1.00 38.55 C ATOM 3479 C ASP D 654 −1.021 37.290 3.990 1.00 36.67 C ATOM 3480 O ASP D 654 −0.482 37.937 4.887 1.00 37.06 O ATOM 3481 CB ASP D 654 −2.805 38.266 2.540 1.00 43.76 C ATOM 3482 CG ASP D 654 −3.066 39.469 1.647 1.00 50.69 C ATOM 3483 OD1 ASP D 654 −2.380 40.504 1.835 1.00 55.30 O ATOM 3484 OD2 ASP D 654 −3.954 39.389 0.765 1.00 53.94 O ATOM 3485 N SER D 655 −1.371 36.016 4.127 1.00 33.71 N ATOM 3486 CA SER D 655 −1.119 35.299 5.375 1.00 32.76 C ATOM 3487 C SER D 655 0.370 35.228 5.703 1.00 32.30 C ATOM 3488 O SER D 655 0.759 35.327 6.867 1.00 33.34 O ATOM 3489 CB SER D 655 −1.695 33.883 5.303 1.00 29.84 C ATOM 3490 OG SER D 655 −3.108 33.915 5.437 1.00 32.16 O ATOM 3491 N LEU D 656 1.196 35.049 4.677 1.00 31.24 N ATOM 3492 CA LEU D 656 2.641 34.959 4.863 1.00 30.45 C ATOM 3493 C LEU D 656 3.198 36.325 5.205 1.00 29.81 C ATOM 3494 O LEU D 656 4.071 36.455 6.063 1.00 30.17 O ATOM 3495 CB LEU D 656 3.308 34.424 3.596 1.00 30.74 C ATOM 3496 CG LEU D 656 3.135 32.926 3.337 1.00 31.26 C ATOM 3497 CD1 LEU D 656 3.629 32.574 1.937 1.00 29.15 C ATOM 3498 CD2 LEU D 656 3.896 32.144 4.403 1.00 30.48 C ATOM 3499 N THR D 657 2.681 37.344 4.535 1.00 30.26 N ATOM 3500 CA THR D 657 3.104 38.712 4.783 1.00 32.29 C ATOM 3501 C THR D 657 2.778 39.138 6.213 1.00 32.55 C ATOM 3502 O THR D 657 3.583 39.802 6.862 1.00 34.64 O ATOM 3503 CB THR D 657 2.432 39.677 3.802 1.00 34.30 C ATOM 3504 OG1 THR D 657 2.838 39.345 2.471 1.00 32.27 O ATOM 3505 CG2 THR D 657 2.826 41.122 4.110 1.00 33.78 C ATOM 3506 N ASP D 658 1.601 38.763 6.702 1.00 34.08 N ATOM 3507 CA ASP D 658 1.199 39.097 8.071 1.00 33.18 C ATOM 3508 C ASP D 658 2.129 38.357 9.031 1.00 31.81 C ATOM 3509 O ASP D 658 2.603 38.903 10.027 1.00 30.73 O ATOM 3510 CB ASP D 658 −0.239 38.636 8.347 1.00 38.52 C ATOM 3511 CG ASP D 658 −1.272 39.288 7.424 1.00 44.07 C ATOM 3512 OD1 ASP D 658 −2.462 38.886 7.501 1.00 44.99 O ATOM 3513 OD2 ASP D 658 −0.908 40.195 6.634 1.00 47.21 O ATOM 3514 N LEU D 659 2.380 37.094 8.721 1.00 29.64 N ATOM 3515 CA LEU D 659 3.234 36.260 9.550 1.00 29.57 C ATOM 3516 C LEU D 659 4.643 36.850 9.684 1.00 30.44 C ATOM 3517 O LEU D 659 5.180 36.946 10.780 1.00 28.18 O ATOM 3518 CB LEU D 659 3.294 34.856 8.952 1.00 27.20 C ATOM 3519 CG LEU D 659 3.988 33.762 9.749 1.00 28.07 C ATOM 3520 CD1 LEU D 659 3.273 33.547 11.073 1.00 24.43 C ATOM 3521 CD2 LEU D 659 3.992 32.481 8.929 1.00 26.60 C ATOM 3522 N LEU D 660 5.223 37.263 8.561 1.00 32.08 N ATOM 3523 CA LEU D 660 6.566 37.839 8.542 1.00 32.91 C ATOM 3524 C LEU D 660 6.762 38.890 9.628 1.00 34.49 C ATOM 3525 O LEU D 660 7.775 38.895 10.326 1.00 36.94 O ATOM 3526 CB LEU D 660 6.844 38.458 7.169 1.00 32.39 C ATOM 3527 CG LEU D 660 8.290 38.718 6.733 1.00 32.52 C ATOM 3528 CD1 LEU D 660 9.087 37.429 6.762 1.00 32.35 C ATOM 3529 CD2 LEU D 660 8.301 39.308 5.333 1.00 32.10 C ATOM 3530 N ASP D 661 5.792 39.778 9.783 1.00 36.15 N ATOM 3531 CA ASP D 661 5.894 40.832 10.785 1.00 34.98 C ATOM 3532 C ASP D 661 5.908 40.354 12.243 1.00 32.23 C ATOM 3533 O ASP D 661 6.042 41.165 13.153 1.00 33.01 O ATOM 3534 CB ASP D 661 4.773 41.863 10.578 1.00 37.81 C ATOM 3535 CG ASP D 661 5.132 42.913 9.528 1.00 43.94 C ATOM 3536 OD1 ASP D 661 6.117 43.651 9.758 1.00 46.95 O ATOM 3537 OD2 ASP D 661 4.443 43.006 8.479 1.00 44.46 O ATOM 3538 N LYS D 662 5.783 39.050 12.475 1.00 27.57 N ATOM 3539 CA LYS D 662 5.805 38.531 13.848 1.00 25.47 C ATOM 3540 C LYS D 662 7.216 38.116 14.290 1.00 25.22 C ATOM 3541 O LYS D 662 7.436 37.750 15.449 1.00 24.24 O ATOM 3542 CB LYS D 662 4.864 37.328 13.975 1.00 23.70 C ATOM 3543 CG LYS D 662 3.433 37.635 13.543 1.00 26.08 C ATOM 3544 CD LYS D 662 2.815 38.689 14.439 1.00 27.79 C ATOM 3545 CE LYS D 662 1.554 39.262 13.821 1.00 30.66 C ATOM 3546 NZ LYS D 662 0.627 38.194 13.388 1.00 35.04 N ATOM 3547 N PHE D 663 8.165 38.167 13.360 1.00 22.40 N ATOM 3548 CA PHE D 663 9.538 37.784 13.662 1.00 24.06 C ATOM 3549 C PHE D 663 10.503 38.921 13.350 1.00 23.21 C ATOM 3550 O PHE D 663 10.111 39.918 12.759 1.00 23.66 O ATOM 3551 CB PHE D 663 9.915 36.520 12.861 1.00 25.53 C ATOM 3552 CG PHE D 663 9.010 35.335 13.133 1.00 26.81 C ATOM 3553 CD1 PHE D 663 7.894 35.091 12.331 1.00 27.78 C ATOM 3554 CD2 PHE D 663 9.244 34.499 14.226 1.00 22.65 C ATOM 3555 CE1 PHE D 663 7.021 34.022 12.617 1.00 26.90 C ATOM 3556 CE2 PHE D 663 8.384 33.443 14.518 1.00 24.82 C ATOM 3557 CZ PHE D 663 7.273 33.202 13.714 1.00 25.89 C ATOM 3558 N SER D 664 11.756 38.773 13.774 1.00 24.44 N ATOM 3559 CA SER D 664 12.791 39.775 13.527 1.00 25.43 C ATOM 3560 C SER D 664 14.016 39.062 12.985 1.00 24.80 C ATOM 3561 O SER D 664 14.173 37.855 13.153 1.00 25.13 O ATOM 3562 CB SER D 664 13.204 40.487 14.825 1.00 26.59 C ATOM 3563 OG SER D 664 12.087 40.922 15.569 1.00 31.80 O ATOM 3564 N ASN D 665 14.894 39.821 12.350 1.00 24.87 N ATOM 3565 CA ASN D 665 16.136 39.277 11.819 1.00 24.88 C ATOM 3566 C ASN D 665 17.097 39.010 12.969 1.00 24.12 C ATOM 3567 O ASN D 665 16.887 39.477 14.089 1.00 21.58 O ATOM 3568 CB ASN D 665 16.785 40.284 10.871 1.00 26.92 C ATOM 3569 CG ASN D 665 15.990 40.484 9.610 1.00 24.93 C ATOM 3570 OD1 ASN D 665 16.013 39.646 8.718 1.00 28.79 O ATOM 3571 ND2 ASN D 665 15.269 41.594 9.533 1.00 27.05 N ATOM 3572 N ILE D 666 18.149 38.252 12.680 1.00 24.28 N ATOM 3573 CA ILE D 666 19.182 37.947 13.661 1.00 26.69 C ATOM 3574 C ILE D 666 20.530 38.117 12.965 1.00 28.56 C ATOM 3575 O ILE D 666 20.594 38.244 11.746 1.00 29.39 O ATOM 3576 CB ILE D 666 19.058 36.494 14.213 1.00 26.87 C ATOM 3577 CG1 ILE D 666 19.111 35.480 13.061 1.00 24.65 C ATOM 3578 CG2 ILE D 666 17.764 36.348 15.000 1.00 24.84 C ATOM 3579 CD1 ILE D 666 19.048 34.021 13.530 1.00 27.83 C ATOM 3580 N SER D 667 21.606 38.116 13.735 1.00 33.18 N ATOM 3581 CA SER D 667 22.940 38.287 13.167 1.00 36.42 C ATOM 3582 C SER D 667 23.378 37.109 12.290 1.00 36.58 C ATOM 3583 O SER D 667 24.070 37.301 11.288 1.00 38.40 O ATOM 3584 CB SER D 667 23.959 38.511 14.292 1.00 39.38 C ATOM 3585 OG SER D 667 25.231 38.838 13.760 1.00 46.92 O ATOM 3586 N GLU D 668 22.993 35.892 12.667 1.00 34.88 N ATOM 3587 CA GLU D 668 23.356 34.711 11.882 1.00 34.52 C ATOM 3588 C GLU D 668 22.581 33.481 12.320 1.00 31.66 C ATOM 3589 O GLU D 668 21.932 33.497 13.353 1.00 29.21 O ATOM 3590 CB GLU D 668 24.870 34.424 11.971 1.00 38.03 C ATOM 3591 CG GLU D 668 25.628 35.126 13.108 1.00 44.35 C ATOM 3592 CD GLU D 668 25.293 34.587 14.486 1.00 48.70 C ATOM 3593 OE1 GLU D 668 24.088 34.510 14.817 1.00 51.51 O ATOM 3594 OE2 GLU D 668 26.237 34.253 15.243 1.00 49.33 O ATOM 3595 N GLY D 669 22.655 32.418 11.526 1.00 31.97 N ATOM 3596 CA GLY D 669 21.967 31.179 11.860 1.00 32.06 C ATOM 3597 C GLY D 669 20.536 31.057 11.364 1.00 32.25 C ATOM 3598 O GLY D 669 20.025 31.933 10.665 1.00 33.15 O ATOM 3599 N LEU D 670 19.890 29.956 11.742 1.00 33.75 N ATOM 3600 CA LEU D 670 18.504 29.657 11.368 1.00 32.29 C ATOM 3601 C LEU D 670 17.562 30.800 11.776 1.00 30.44 C ATOM 3602 O LEU D 670 17.341 31.042 12.974 1.00 30.45 O ATOM 3603 CB LEU D 670 18.061 28.363 12.058 1.00 35.46 C ATOM 3604 CG LEU D 670 16.981 27.492 11.395 1.00 37.43 C ATOM 3605 CD1 LEU D 670 16.490 26.458 12.406 1.00 37.83 C ATOM 3606 CD2 LEU D 670 15.826 28.346 10.919 1.00 40.46 C ATOM 3607 N SER D 671 17.001 31.482 10.778 1.00 25.84 N ATOM 3608 CA SER D 671 16.094 32.615 11.007 1.00 23.68 C ATOM 3609 C SER D 671 14.693 32.368 10.446 1.00 23.41 C ATOM 3610 O SER D 671 14.529 32.194 9.236 1.00 21.63 O ATOM 3611 CB SER D 671 16.675 33.871 10.356 1.00 23.21 C ATOM 3612 OG SER D 671 15.746 34.934 10.338 1.00 25.59 O ATOM 3613 N ASN D 672 13.689 32.349 11.320 1.00 21.36 N ATOM 3614 CA ASN D 672 12.308 32.143 10.875 1.00 22.35 C ATOM 3615 C ASN D 672 11.912 33.258 9.902 1.00 22.21 C ATOM 3616 O ASN D 672 11.157 33.032 8.950 1.00 24.69 O ATOM 3617 CB ASN D 672 11.337 32.149 12.065 1.00 20.58 C ATOM 3618 CG ASN D 672 11.329 30.833 12.837 1.00 21.92 C ATOM 3619 OD1 ASN D 672 12.025 29.886 12.480 1.00 19.61 O ATOM 3620 ND2 ASN D 672 10.534 30.776 13.908 1.00 17.38 N ATOM 3621 N TYR D 673 12.432 34.456 10.145 1.00 21.48 N ATOM 3622 CA TYR D 673 12.149 35.619 9.304 1.00 21.97 C ATOM 3623 C TYR D 673 12.655 35.459 7.864 1.00 21.83 C ATOM 3624 O TYR D 673 11.902 35.648 6.903 1.00 20.20 O ATOM 3625 CB TYR D 673 12.784 36.886 9.904 1.00 23.46 C ATOM 3626 CG TYR D 673 12.445 38.150 9.131 1.00 26.59 C ATOM 3627 CD1 TYR D 673 11.410 38.985 9.543 1.00 26.58 C ATOM 3628 CD2 TYR D 673 13.081 38.442 7.920 1.00 30.47 C ATOM 3629 CE1 TYR D 673 11.005 40.066 8.768 1.00 28.11 C ATOM 3630 CE2 TYR D 673 12.679 39.522 7.134 1.00 28.23 C ATOM 3631 CZ TYR D 673 11.639 40.322 7.565 1.00 27.76 C ATOM 3632 OH TYR D 673 11.205 41.353 6.771 1.00 30.64 O ATOM 3633 N SER D 674 13.929 35.121 7.701 1.00 22.90 N ATOM 3634 CA SER D 674 14.463 34.997 6.352 1.00 25.20 C ATOM 3635 C SER D 674 13.767 33.896 5.585 1.00 24.29 C ATOM 3636 O SER D 674 13.400 34.080 4.425 1.00 25.42 O ATOM 3637 CB SER D 674 15.985 34.779 6.373 1.00 26.07 C ATOM 3638 OG SER D 674 16.352 33.749 7.265 1.00 33.54 O ATOM 3639 N ILE D 675 13.568 32.753 6.227 1.00 23.44 N ATOM 3640 CA ILE D 675 12.878 31.653 5.558 1.00 25.04 C ATOM 3641 C ILE D 675 11.495 32.101 5.075 1.00 23.96 C ATOM 3642 O ILE D 675 11.128 31.875 3.924 1.00 24.31 O ATOM 3643 CB ILE D 675 12.701 30.456 6.493 1.00 26.81 C ATOM 3644 CG1 ILE D 675 14.068 29.859 6.822 1.00 27.96 C ATOM 3645 CG2 ILE D 675 11.794 29.421 5.849 1.00 29.47 C ATOM 3646 CD1 ILE D 675 14.017 28.844 7.936 1.00 31.50 C ATOM 3647 N ILE D 676 10.738 32.749 5.949 1.00 24.69 N ATOM 3648 CA ILE D 676 9.406 33.209 5.581 1.00 26.76 C ATOM 3649 C ILE D 676 9.490 34.244 4.466 1.00 28.81 C ATOM 3650 O ILE D 676 8.621 34.297 3.595 1.00 28.83 O ATOM 3651 CB ILE D 676 8.677 33.815 6.811 1.00 26.99 C ATOM 3652 CG1 ILE D 676 8.440 32.719 7.858 1.00 22.68 C ATOM 3653 CG2 ILE D 676 7.356 34.476 6.388 1.00 23.23 C ATOM 3654 CD1 ILE D 676 7.799 33.227 9.159 1.00 17.83 C ATOM 3655 N ASP D 677 10.547 35.056 4.485 1.00 31.95 N ATOM 3656 CA ASP D 677 10.729 36.089 3.468 1.00 32.21 C ATOM 3657 C ASP D 677 10.961 35.454 2.095 1.00 32.22 C ATOM 3658 O ASP D 677 10.474 35.965 1.092 1.00 29.94 O ATOM 3659 CB ASP D 677 11.909 37.006 3.826 1.00 34.63 C ATOM 3660 CG ASP D 677 11.887 38.319 3.049 1.00 33.89 C ATOM 3661 OD1 ASP D 677 12.959 38.922 2.860 1.00 36.85 O ATOM 3662 OD2 ASP D 677 10.795 38.759 2.634 1.00 36.66 O ATOM 3663 N LYS D 678 11.711 34.352 2.051 1.00 33.09 N ATOM 3664 CA LYS D 678 11.957 33.651 0.790 1.00 36.81 C ATOM 3665 C LYS D 678 10.578 33.231 0.270 1.00 36.33 C ATOM 3666 O LYS D 678 10.234 33.482 −0.874 1.00 39.07 O ATOM 3667 CB LYS D 678 12.785 32.371 0.993 1.00 36.47 C ATOM 3668 CG LYS D 678 13.982 32.472 1.912 1.00 43.59 C ATOM 3669 CD LYS D 678 15.174 33.140 1.250 1.00 45.20 C ATOM 3670 CE LYS D 678 16.381 33.135 2.182 1.00 46.75 C ATOM 3671 NZ LYS D 678 17.522 33.918 1.623 1.00 48.88 N ATOM 3672 N LEU D 679 9.800 32.579 1.124 1.00 36.79 N ATOM 3673 CA LEU D 679 8.462 32.130 0.756 1.00 37.88 C ATOM 3674 C LEU D 679 7.656 33.264 0.145 1.00 37.94 C ATOM 3675 O LEU D 679 7.076 33.116 −0.919 1.00 37.41 O ATOM 3676 CB LEU D 679 7.731 31.587 1.981 1.00 36.90 C ATOM 3677 CG LEU D 679 7.811 30.078 2.212 1.00 40.44 C ATOM 3678 CD1 LEU D 679 9.228 29.591 1.984 1.00 38.86 C ATOM 3679 CD2 LEU D 679 7.322 29.751 3.619 1.00 38.47 C ATOM 3680 N VAL D 680 7.607 34.398 0.827 1.00 38.68 N ATOM 3681 CA VAL D 680 6.869 35.524 0.293 1.00 40.58 C ATOM 3682 C VAL D 680 7.385 35.883 −1.101 1.00 42.70 C ATOM 3683 O VAL D 680 6.610 36.250 −1.977 1.00 40.04 O ATOM 3684 CB VAL D 680 6.991 36.752 1.197 1.00 41.30 C ATOM 3685 CG1 VAL D 680 6.397 37.959 0.498 1.00 38.50 C ATOM 3686 CG2 VAL D 680 6.278 36.489 2.535 1.00 40.52 C ATOM 3687 N ASN D 681 8.694 35.767 −1.308 1.00 44.70 N ATOM 3688 CA ASN D 681 9.268 36.092 −2.605 1.00 47.19 C ATOM 3689 C ASN D 681 8.870 35.115 −3.699 1.00 49.09 C ATOM 3690 O ASN D 681 8.402 35.526 −4.758 1.00 49.55 O ATOM 3691 CB ASN D 681 10.793 36.183 −2.517 1.00 46.42 C ATOM 3692 CG ASN D 681 11.255 37.431 −1.788 1.00 47.04 C ATOM 3693 OD1 ASN D 681 10.559 38.447 −1.786 1.00 46.74 O ATOM 3694 ND2 ASN D 681 12.438 37.369 −1.179 1.00 47.65 N ATOM 3695 N ILE D 682 9.034 33.823 −3.443 1.00 52.35 N ATOM 3696 CA ILE D 682 8.689 32.820 −4.444 1.00 56.10 C ATOM 3697 C ILE D 682 7.199 32.786 −4.778 1.00 58.45 C ATOM 3698 O ILE D 682 6.812 32.342 −5.860 1.00 60.06 O ATOM 3699 CB ILE D 682 9.155 31.390 −4.017 1.00 55.79 C ATOM 3700 CG1 ILE D 682 7.956 30.505 −3.664 1.00 56.27 C ATOM 3701 CG2 ILE D 682 10.125 31.480 −2.854 1.00 55.49 C ATOM 3702 CD1 ILE D 682 7.271 30.852 −2.363 1.00 57.94 C ATOM 3703 N VAL D 683 6.367 33.260 −3.858 1.00 60.52 N ATOM 3704 CA VAL D 683 4.925 33.257 −4.074 1.00 63.15 C ATOM 3705 C VAL D 683 4.446 34.534 −4.752 1.00 65.06 C ATOM 3706 O VAL D 683 3.555 34.497 −5.596 1.00 65.30 O ATOM 3707 CB VAL D 683 4.161 33.064 −2.740 1.00 63.35 C ATOM 3708 CG1 VAL D 683 4.430 34.228 −1.804 1.00 64.93 C ATOM 3709 CG2 VAL D 683 2.676 32.928 −3.005 1.00 63.39 C ATOM 3710 N ASP D 684 5.038 35.664 −4.384 1.00 67.27 N ATOM 3711 CA ASP D 684 4.660 36.934 −4.986 1.00 69.50 C ATOM 3712 C ASP D 684 4.993 36.934 −6.472 1.00 71.59 C ATOM 3713 O ASP D 684 4.454 37.735 −7.237 1.00 71.99 O ATOM 3714 CB ASP D 684 5.367 38.091 −4.276 1.00 68.58 C ATOM 3715 CG ASP D 684 4.664 38.495 −2.991 1.00 69.72 C ATOM 3716 OD1 ASP D 684 4.179 37.594 −2.273 1.00 70.09 O ATOM 3717 OD2 ASP D 684 4.599 39.708 −2.692 1.00 69.37 O ATOM 3718 N ASP D 685 5.880 36.032 −6.880 1.00 73.80 N ATOM 3719 CA ASP D 685 6.251 35.929 −8.285 1.00 75.57 C ATOM 3720 C ASP D 685 5.175 35.127 −9.001 1.00 76.68 C ATOM 3721 O ASP D 685 4.844 35.398 −10.156 1.00 77.13 O ATOM 3722 CB ASP D 685 7.608 35.243 −8.442 1.00 75.95 C ATOM 3723 CG ASP D 685 8.738 36.038 −7.821 1.00 77.23 C ATOM 3724 OD1 ASP D 685 8.823 37.260 −8.075 1.00 76.55 O ATOM 3725 OD2 ASP D 685 9.548 35.439 −7.084 1.00 78.99 O ATOM 3726 N LEU D 686 4.628 34.134 −8.311 1.00 77.72 N ATOM 3727 CA LEU D 686 3.570 33.321 −8.892 1.00 79.71 C ATOM 3728 C LEU D 686 2.360 34.228 −9.082 1.00 80.70 C ATOM 3729 O LEU D 686 1.616 34.099 −10.053 1.00 80.11 O ATOM 3730 CB LEU D 686 3.215 32.163 −7.959 1.00 79.55 C ATOM 3731 CG LEU D 686 4.346 31.181 −7.646 1.00 80.42 C ATOM 3732 CD1 LEU D 686 3.840 30.122 −6.676 1.00 80.91 C ATOM 3733 CD2 LEU D 686 4.849 30.537 −8.929 1.00 79.73 C ATOM 3734 N VAL D 687 2.182 35.151 −8.142 1.00 82.79 N ATOM 3735 CA VAL D 687 1.080 36.103 −8.185 1.00 85.25 C ATOM 3736 C VAL D 687 1.232 36.965 −9.433 1.00 86.98 C ATOM 3737 O VAL D 687 0.248 37.366 −10.053 1.00 87.41 O ATOM 3738 CB VAL D 687 1.088 37.025 −6.943 1.00 85.38 C ATOM 3739 CG1 VAL D 687 −0.095 37.983 −6.993 1.00 85.62 C ATOM 3740 CG2 VAL D 687 1.049 36.191 −5.673 1.00 84.82 C ATOM 3741 N GLU D 688 2.480 37.242 −9.792 1.00 89.00 N ATOM 3742 CA GLU D 688 2.786 38.048 −10.964 1.00 91.27 C ATOM 3743 C GLU D 688 2.228 37.366 −12.213 1.00 92.66 C ATOM 3744 O GLU D 688 1.660 38.020 −13.092 1.00 92.59 O ATOM 3745 CB GLU D 688 4.305 38.227 −11.075 1.00 91.61 C ATOM 3746 CG GLU D 688 4.768 39.112 −12.217 1.00 92.97 C ATOM 3747 CD GLU D 688 6.227 39.507 −12.081 1.00 93.95 C ATOM 3748 OE1 GLU D 688 7.074 38.610 −11.886 1.00 94.46 O ATOM 3749 OE2 GLU D 688 6.529 40.716 −12.171 1.00 94.79 O ATOM 3750 N CYS D 689 2.381 36.046 −12.277 1.00 94.04 N ATOM 3751 CA CYS D 689 1.887 35.268 −13.408 1.00 95.48 C ATOM 3752 C CYS D 689 0.356 35.271 −13.421 1.00 96.12 C ATOM 3753 O CYS D 689 −0.268 34.972 −14.442 1.00 96.57 O ATOM 3754 CB CYS D 689 2.409 33.829 −13.321 1.00 95.86 C ATOM 3755 SG CYS D 689 2.002 32.775 −14.743 1.00 96.55 S ATOM 3756 N VAL D 690 −0.242 35.613 −12.282 1.00 96.33 N ATOM 3757 CA VAL D 690 −1.697 35.661 −12.154 1.00 96.28 C ATOM 3758 C VAL D 690 −2.238 37.003 −12.642 1.00 95.97 C ATOM 3759 O VAL D 690 −3.206 37.050 −13.402 1.00 95.87 O ATOM 3760 CB VAL D 690 −2.134 35.450 −10.688 1.00 96.58 C ATOM 3761 CG1 VAL D 690 −3.649 35.491 −10.586 1.00 96.64 C ATOM 3762 CG2 VAL D 690 −1.604 34.123 −10.174 1.00 96.70 C ATOM 3763 N LYS D 691 −1.615 38.089 −12.192 1.00 95.50 N ATOM 3764 CA LYS D 691 −2.017 39.432 −12.601 1.00 95.00 C ATOM 3765 C LYS D 691 −1.937 39.497 −14.123 1.00 94.21 C ATOM 3766 O LYS D 691 −2.702 40.207 −14.777 1.00 94.03 O ATOM 3767 CB LYS D 691 −1.075 40.469 −11.982 1.00 95.64 C ATOM 3768 CG LYS D 691 −1.254 41.892 −12.501 1.00 96.98 C ATOM 3769 CD LYS D 691 −2.627 42.458 −12.175 1.00 97.92 C ATOM 3770 CE LYS D 691 −2.757 43.889 −12.679 1.00 98.61 C ATOM 3771 NZ LYS D 691 −4.089 44.483 −12.373 1.00 99.33 N ATOM 3772 N GLU D 692 −0.996 38.731 −14.667 1.00 93.18 N ATOM 3773 CA GLU D 692 −0.762 38.642 −16.103 1.00 91.81 C ATOM 3774 C GLU D 692 −1.879 37.862 −16.791 1.00 91.95 C ATOM 3775 O GLU D 692 −2.336 38.229 −17.876 1.00 91.71 O ATOM 3776 CB GLU D 692 0.576 37.944 −16.347 1.00 90.32 C ATOM 3777 CG GLU D 692 0.773 37.422 −17.752 1.00 88.30 C ATOM 3778 CD GLU D 692 2.032 36.591 −17.881 1.00 87.50 C ATOM 3779 OE1 GLU D 692 3.132 37.138 −17.656 1.00 86.63 O ATOM 3780 OE2 GLU D 692 1.923 35.390 −18.203 1.00 87.16 O ATOM 3781 N ASN D 693 −2.312 36.783 −16.146 1.00 92.11 N ATOM 3782 CA ASN D 693 −3.365 35.924 −16.676 1.00 92.10 C ATOM 3783 C ASN D 693 −4.707 36.645 −16.786 1.00 92.44 C ATOM 3784 O ASN D 693 −5.733 36.024 −17.068 1.00 92.48 O ATOM 3785 CB ASN D 693 −3.519 34.688 −15.787 1.00 91.67 C ATOM 3786 CG ASN D 693 −4.404 33.629 −16.411 1.00 91.37 C ATOM 3787 OD1 ASN D 693 −4.050 33.029 −17.427 1.00 91.61 O ATOM 3788 ND2 ASN D 693 −5.565 33.397 −15.808 1.00 90.95 N ATOM 3789 N SER D 694 −4.701 37.955 −16.559 1.00 92.92 N ATOM 3790 CA SER D 694 −5.927 38.740 −16.653 1.00 93.70 C ATOM 3791 C SER D 694 −6.313 38.895 −18.123 1.00 94.44 C ATOM 3792 O SER D 694 −7.191 39.689 −18.464 1.00 94.58 O ATOM 3793 CB SER D 694 −5.726 40.122 −16.021 1.00 93.44 C ATOM 3794 OG SER D 694 −4.747 40.873 −16.720 1.00 92.64 O ATOM 3795 N SER D 695 −5.649 38.125 −18.984 1.00 95.04 N ATOM 3796 CA SER D 695 −5.895 38.169 −20.423 1.00 95.13 C ATOM 3797 C SER D 695 −6.702 36.972 −20.935 1.00 95.56 C ATOM 3798 O SER D 695 −6.197 35.848 −20.998 1.00 95.95 O ATOM 3799 CB SER D 695 −4.562 38.258 −21.180 1.00 94.47 C ATOM 3800 OG SER D 695 −3.711 37.166 −20.871 1.00 93.11 O ATOM 3801 N LYS D 696 −7.957 37.236 −21.297 1.00 95.46 N ATOM 3802 CA LYS D 696 −8.879 36.227 −21.824 1.00 94.89 C ATOM 3803 C LYS D 696 −8.843 34.878 −21.101 1.00 94.36 C ATOM 3804 O LYS D 696 −9.328 33.871 −21.625 1.00 93.84 O ATOM 3805 CB LYS D 696 −8.622 36.025 −23.319 1.00 94.98 C ATOM 3806 N ASP D 697 −8.277 34.859 −19.898 1.00 93.56 N ATOM 3807 CA ASP D 697 −8.186 33.630 −19.118 1.00 92.68 C ATOM 3808 C ASP D 697 −8.977 33.819 −17.827 1.00 91.92 C ATOM 3809 O ASP D 697 −8.590 34.609 −16.965 1.00 91.14 O ATOM 3810 CB ASP D 697 −6.717 33.320 −18.800 1.00 93.02 C ATOM 3811 CG ASP D 697 −6.447 31.827 −18.644 1.00 93.69 C ATOM 3812 OD1 ASP D 697 −7.092 31.181 −17.789 1.00 93.85 O ATOM 3813 OD2 ASP D 697 −5.580 31.299 −19.378 1.00 93.74 O ATOM 3814 N LEU D 698 −10.087 33.098 −17.700 1.00 91.37 N ATOM 3815 CA LEU D 698 −10.930 33.205 −16.514 1.00 91.28 C ATOM 3816 C LEU D 698 −10.404 32.357 −15.357 1.00 92.32 C ATOM 3817 O LEU D 698 −9.417 31.633 −15.497 1.00 91.67 O ATOM 3818 CB LEU D 698 −12.371 32.795 −16.848 1.00 89.61 C ATOM 3819 CG LEU D 698 −13.450 33.088 −15.795 1.00 88.07 C ATOM 3820 CD1 LEU D 698 −13.535 34.588 −15.547 1.00 86.94 C ATOM 3821 CD2 LEU D 698 −14.792 32.557 −16.267 1.00 86.97 C ATOM 3822 N LYS D 699 −11.075 32.465 −14.213 1.00 94.08 N ATOM 3823 CA LYS D 699 −10.717 31.732 −13.002 1.00 95.68 C ATOM 3824 C LYS D 699 −11.705 32.139 −11.917 1.00 96.86 C ATOM 3825 O LYS D 699 −11.381 32.941 −11.038 1.00 97.13 O ATOM 3826 CB LYS D 699 −9.291 32.078 −12.573 1.00 95.48 C ATOM 3827 N LYS D 700 −12.913 31.586 −11.986 1.00 98.29 N ATOM 3828 CA LYS D 700 −13.960 31.911 −11.023 1.00 99.67 C ATOM 3829 C LYS D 700 −14.250 30.798 −10.021 1.00 100.65 C ATOM 3830 O LYS D 700 −14.552 29.664 −10.401 1.00 101.39 O ATOM 3831 CB LYS D 700 −15.241 32.286 −11.761 1.00 99.60 C ATOM 3832 N SER D 701 −14.161 31.148 −8.739 1.00 100.84 N ATOM 3833 CA SER D 701 −14.412 30.230 −7.630 1.00 100.59 C ATOM 3834 C SER D 701 −13.874 30.848 −6.348 1.00 100.43 C ATOM 3835 O SER D 701 −13.041 30.254 −5.663 1.00 100.66 O ATOM 3836 CB SER D 701 −13.737 28.894 −7.879 1.00 100.76 C ATOM 3837 N PHE D 702 −14.351 32.048 −6.030 1.00 99.83 N ATOM 3838 CA PHE D 702 −13.910 32.748 −4.830 1.00 98.88 C ATOM 3839 C PHE D 702 −14.937 33.780 −4.372 1.00 97.79 C ATOM 3840 O PHE D 702 −14.829 34.964 −4.697 1.00 97.98 O ATOM 3841 CB PHE D 702 −12.566 33.429 −5.089 1.00 98.81 C ATOM 3842 N LYS D 703 −15.935 33.323 −3.620 1.00 95.97 N ATOM 3843 CA LYS D 703 −16.972 34.214 −3.111 1.00 93.51 C ATOM 3844 C LYS D 703 −16.330 35.178 −2.122 1.00 91.41 C ATOM 3845 O LYS D 703 −15.883 36.264 −2.493 1.00 91.96 O ATOM 3846 CB LYS D 703 −18.071 33.406 −2.426 1.00 93.25 C ATOM 3847 N SER D 704 −16.287 34.767 −0.861 1.00 88.69 N ATOM 3848 CA SER D 704 −15.684 35.562 0.201 1.00 85.20 C ATOM 3849 C SER D 704 −14.912 34.587 1.077 1.00 82.83 C ATOM 3850 O SER D 704 −15.429 34.111 2.089 1.00 83.42 O ATOM 3851 CB SER D 704 −16.763 36.259 1.035 1.00 84.52 C ATOM 3852 OG SER D 704 −17.574 37.096 0.234 1.00 82.90 O ATOM 3853 N PRO D 705 −13.668 34.259 0.688 1.00 79.97 N ATOM 3854 CA PRO D 705 −12.863 33.325 1.476 1.00 76.91 C ATOM 3855 C PRO D 705 −12.953 33.616 2.972 1.00 74.02 C ATOM 3856 O PRO D 705 −12.356 34.567 3.467 1.00 74.68 O ATOM 3857 CB PRO D 705 −11.460 33.535 0.916 1.00 76.37 C ATOM 3858 CG PRO D 705 −11.733 33.807 −0.522 1.00 77.44 C ATOM 3859 CD PRO D 705 −12.896 34.776 −0.457 1.00 78.70 C ATOM 3860 N GLU D 706 −13.720 32.797 3.683 1.00 71.23 N ATOM 3861 CA GLU D 706 −13.886 32.963 5.121 1.00 67.86 C ATOM 3862 C GLU D 706 −12.562 32.719 5.851 1.00 63.69 C ATOM 3863 O GLU D 706 −11.985 31.632 5.768 1.00 62.35 O ATOM 3864 CB GLU D 706 −14.953 31.987 5.645 1.00 70.07 C ATOM 3865 CG GLU D 706 −15.132 31.997 7.167 1.00 72.39 C ATOM 3866 CD GLU D 706 −16.106 30.933 7.670 1.00 75.20 C ATOM 3867 OE1 GLU D 706 −17.334 31.081 7.449 1.00 75.30 O ATOM 3868 OE2 GLU D 706 −15.638 29.945 8.287 1.00 74.89 O ATOM 3869 N PRO D 707 −12.060 33.735 6.572 1.00 59.49 N ATOM 3870 CA PRO D 707 −10.800 33.583 7.308 1.00 56.04 C ATOM 3871 C PRO D 707 −10.896 32.465 8.339 1.00 51.97 C ATOM 3872 O PRO D 707 −11.812 32.437 9.158 1.00 50.54 O ATOM 3873 CB PRO D 707 −10.599 34.958 7.949 1.00 56.55 C ATOM 3874 CG PRO D 707 −11.999 35.492 8.074 1.00 57.25 C ATOM 3875 CD PRO D 707 −12.619 35.084 6.762 1.00 58.60 C ATOM 3876 N ARG D 708 −9.948 31.540 8.277 1.00 48.78 N ATOM 3877 CA ARG D 708 −9.907 30.406 9.183 1.00 46.21 C ATOM 3878 C ARG D 708 −8.555 30.341 9.879 1.00 43.96 C ATOM 3879 O ARG D 708 −7.595 30.996 9.466 1.00 42.60 O ATOM 3880 CB ARG D 708 −10.154 29.109 8.407 1.00 48.71 C ATOM 3881 CG ARG D 708 −11.570 28.961 7.884 1.00 52.85 C ATOM 3882 CD ARG D 708 −11.704 27.807 6.891 1.00 56.82 C ATOM 3883 NE ARG D 708 −11.230 26.528 7.420 1.00 59.99 N ATOM 3884 CZ ARG D 708 −11.349 25.365 6.782 1.00 61.51 C ATOM 3885 NH1 ARG D 708 −11.933 25.317 5.590 1.00 63.09 N ATOM 3886 NH2 ARG D 708 −10.867 24.251 7.322 1.00 61.87 N ATOM 3887 N LEU D 709 −8.485 29.556 10.946 1.00 41.48 N ATOM 3888 CA LEU D 709 −7.247 29.412 11.688 1.00 39.42 C ATOM 3889 C LEU D 709 −6.624 28.053 11.395 1.00 36.66 C ATOM 3890 O LEU D 709 −7.319 27.038 11.339 1.00 35.31 O ATOM 3891 CB LEU D 709 −7.502 29.582 13.188 1.00 38.48 C ATOM 3892 CG LEU D 709 −7.990 30.975 13.600 1.00 39.85 C ATOM 3893 CD1 LEU D 709 −8.041 31.071 15.111 1.00 39.71 C ATOM 3894 CD2 LEU D 709 −7.064 32.045 13.049 1.00 39.94 C ATOM 3895 N PHE D 710 −5.310 28.047 11.194 1.00 33.55 N ATOM 3896 CA PHE D 710 −4.590 26.816 10.896 1.00 31.41 C ATOM 3897 C PHE D 710 −3.347 26.700 11.758 1.00 29.90 C ATOM 3898 O PHE D 710 −2.717 27.710 12.080 1.00 27.69 O ATOM 3899 CB PHE D 710 −4.174 26.784 9.419 1.00 31.40 C ATOM 3900 CG PHE D 710 −5.334 26.816 8.450 1.00 34.01 C ATOM 3901 CD1 PHE D 710 −6.004 28.010 8.173 1.00 34.43 C ATOM 3902 CD2 PHE D 710 −5.771 25.649 7.831 1.00 33.62 C ATOM 3903 CE1 PHE D 710 −7.092 28.042 7.297 1.00 31.45 C ATOM 3904 CE2 PHE D 710 −6.861 25.672 6.951 1.00 34.68 C ATOM 3905 CZ PHE D 710 −7.520 26.876 6.687 1.00 33.49 C ATOM 3906 N THR D 711 −3.002 25.478 12.160 1.00 29.11 N ATOM 3907 CA THR D 711 −1.778 25.303 12.932 1.00 27.42 C ATOM 3908 C THR D 711 −0.691 25.389 11.860 1.00 26.26 C ATOM 3909 O THR D 711 −0.999 25.330 10.667 1.00 25.34 O ATOM 3910 CB THR D 711 −1.713 23.934 13.642 1.00 26.97 C ATOM 3911 OG1 THR D 711 −1.979 22.894 12.704 1.00 24.41 O ATOM 3912 CG2 THR D 711 −2.716 23.871 14.776 1.00 25.72 C ATOM 3913 N PRO D 712 0.581 25.565 12.255 1.00 26.02 N ATOM 3914 CA PRO D 712 1.616 25.649 11.215 1.00 26.21 C ATOM 3915 C PRO D 712 1.557 24.444 10.281 1.00 28.47 C ATOM 3916 O PRO D 712 1.554 24.586 9.047 1.00 25.16 O ATOM 3917 CB PRO D 712 2.902 25.718 12.026 1.00 22.24 C ATOM 3918 CG PRO D 712 2.469 26.544 13.205 1.00 23.05 C ATOM 3919 CD PRO D 712 1.134 25.912 13.576 1.00 23.09 C ATOM 3920 N GLU D 713 1.490 23.266 10.891 1.00 29.14 N ATOM 3921 CA GLU D 713 1.407 22.007 10.164 1.00 32.67 C ATOM 3922 C GLU D 713 0.417 22.064 8.999 1.00 31.32 C ATOM 3923 O GLU D 713 0.785 21.884 7.842 1.00 32.51 O ATOM 3924 CB GLU D 713 0.971 20.889 11.118 1.00 34.67 C ATOM 3925 CG GLU D 713 1.911 19.705 11.123 1.00 41.80 C ATOM 3926 CD GLU D 713 1.433 18.571 12.007 1.00 40.60 C ATOM 3927 OE1 GLU D 713 2.151 17.559 12.077 1.00 45.79 O ATOM 3928 OE2 GLU D 713 0.352 18.682 12.621 1.00 39.13 O ATOM 3929 N GLU D 714 −0.844 22.328 9.307 1.00 30.43 N ATOM 3930 CA GLU D 714 −1.849 22.344 8.264 1.00 30.71 C ATOM 3931 C GLU D 714 −1.754 23.559 7.339 1.00 28.77 C ATOM 3932 O GLU D 714 −2.101 23.480 6.155 1.00 28.54 O ATOM 3933 CB GLU D 714 −3.247 22.191 8.900 1.00 31.99 C ATOM 3934 CG GLU D 714 −3.625 23.269 9.896 1.00 37.31 C ATOM 3935 CD GLU D 714 −4.553 22.772 11.002 1.00 39.58 C ATOM 3936 OE1 GLU D 714 −5.266 23.612 11.597 1.00 38.58 O ATOM 3937 OE2 GLU D 714 −4.555 21.552 11.290 1.00 40.23 O ATOM 3938 N PHE D 715 −1.266 24.684 7.847 1.00 27.44 N ATOM 3939 CA PHE D 715 −1.145 25.849 6.980 1.00 24.07 C ATOM 3940 C PHE D 715 −0.157 25.559 5.856 1.00 24.36 C ATOM 3941 O PHE D 715 −0.419 25.855 4.690 1.00 21.57 O ATOM 3942 CB PHE D 715 −0.649 27.075 7.746 1.00 23.21 C ATOM 3943 CG PHE D 715 −0.450 28.296 6.871 1.00 22.37 C ATOM 3944 CD1 PHE D 715 −1.496 29.183 6.640 1.00 22.39 C ATOM 3945 CD2 PHE D 715 0.778 28.546 6.272 1.00 21.02 C ATOM 3946 CE1 PHE D 715 −1.319 30.312 5.824 1.00 26.50 C ATOM 3947 CE2 PHE D 715 0.970 29.666 5.452 1.00 22.98 C ATOM 3948 CZ PHE D 715 −0.082 30.555 5.229 1.00 24.25 C ATOM 3949 N PHE D 716 0.987 24.981 6.203 1.00 25.04 N ATOM 3950 CA PHE D 716 1.989 24.714 5.184 1.00 28.02 C ATOM 3951 C PHE D 716 1.745 23.514 4.276 1.00 29.77 C ATOM 3952 O PHE D 716 2.322 23.426 3.192 1.00 30.86 O ATOM 3953 CB PHE D 716 3.379 24.673 5.817 1.00 20.28 C ATOM 3954 CG PHE D 716 3.882 26.036 6.199 1.00 21.93 C ATOM 3955 CD1 PHE D 716 3.804 26.482 7.515 1.00 19.71 C ATOM 3956 CD2 PHE D 716 4.351 26.913 5.217 1.00 19.54 C ATOM 3957 CE1 PHE D 716 4.174 27.769 7.850 1.00 19.20 C ATOM 3958 CE2 PHE D 716 4.725 28.208 5.536 1.00 19.96 C ATOM 3959 CZ PHE D 716 4.638 28.644 6.857 1.00 20.24 C ATOM 3960 N ARG D 717 0.879 22.603 4.689 1.00 32.19 N ATOM 3961 CA ARG D 717 0.581 21.475 3.821 1.00 36.18 C ATOM 3962 C ARG D 717 −0.269 22.103 2.716 1.00 35.80 C ATOM 3963 O ARG D 717 −0.186 21.727 1.545 1.00 35.14 O ATOM 3964 CB ARG D 717 −0.209 20.400 4.570 1.00 39.40 C ATOM 3965 CG ARG D 717 −0.437 19.144 3.743 1.00 42.14 C ATOM 3966 CD ARG D 717 −1.206 18.102 4.518 1.00 43.31 C ATOM 3967 NE ARG D 717 −2.413 18.664 5.117 1.00 48.20 N ATOM 3968 CZ ARG D 717 −3.359 17.940 5.714 1.00 50.40 C ATOM 3969 NH1 ARG D 717 −3.240 16.618 5.787 1.00 48.68 N ATOM 3970 NH2 ARG D 717 −4.415 18.536 6.251 1.00 51.09 N ATOM 3971 N ILE D 718 −1.074 23.086 3.110 1.00 36.09 N ATOM 3972 CA ILE D 718 −1.919 23.817 2.175 1.00 33.20 C ATOM 3973 C ILE D 718 −1.019 24.658 1.290 1.00 32.86 C ATOM 3974 O ILE D 718 −1.242 24.769 0.085 1.00 32.44 O ATOM 3975 CB ILE D 718 −2.893 24.749 2.913 1.00 32.66 C ATOM 3976 CG1 ILE D 718 −3.916 23.917 3.686 1.00 32.71 C ATOM 3977 CG2 ILE D 718 −3.596 25.668 1.924 1.00 31.11 C ATOM 3978 CD1 ILE D 718 −4.837 24.749 4.545 1.00 30.41 C ATOM 3979 N PHE D 719 −0.003 25.265 1.895 1.00 34.20 N ATOM 3980 CA PHE D 719 0.935 26.083 1.138 1.00 34.51 C ATOM 3981 C PHE D 719 1.675 25.248 0.093 1.00 36.52 C ATOM 3982 O PHE D 719 1.831 25.669 −1.050 1.00 36.77 O ATOM 3983 CB PHE D 719 1.965 26.715 2.057 1.00 32.83 C ATOM 3984 CG PHE D 719 3.112 27.338 1.321 1.00 32.14 C ATOM 3985 CD1 PHE D 719 2.998 28.614 0.783 1.00 32.64 C ATOM 3986 CD2 PHE D 719 4.303 26.640 1.150 1.00 29.99 C ATOM 3987 CE1 PHE D 719 4.060 29.193 0.085 1.00 31.46 C ATOM 3988 CE2 PHE D 719 5.363 27.201 0.459 1.00 32.01 C ATOM 3989 CZ PHE D 719 5.243 28.486 −0.076 1.00 31.65 C ATOM 3990 N ASN D 720 2.148 24.075 0.501 1.00 38.51 N ATOM 3991 CA ASN D 720 2.871 23.185 −0.402 1.00 40.99 C ATOM 3992 C ASN D 720 1.975 22.710 −1.540 1.00 42.05 C ATOM 3993 O ASN D 720 2.318 22.856 −2.715 1.00 38.56 O ATOM 3994 CB ASN D 720 3.406 21.975 0.365 1.00 41.82 C ATOM 3995 CG ASN D 720 4.676 22.282 1.128 1.00 43.96 C ATOM 3996 OD1 ASN D 720 5.114 21.492 1.962 1.00 47.53 O ATOM 3997 ND2 ASN D 720 5.283 23.423 0.838 1.00 45.70 N ATOM 3998 N ARG D 721 0.831 22.134 −1.183 1.00 44.34 N ATOM 3999 CA ARG D 721 −0.119 21.655 −2.174 1.00 48.41 C ATOM 4000 C ARG D 721 −0.392 22.795 −3.147 1.00 50.49 C ATOM 4001 O ARG D 721 −0.153 22.679 −4.349 1.00 51.59 O ATOM 4002 CB ARG D 721 −1.427 21.230 −1.494 1.00 50.30 C ATOM 4003 CG ARG D 721 −2.511 20.736 −2.446 1.00 54.70 C ATOM 4004 CD ARG D 721 −2.278 19.294 −2.895 1.00 60.17 C ATOM 4005 NE ARG D 721 −2.917 18.317 −2.009 1.00 63.19 N ATOM 4006 CZ ARG D 721 −2.833 16.996 −2.160 1.00 64.19 C ATOM 4007 NH1 ARG D 721 −2.131 16.482 −3.165 1.00 65.14 N ATOM 4008 NH2 ARG D 721 −3.457 16.185 −1.313 1.00 63.41 N ATOM 4009 N SER D 722 −0.874 23.908 −2.611 1.00 52.95 N ATOM 4010 CA SER D 722 −1.202 25.075 −3.418 1.00 55.12 C ATOM 4011 C SER D 722 −0.090 25.474 −4.380 1.00 57.42 C ATOM 4012 O SER D 722 −0.344 25.754 −5.553 1.00 57.12 O ATOM 4013 CB SER D 722 −1.546 26.256 −2.508 1.00 54.05 C ATOM 4014 OG SER D 722 −1.776 27.426 −3.268 1.00 54.05 O ATOM 4015 N ILE D 723 1.142 25.503 −3.889 1.00 60.20 N ATOM 4016 CA ILE D 723 2.266 25.876 −4.734 1.00 64.22 C ATOM 4017 C ILE D 723 2.435 24.918 −5.904 1.00 67.18 C ATOM 4018 O ILE D 723 2.520 25.350 −7.052 1.00 67.37 O ATOM 4019 CB ILE D 723 3.581 25.930 −3.933 1.00 63.96 C ATOM 4020 CG1 ILE D 723 3.561 27.136 −2.992 1.00 64.48 C ATOM 4021 CG2 ILE D 723 4.765 26.014 −4.876 1.00 63.91 C ATOM 4022 CD1 ILE D 723 3.337 28.464 −3.695 1.00 64.40 C ATOM 4023 N ASP D 724 2.476 23.621 −5.620 1.00 70.57 N ATOM 4024 CA ASP D 724 2.639 22.643 −6.685 1.00 74.58 C ATOM 4025 C ASP D 724 1.443 22.705 −7.628 1.00 76.51 C ATOM 4026 O ASP D 724 1.563 22.438 −8.823 1.00 76.39 O ATOM 4027 CB ASP D 724 2.786 21.230 −6.110 1.00 76.01 C ATOM 4028 CG ASP D 724 3.246 20.221 −7.157 1.00 78.85 C ATOM 4029 OD1 ASP D 724 2.468 19.935 −8.099 1.00 79.06 O ATOM 4030 OD2 ASP D 724 4.390 19.723 −7.044 1.00 79.21 O ATOM 4031 N ALA D 725 0.287 23.063 −7.083 1.00 79.26 N ATOM 4032 CA ALA D 725 −0.916 23.169 −7.888 1.00 82.39 C ATOM 4033 C ALA D 725 −0.727 24.306 −8.876 1.00 85.18 C ATOM 4034 O ALA D 725 −1.228 24.257 −9.996 1.00 85.62 O ATOM 4035 CB ALA D 725 −2.115 23.442 −7.005 1.00 82.12 C ATOM 4036 N PHE D 726 0.007 25.329 −8.453 1.00 88.76 N ATOM 4037 CA PHE D 726 0.258 26.479 −9.307 1.00 92.49 C ATOM 4038 C PHE D 726 1.285 26.121 −10.365 1.00 94.74 C ATOM 4039 O PHE D 726 1.358 26.761 −11.412 1.00 95.57 O ATOM 4040 CB PHE D 726 0.766 27.664 −8.488 1.00 93.45 C ATOM 4041 CG PHE D 726 0.704 28.970 −9.224 1.00 94.42 C ATOM 4042 CD1 PHE D 726 −0.505 29.643 −9.366 1.00 94.75 C ATOM 4043 CD2 PHE D 726 1.846 29.512 −9.804 1.00 94.94 C ATOM 4044 CE1 PHE D 726 −0.577 30.839 −10.076 1.00 94.86 C ATOM 4045 CE2 PHE D 726 1.785 30.708 −10.517 1.00 95.15 C ATOM 4046 CZ PHE D 726 0.571 31.372 −10.653 1.00 94.93 C ATOM 4047 N LYS D 727 2.091 25.103 −10.085 1.00 97.62 N ATOM 4048 CA LYS D 727 3.096 24.659 −11.040 1.00 100.84 C ATOM 4049 C LYS D 727 2.390 23.922 −12.169 1.00 102.89 C ATOM 4050 O LYS D 727 3.026 23.230 −12.962 1.00 103.74 O ATOM 4051 CB LYS D 727 4.102 23.715 −10.378 1.00 100.90 C ATOM 4052 CG LYS D 727 5.054 24.382 −9.402 1.00 102.65 C ATOM 4053 CD LYS D 727 6.110 23.394 −8.915 1.00 103.29 C ATOM 4054 CE LYS D 727 7.109 24.056 −7.977 1.00 103.25 C ATOM 4055 NZ LYS D 727 8.168 23.108 −7.526 1.00 103.06 N ATOM 4056 N ASP D 728 1.070 24.073 −12.229 1.00 105.08 N ATOM 4057 CA ASP D 728 0.259 23.419 −13.251 1.00 106.79 C ATOM 4058 C ASP D 728 −1.023 24.211 −13.512 1.00 107.51 C ATOM 4059 O ASP D 728 −2.032 23.640 −13.923 1.00 107.48 O ATOM 4060 CB ASP D 728 −0.113 22.002 −12.799 1.00 107.76 C ATOM 4061 CG ASP D 728 1.090 21.189 −12.353 1.00 108.44 C ATOM 4062 OD1 ASP D 728 1.982 20.930 −13.188 1.00 109.36 O ATOM 4063 OD2 ASP D 728 1.142 20.810 −11.163 1.00 108.52 O ATOM 4064 N PHE D 729 −0.983 25.518 −13.271 1.00 108.65 N ATOM 4065 CA PHE D 729 −2.156 26.365 −13.475 1.00 110.01 C ATOM 4066 C PHE D 729 −2.757 26.176 −14.865 1.00 110.93 C ATOM 4067 O PHE D 729 −3.705 25.409 −15.036 1.00 111.27 O ATOM 4068 CB PHE D 729 −1.796 27.838 −13.250 1.00 109.77 C ATOM 4069 CG PHE D 729 −2.965 28.773 −13.382 1.00 109.64 C ATOM 4070 CD1 PHE D 729 −4.185 28.470 −12.786 1.00 109.79 C ATOM 4071 CG2 PHE D 729 −2.848 29.957 −14.097 1.00 109.96 C ATOM 4072 CE1 PHE D 729 −5.273 29.332 −12.903 1.00 109.64 C ATOM 4073 CE2 PHE D 729 −3.931 30.828 −14.219 1.00 110.09 C ATOM 4074 CZ PHE D 729 −5.146 30.513 −13.621 1.00 109.50 C ATOM 4075 N VAL D 730 −2.214 26.882 −15.852 1.00 111.95 N ATOM 4076 CA VAL D 730 −2.696 26.766 −17.226 1.00 112.76 C ATOM 4077 C VAL D 730 −1.608 26.079 −18.051 1.00 113.09 C ATOM 4078 O VAL D 730 −1.622 26.110 −19.281 1.00 113.21 O ATOM 4079 CB VAL D 730 −3.017 28.158 −17.838 1.00 113.05 C ATOM 4080 CG1 VAL D 730 −3.632 28.001 −19.222 1.00 113.29 C ATOM 4081 CG2 VAL D 730 −3.979 28.911 −16.939 1.00 112.88 C ATOM 4082 N VAL D 731 −0.664 25.454 −17.352 1.00 113.55 N ATOM 4083 CA VAL D 731 0.442 24.749 −17.992 1.00 113.65 C ATOM 4084 C VAL D 731 0.119 23.263 −18.121 1.00 113.98 C ATOM 4085 O VAL D 731 0.510 22.614 −19.090 1.00 114.23 O ATOM 4086 CB VAL D 731 1.750 24.907 −17.178 1.00 113.39 C ATOM 4087 CG1 VAL D 731 2.888 24.165 −17.864 1.00 112.68 C ATOM 4088 CG2 VAL D 731 2.092 26.380 −17.029 1.00 113.00 C ATOM 4089 N ALA D 732 −8.151 23.191 −20.446 1.00 112.99 N ATOM 4090 CA ALA D 732 −8.781 23.296 −19.136 1.00 112.99 C ATOM 4091 C ALA D 732 −10.158 23.942 −19.244 1.00 112.89 C ATOM 4092 O ALA D 732 −11.068 23.624 −18.476 1.00 112.43 O ATOM 4093 CB ALA D 732 −7.895 24.105 −18.199 1.00 113.07 C TER 4094 ALA D 732 HETATM 4095 SM SM C 801 3.382 22.913 33.418 1.00 1.01 SM HETATM 4096 SM SM 802 12.310 41.103 1.729 1.00 46.23 SM HETATM 4097 SM SM B 803 34.722 60.629 −13.944 1.00 31.85 SM HETATM 4098 SM SM 804 23.452 43.030 48.466 1.00 29.22 SM HETATM 4099 CA CA C 805 10.432 45.369 22.564 1.00 13.16 CA HETATM 4100 CA CA A 806 35.803 63.939 33.610 1.00 29.63 CA HETATM 4101 C TRS 807 12.090 38.542 −7.133 1.00 65.56 C HETATM 4102 C1 TRS 807 11.580 37.873 −5.842 1.00 65.64 C HETATM 4103 C2 TRS 807 12.288 37.549 −8.116 1.00 66.45 C HETATM 4104 C3 TRS 807 13.335 39.347 −6.731 1.00 65.43 C HETATM 4105 N TRS 807 11.058 39.471 −7.617 1.00 65.22 N HETATM 4106 O1 TRS 807 12.450 36.961 −5.333 1.00 66.42 O HETATM 4107 O2 TRS 807 13.351 36.656 −7.967 1.00 66.52 O HETATM 4108 O3 TRS 807 13.974 40.049 −7.756 1.00 67.00 O HETATM 4109 O HOH 811 8.606 30.195 16.587 1.00 16.28 O HETATM 4110 O HOH 812 15.796 28.952 16.244 1.00 25.74 O HETATM 4111 O HOH 813 8.996 37.339 20.117 1.00 20.66 O HETATM 4112 O HOH 814 36.198 57.554 35.884 1.00 24.36 O HETATM 4113 O HOH 815 15.748 41.466 32.458 1.00 25.24 O HETATM 4114 O HOH 816 12.670 24.054 17.321 1.00 25.31 O HETATM 4115 O HOH 817 25.605 46.320 26.127 1.00 20.83 O HETATM 4116 O HOH 818 29.793 46.559 4.826 1.00 27.80 O HETATM 4117 O HOH 820 23.636 52.838 21.810 1.00 29.62 O HETATM 4118 O HOH 821 −5.477 35.005 4.087 1.00 38.64 O HETATM 4119 O HOH 822 9.263 22.777 37.596 1.00 30.45 O HETATM 4120 O HOH 823 18.824 65.144 45.840 1.00 28.91 O HETATM 4121 O HOH 824 41.938 49.349 29.824 1.00 36.33 O HETATM 4122 O HOH 825 14.204 35.302 12.661 1.00 26.09 O HETATM 4123 O HOH 826 5.154 28.366 35.565 1.00 27.41 O HETATM 4124 O HOH 827 17.420 47.026 21.845 1.00 27.81 O HETATM 4125 O HOH 828 29.550 40.761 7.680 1.00 35.99 O HETATM 4126 O HOH 829 28.265 45.994 11.706 1.00 32.91 O HETATM 4127 O HOH 830 12.962 31.889 47.898 1.00 42.72 O HETATM 4128 O HOH 831 16.808 31.403 5.277 1.00 43.76 O HETATM 4129 O HOH 832 32.631 57.885 29.873 1.00 37.74 O HETATM 4130 O HOH 833 2.250 27.901 24.836 1.00 43.13 O HETATM 4131 O HOH 834 29.990 44.971 9.328 1.00 31.81 O HETATM 4132 O HOH 835 −1.600 20.408 13.679 1.00 43.79 O HETATM 4133 O HOH 836 11.220 47.746 7.580 1.00 30.14 O HETATM 4134 O HOH 837 20.724 44.044 29.836 1.00 30.56 O HETATM 4135 O HOH 838 2.173 22.432 13.281 1.00 22.54 O HETATM 4136 O HOH 839 17.557 36.992 9.840 1.00 31.87 O HETATM 4137 O HOH 840 4.550 23.994 14.170 1.00 27.46 O HETATM 4138 O HOH 841 25.281 39.695 6.782 1.00 41.84 O HETATM 4139 O HOH 842 9.383 42.930 6.783 1.00 47.18 O HETATM 4140 O HOH 843 6.361 42.296 24.220 1.00 37.78 O HETATM 4141 O HOH 844 39.382 57.416 48.330 1.00 48.52 O HETATM 4142 O HOH 845 32.247 41.153 5.687 1.00 41.83 O HETATM 4143 O HOH 846 26.125 49.499 −8.757 1.00 30.11 O HETATM 4144 O HOH 847 0.290 30.022 23.939 1.00 50.00 O HETATM 4145 O HOH 848 8.376 42.541 9.479 1.00 43.80 O HETATM 4146 O HOH 849 19.958 38.970 5.910 1.00 46.78 O HETATM 4147 O HOH 850 22.162 39.657 21.182 1.00 33.34 O HETATM 4148 O HOH 851 8.230 39.327 21.959 1.00 33.00 O HETATM 4149 O HOH 852 23.921 60.495 19.790 1.00 35.77 O HETATM 4150 O HOH 853 6.817 22.716 16.090 1.00 27.55 O HETATM 4151 O HOH 854 34.018 56.401 28.113 1.00 34.61 O HETATM 4152 O HOH 856 27.581 39.513 34.077 1.00 42.95 O HETATM 4153 O HOH 857 −0.751 35.172 8.963 1.00 32.87 O HETATM 4154 O HOH 859 32.429 60.073 −13.200 1.00 23.38 O HETATM 4155 O HOH 860 −7.012 24.072 13.604 1.00 34.71 O HETATM 4156 O HOH 861 39.074 63.063 33.662 1.00 58.21 O HETATM 4157 O HOH 862 21.440 42.915 27.714 1.00 22.95 O HETATM 4158 O HOH 864 37.581 61.643 36.898 1.00 39.63 O HETATM 4159 O HOH 865 0.685 21.698 15.184 1.00 28.66 O HETATM 4160 O HOH 866 22.254 64.084 49.555 1.00 44.64 O HETATM 4161 O HOH 867 35.264 53.161 23.559 1.00 43.70 O HETATM 4162 O HOH 868 6.596 44.632 15.034 1.00 59.30 O HETATM 4163 O HOH 869 22.825 56.530 −12.218 1.00 52.42 O HETATM 4164 O HOH 870 31.995 63.552 10.190 1.00 36.82 O HETATM 4165 O HOH 871 0.793 40.178 0.296 1.00 48.61 O HETATM 4166 O HOH 872 23.300 60.113 −7.891 1.00 49.86 O HETATM 4167 O HOH 873 11.054 40.390 18.125 1.00 48.30 O HETATM 4168 O HOH 874 13.243 21.325 37.798 1.00 32.31 O HETATM 4169 O HOH 875 −1.787 35.888 19.682 1.00 48.97 O HETATM 4170 O HOH 876 24.682 67.138 31.722 1.00 50.20 O HETATM 4171 O HOH 877 −1.307 36.711 41.965 1.00 50.56 O HETATM 4172 O HOH 878 −0.438 34.252 13.488 1.00 46.62 O HETATM 4173 O HOH 879 27.258 44.610 27.195 1.00 30.34 O HETATM 4174 O HOH 880 25.059 58.789 17.500 1.00 24.33 O HETATM 4175 O HOH 881 15.549 41.179 5.494 1.00 27.27 O HETATM 4176 O HOH 882 6.184 20.441 14.801 1.00 33.01 O HETATM 4177 O HOH 884 35.838 55.016 50.740 1.00 26.63 O HETATM 4178 O HOH 885 15.613 16.978 24.799 1.00 46.01 O HETATM 4179 O HOH 886 18.940 41.747 27.441 1.00 43.83 O HETATM 4180 O HOH 887 21.025 38.556 16.332 1.00 25.23 O HETATM 4181 O HOH 888 7.893 19.264 12.842 1.00 38.30 O HETATM 4182 O HOH 889 33.533 59.350 3.597 1.00 47.44 O HETATM 4183 O HOH 890 9.571 38.165 17.010 1.00 31.45 O HETATM 4184 O HOH 891 28.775 35.831 14.058 1.00 40.18 O HETATM 4185 O HOH 892 26.247 53.039 −17.253 1.00 46.82 O HETATM 4186 O HOH 893 32.415 61.335 17.452 1.00 38.77 O HETATM 4187 O HOH 894 23.460 45.149 24.354 1.00 26.05 O HETATM 4188 O HOH 895 3.991 24.967 37.153 1.00 42.80 O HETATM 4189 O HOH 896 19.794 41.241 31.566 1.00 50.67 O HETATM 4190 O HOH 897 19.768 25.882 9.816 1.00 44.44 O HETATM 4191 O HOH 898 27.528 39.803 14.126 1.00 40.31 O HETATM 4192 O HOH 899 15.999 61.065 33.673 1.00 40.88 O HETATM 4193 O HOH 900 15.539 19.636 28.723 1.00 47.29 O HETATM 4194 O HOH 901 38.498 54.225 8.757 1.00 30.13 O HETATM 4195 O HOH 902 32.463 48.114 54.923 1.00 38.66 O HETATM 4196 O HOH 903 −2.634 37.278 32.151 1.00 35.03 O HETATM 4197 O HOH 904 29.906 38.640 9.627 1.00 38.75 O HETATM 4198 O HOH 905 2.033 18.537 15.351 1.00 26.34 O HETATM 4199 O HOH 906 27.804 65.306 43.860 1.00 32.86 O HETATM 4200 O HOH 907 18.984 58.578 24.142 1.00 29.87 O HETATM 4201 O HOH 908 21.742 28.140 13.049 1.00 30.99 O HETATM 4202 O HOH 909 20.378 21.642 23.293 1.00 39.19 O HETATM 4203 O HOH 910 −6.019 39.244 2.216 1.00 34.77 O HETATM 4204 O HOH 911 17.624 66.255 35.268 1.00 51.56 O HETATM 4205 O HOH 912 3.763 20.127 13.752 1.00 30.70 O HETATM 4206 O HOH 913 3.362 27.348 33.755 1.00 23.36 O HETATM 4207 O HOH 914 24.559 28.693 12.265 1.00 43.09 O HETATM 4208 O HOH 915 36.824 59.818 47.570 1.00 30.39 O HETATM 4209 O HOH 916 22.924 22.342 40.503 1.00 44.39 O HETATM 4210 O HOH 917 4.702 18.252 11.499 1.00 32.74 O HETATM 4211 O HOH 918 3.467 17.089 17.532 1.00 39.40 O HETATM 4212 O HOH 919 29.413 49.496 −7.485 1.00 47.21 O HETATM 4213 O HOH 920 34.259 51.561 21.638 1.00 37.97 O HETATM 4214 O HOH 921 32.610 44.187 35.494 1.00 38.79 O HETATM 4215 O HOH 922 32.804 43.191 23.362 1.00 49.05 O HETATM 4216 O HOH 923 22.149 37.679 18.847 1.00 30.70 O HETATM 4217 O HOH 924 17.587 59.642 39.191 1.00 43.12 O HETATM 4218 O HOH 925 22.812 24.637 9.520 1.00 46.83 O HETATM 4219 O HOH 926 22.586 61.146 9.839 1.00 30.25 O HETATM 4220 O HOH 927 20.143 20.685 34.805 1.00 32.86 O HETATM 4221 O HOH 928 −0.129 30.047 26.719 1.00 41.23 O HETATM 4222 O HOH 929 18.693 64.441 43.617 1.00 26.18 O HETATM 4223 O HOH 930 3.316 26.782 31.229 1.00 30.65 O HETATM 4224 O HOH 931 8.782 41.756 37.184 1.00 38.10 O HETATM 4225 O HOH 932 26.815 65.475 31.026 1.00 37.12 O HETATM 4226 O HOH 933 8.096 48.366 22.796 1.00 45.13 O HETATM 4227 O HOH 934 4.661 27.558 28.897 1.00 33.72 O HETATM 4228 O HOH 935 40.351 55.087 47.376 1.00 47.23 O HETATM 4229 O HOH 936 7.950 32.677 47.497 1.00 39.88 O HETATM 4230 O HOH 937 12.548 44.676 21.718 1.00 34.89 O HETATM 4231 O HOH 938 −8.820 40.219 1.469 1.00 49.47 O HETATM 4232 O HOH 939 7.489 53.321 8.112 1.00 49.45 O HETATM 4233 O HOH 940 19.944 39.180 44.418 1.00 45.27 O HETATM 4234 O HOH 941 29.508 64.292 41.649 1.00 47.23 O HETATM 4235 O HOH 942 47.050 56.585 38.269 1.00 50.59 O HETATM 4236 O HOH 943 7.616 45.571 21.859 1.00 39.67 O HETATM 4237 O HOH 944 7.909 44.216 26.286 1.00 48.09 O HETATM 4238 O HOH 945 30.114 47.882 12.560 1.00 44.31 O HETATM 4239 O HOH 946 2.782 22.874 35.242 1.00 41.79 O HETATM 4240 O HOH 947 16.770 62.683 36.910 1.00 41.79 O CONECT   6  661 CONECT  300 1042 CONECT  661   6 CONECT 1042  300 CONECT 1068 1738 CONECT 1377 2103 CONECT 1738 1068 CONECT 2097 4097 CONECT 2103 1377 CONECT 2388 3114 CONECT 3114 2388 CONECT 4097 2097 CONECT 4101 4102 4103 4104 4105 CONECT 4102 4101 4106 CONECT 4103 4101 4107 CONECT 4104 4101 4108 CONECT 4105 4101 CONECT 4106 4102 CONECT 4107 4103 CONECT 4108 4104 MASTER  385   0   7  19 8 0 0 6 4236 4 20 44

TABLE 6 FGF2/FGFR1/Heparin Ternary Complex REMARK coordinates from simulated annealing refinement REMARK refinement resolution: 25.0 − 3.0 A REMARK starting r= 0.2340 free_r= 0.2850 REMARK final r=0.2310 free_r= 0.2893 REMARK rmsd bonds= 0.008843 rmsd angles= 1.48262 REMARK wa_initial= 5.38223 wa_dynamics= 5.24774 wa_final= 5.67599 REMARK target= mlf md-method= cartesian annealing schedule= slowcool REMARK starting temperature= 2500 total md steps= 100 * 50 REMARK sg= P4(1)2(1)2 a= 98.888 b= 98.888 c= 196.292 alpha= 90 beta=90 gamma= 90 REMARK parameter file 1 : CNS_TOPPAR:protein_rep.param REMARK parameter file 2 : CNS_TOPPAR:dna-rna.param REMARK parameter file 3 : CNS_TOPPAR:water_rep.param REMARK parameter file 4 : CNS_TOPPAR:ion.param REMARK parameter file 5 : hexa.param REMARK molecular structure file: deca2_8.mtf REMARK input coordinates: deca2_8XB.pdb REMARK reflection file= 23bdec2.hklt REMARK ncs= restrain ncs file= ncs.def REMARK B-correction resolution: 6.0 − 3.0 REMARK initial B-factor correction applied to fobs: REMARK B11= −10.663 B22= −10.663 B33= 21.325 REMARK B12=    0.000 B13=    0.000 B23=  0.000 REMARK B-factor correction applied to coordinate array B: 1.815 REMARK bulk solvent: density level= 0.295271 e/A{circumflex over ( )}3, B-factor= 10 A{circumflex over ( )}2 REMARK reflections with |Fobs|/sigma_F < 0.0 rejected REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected REMARK theoretical total number of refl. in resol. range: 20197 (100.0%) REMARK number of unobserved reflections (no entry or |F|=0): 1892 (9.4%) REMARX number of reflections rejected: 0 (0.0%) REMARK total number of reflections used: 18305 (90.6%) REMARK number of reflections in working set: 17419 (86.2%) REMARK number of reflections in test set: 886 (4.4%) CRYST1  98.888  98.888  196.292  90.00  90.00  90.00  P 41  21  2 REMARK FILENAME=“deca2_8XBA_1.pdb” REMARK DATE: 26-Jun-00  16:58:39     created by user: mohammad REMARK VERSION: 0.5 ATOM 1 CB HIS 16 69.300 30.458 136.592 1.00 53.12 ATOM 2 CG HIS 16 68.282 29.746 137.434 1.00 53.81 ATOM 3 CD2 HIS 16 68.024 29.802 138.763 1.00 53.82 ATOM 4 ND1 HIS 16 67.400 28.821 136.918 1.00 53.71 ATOM 5 CE1 HIS 16 66.646 28.337 137.890 1.00 52.39 ATOM 6 NE2 HIS 16 67.004 28.917 139.019 1.00 52.97 ATOM 7 C HIS 16 69.392 28.671 134.893 1.00 53.57 ATOM 8 O HIS 16 69.057 29.086 133.779 1.00 54.30 ATOM 9 N HIS 16 71.340 30.243 135.155 1.00 53.53 ATOM 10 CA HIS 16 70.228 29.513 135.838 1.00 53.43 ATOM 11 N PHE 17 69.038 27.478 135.354 1.00 53.60 ATOM 12 CA PHE 17 68.267 26.563 134.527 1.00 52.77 ATOM 13 CB PHE 17 68.347 25.142 135.112 1.00 50.35 ATOM 14 CG PHE 17 67.444 24.910 136.279 1.00 49.67 ATOM 15 CD1 PHE 17 66.154 24.417 136.087 1.00 48.74 ATOM 16 CD2 PHE 17 67.865 25.204 137.570 1.00 49.40 ATOM 17 CE1 PHE 17 65.293 24.221 137.164 1.00 47.80 ATOM 18 CE2 PHE 17 67.007 25.012 138.659 1.00 49.12 ATOM 19 CZ PHE 17 65.718 24.519 138.451 1.00 47.95 ATOM 20 C PHE 17 66.813 27.007 134.268 1.00 52.61 ATOM 21 O PHE 17 66.198 26.567 133.294 1.00 53.57 ATOM 22 N LYS 18 66.275 27.895 135.104 1.00 51.30 ATOM 23 CA LYS 18 64.909 28.375 134.913 1.00 50.46 ATOM 24 CB LYS 18 64.275 28.772 136.248 1.00 49.68 ATOM 25 C LYS 18 64.821 29.555 133.936 1.00 50.17 ATOM 26 O LYS 18 63.792 29.745 133.289 1.00 50.91 ATOM 27 N ASP 19 65.889 30.344 133.822 1.00 48.70 ATOM 28 CA ASP 19 65.888 31.486 132.910 1.00 47.03 ATOM 29 CB ASP 19 67.043 32.421 133.234 1.00 48.46 ATOM 30 CG ASP 19 67.278 32.545 134.709 1.00 50.22 ATOM 31 OD1 ASP 19 66.272 32.491 135.453 1.00 50.85 ATOM 32 OD2 ASP 19 68.455 32.701 135.120 1.00 51.12 ATOM 33 C ASP 19 66.022 31.021 131.469 1.00 45.37 ATOM 34 O ASP 19 66.485 29.913 131.210 1.00 46.46 ATOM 35 N PRO 20 65.598 31.857 130.508 1.00 43.28 ATOM 36 CD PRO 20 64.692 33.003 130.659 1.00 42.19 ATOM 37 CA PRO 20 65.701 31.485 129.097 1.00 41.14 ATOM 38 CB PRO 20 64.948 32.602 128.399 1.00 39.82 ATOM 39 CG PRO 20 63.907 32.939 129.376 1.00 40.47 ATOM 40 C PRO 20 67.160 31.434 128.676 1.00 39.83 ATOM 41 O PRO 20 68.037 31.887 129.405 1.00 40.57 ATOM 42 N LYS 21 67.415 30.867 127.506 1.00 37.64 ATOM 43 CA LYS 21 68.766 30.776 126.980 1.00 34.69 ATOM 44 CB LYS 21 69.352 29.384 127.208 1.00 33.35 ATOM 45 CG LYS 21 69.626 29.032 128.645 1.00 33.21 ATOM 46 CD LYS 21 70.484 27.781 128.733 1.00 33.06 ATOM 47 CE LYS 21 70.796 27.418 130.183 1.00 34.73 ATOM 48 NZ LYS 21 71.677 26.215 130.332 1.00 33.57 ATOM 49 C LYS 21 68.742 31.041 125.490 1.00 33.43 ATOM 50 O LYS 21 67.694 30.975 124.852 1.00 33.06 ATOM 51 N ARG 22 69.897 31.370 124.937 1.00 32.25 ATOM 52 CA ARG 22 70.004 31.581 123.506 1.00 31.08 ATOM 53 CB ARG 22 70.687 32.911 123.203 1.00 32.57 ATOM 54 CG ARG 22 69.732 34.071 122.957 1.00 34.47 ATOM 55 CD ARG 22 70.516 35.341 122.616 1.00 36.93 ATOM 56 NE ARG 22 70.829 36.139 123.798 1.00 38.72 ATOM 57 CZ ARG 22 70.073 37.138 124.238 1.00 40.61 ATOM 58 NH1 ARG 22 68.965 37.475 123.587 1.00 40.39 ATOM 59 NH2 ARG 22 70.402 37.775 125.353 1.00 41.63 ATOM 60 C ARG 22 70.890 30.421 123.081 1.00 28.84 ATOM 61 O ARG 22 71.770 30.019 123.845 1.00 28.33 ATOM 62 N LEU 23 70.658 29.856 121.900 1.00 25.80 ATOM 63 CA LEU 23 71.496 28.743 121.464 1.00 23.35 ATOM 64 CB LEU 23 70.652 27.528 121.105 1.00 20.30 ATOM 65 CG LEU 23 70.055 26.819 122.315 1.00 17.64 ATOM 66 CD1 LEU 23 69.385 25.554 121.854 1.00 16.44 ATOM 67 CD2 LEU 23 71.145 26.494 123.314 1.00 17.15 ATOM 68 C LEU 23 72.400 29.113 120.305 1.00 23.17 ATOM 69 O LEU 23 71.997 29.062 119.151 1.00 23.67 ATOM 70 N TYR 24 73.633 29.479 120.641 1.00 22.61 ATOM 71 CA TYR 24 74.639 29.894 119.677 1.00 22.55 ATOM 72 CB TYR 24 75.674 30.742 120.411 1.00 21.56 ATOM 73 CG TYR 24 76.854 31.226 119.591 1.00 22.00 ATOM 74 CD1 TYR 24 78.021 30.475 119.496 1.00 20.66 ATOM 75 CE1 TYR 24 79.133 30.959 118.835 1.00 20.25 ATOM 76 CD2 TYR 24 76.835 32.477 118.981 1.00 22.00 ATOM 77 CE2 TYR 24 77.949 32.966 118.309 1.00 21.75 ATOM 78 CZ TYR 24 79.092 32.202 118.246 1.00 21.10 ATOM 79 OH TYR 24 80.206 32.694 117.607 1.00 22.44 ATOM 80 C TYR 24 75.285 28.697 118.989 1.00 23.15 ATOM 81 O TYR 24 76.038 27.946 119.605 1.00 23.41 ATOM 82 N CYS 25 74.986 28.524 117.707 1.00 23.63 ATOM 83 CA CYS 25 75.524 27.401 116.945 1.00 24.20 ATOM 84 CB CYS 25 74.661 27.110 115.727 1.00 24.21 ATOM 85 SG CYS 25 75.389 25.850 114.684 1.00 26.18 ATOM 86 C CYS 25 76.944 27.630 116.473 1.00 23.32 ATOM 87 O CYS 25 77.215 28.599 115.788 1.00 24.36 ATOM 88 N LYS 26 77.832 26.709 116.814 1.00 22.03 ATOM 89 CA LYS 26 79.234 26.804 116.434 1.00 21.70 ATOM 90 CB LYS 26 79.948 25.505 116.809 1.00 19.91 ATOM 91 CG LYS 26 81.443 25.475 116.512 1.00 19.56 ATOM 92 CD LYS 26 82.119 24.288 117.228 1.00 20.95 ATOM 93 CE LYS 26 83.649 24.402 117.274 1.00 19.82 ATOM 94 NZ LYS 26 84.326 23.753 116.099 1.00 20.63 ATOM 95 C LYS 26 79.455 27.086 114.954 1.00 22.52 ATOM 96 O LYS 26 80.424 27.743 114.591 1.00 23.05 ATOM 97 N ASN 27 78.559 26.591 114.104 1.00 22.60 ATOM 98 CA ASN 27 78.712 26.775 112.668 1.00 22.64 ATOM 99 CB ASN 27 77.983 25.661 111.909 1.00 21.87 ATOM 100 CG ASN 27 78.352 25.622 110.431 1.00 21.71 ATOM 101 OD1 ASN 27 79.459 25.995 110.046 1.00 20.77 ATOM 102 ND2 ASN 27 77.433 25.148 109.603 1.00 20.65 ATOM 103 C ASN 27 78.253 28.128 112.156 1.00 23.27 ATOM 104 O ASN 27 77.146 28.273 111.647 1.00 24.11 ATOM 105 N GLY 28 79.118 29.124 112.292 1.00 23.45 ATOM 106 CA GLY 28 78.781 30.449 111.809 1.00 23.50 ATOM 107 C GLY 28 78.349 31.457 112.849 1.00 22.32 ATOM 108 O GLY 28 78.227 32.638 112.545 1.00 22.80 ATOM 109 N GLY 29 78.113 31.011 114.072 1.00 21.39 ATOM 110 CA GLY 29 77.698 31.935 115.107 1.00 20.23 ATOM 111 C GLY 29 76.240 32.346 115.001 1.00 20.30 ATOM 112 O GLY 29 75.852 33.405 115.468 1.00 20.85 ATOM 113 N PHE 30 75.419 31.516 114.382 1.00 19.92 ATOM 114 CA PHE 30 74.012 31.827 114.266 1.00 18.77 ATOM 115 CB PHE 30 73.413 31.150 113.044 1.00 19.08 ATOM 116 CG PHE 30 73.998 31.622 111.751 1.00 18.63 ATOM 117 CD1 PHE 30 75.294 31.279 111.398 1.00 18.35 ATOM 118 CD2 PHE 30 73.271 32.454 110.910 1.00 17.69 ATOM 119 CE1 PHE 30 75.855 31.755 110.240 1.00 18.97 ATOM 120 CE2 PHE 30 73.826 32.938 109.746 1.00 17.78 ATOM 121 CZ PHE 30 75.117 32.591 109.408 1.00 18.74 ATOM 122 C PHE 30 73.286 31.328 115.493 1.00 18.17 ATOM 123 O PHE 30 73.516 30.208 115.926 1.00 18.61 ATOM 124 N PHE 31 72.425 32.168 116.058 1.00 18.34 ATOM 125 CA PHE 31 71.634 31.800 117.226 1.00 17.11 ATOM 126 CB PHE 31 71.139 33.029 117.976 1.00 14.87 ATOM 127 CG PHE 31 72.204 33.774 118.690 1.00 14.67 ATOM 128 CD1 PHE 31 72.730 33.286 119.887 1.00 14.59 ATOM 129 CD2 PHE 31 72.692 34.970 118.166 1.00 13.25 ATOM 130 CE1 PHE 31 73.727 33.973 120.554 1.00 13.47 ATOM 131 CE2 PHE 31 73.690 35.667 118.819 1.00 12.61 ATOM 132 CZ PHE 31 74.212 35.167 120.016 1.00 13.50 ATOM 133 C PHE 31 70.424 31.087 116.688 1.00 17.61 ATOM 134 O PHE 31 69.829 31.546 115.719 1.00 18.12 ATOM 135 N LEU 32 70.049 29.975 117.306 1.00 17.96 ATOM 136 CA LEU 32 68.878 29.250 116.847 1.00 18.36 ATOM 137 CB LEU 32 68.697 27.951 117.627 1.00 17.45 ATOM 138 CG LEU 32 67.534 27.082 117.137 1.00 17.14 ATOM 139 CD1 LEU 32 67.753 26.717 115.686 1.00 16.23 ATOM 140 CD2 LEU 32 67.422 25.821 117.984 1.00 17.14 ATOM 141 C LEU 32 67.672 30.148 117.062 1.00 18.83 ATOM 142 O LEU 32 67.453 30.660 118.150 1.00 19.06 ATOM 143 N ARG 33 66.886 30.330 116.017 1.00 19.84 ATOM 144 CA ARG 33 65.721 31.185 116.084 1.00 21.62 ATOM 145 CB ARG 33 65.930 32.375 115.158 1.00 19.43 ATOM 146 CG ARG 33 64.697 33.208 114.964 1.00 17.69 ATOM 147 CD ARG 33 65.026 34.490 114.237 1.00 16.18 ATOM 148 NE ARG 33 65.443 34.278 112.861 1.00 13.18 ATOM 149 CZ ARG 33 65.745 35.265 112.031 1.00 12.69 ATOM 150 NH1 ARG 33 65.676 36.511 112.455 1.00 9.98 ATOM 151 NH2 ARG 33 66.124 35.013 110.782 1.00 14.90 ATOM 152 C ARG 33 64.395 30.529 115.724 1.00 23.39 ATOM 153 O ARG 33 64.300 29.769 114.763 1.00 23.37 ATOM 154 N ILE 34 63.368 30.846 116.499 1.00 24.83 ATOM 155 CA ILE 34 62.043 30.326 116.239 1.00 27.05 ATOM 156 CB ILE 34 61.503 29.555 117.423 1.00 26.29 ATOM 157 CG2 ILE 34 60.127 29.035 117.090 1.00 25.19 ATOM 158 CG1 ILE 34 62.453 28.415 117.771 1.00 25.48 ATOM 159 CD1 ILE 34 62.082 27.694 119.040 1.00 25.09 ATOM 160 C ILE 34 61.115 31.504 115.959 1.00 29.23 ATOM 161 O ILE 34 60.862 32.338 116.834 1.00 30.21 ATOM 162 N HIS 35 60.628 31.572 114.725 1.00 30.40 ATOM 163 CA HIS 35 59.727 32.630 114.301 1.00 30.70 ATOM 164 CB HIS 35 59.619 32.664 112.775 1.00 31.64 ATOM 165 CG HIS 35 60.916 32.944 112.082 1.00 33.81 ATOM 166 CD2 HIS 35 61.745 32.136 111.379 1.00 34.56 ATOM 167 ND1 HIS 35 61.517 34.184 112.104 1.00 34.42 ATOM 168 CE1 HIS 35 62.663 34.127 111.447 1.00 34.81 ATOM 169 NE2 HIS 35 62.825 32.895 110.998 1.00 35.40 ATOM 170 C HIS 35 58.353 32.356 114.874 1.00 30.61 ATOM 171 O HIS 35 57.996 31.209 115.132 1.00 30.59 ATOM 172 N PRO 36 57.560 33.411 115.084 1.00 30.75 ATOM 173 CD PRO 36 57.903 34.836 114.961 1.00 30.69 ATOM 174 CA PRO 36 56.216 33.247 115.628 1.00 30.14 ATOM 175 CB PRO 36 55.726 34.683 115.757 1.00 29.29 ATOM 176 CG PRO 36 56.990 35.460 115.966 1.00 29.66 ATOM 177 C PRO 36 55.346 32.422 114.680 1.00 30.78 ATOM 178 O PRO 36 54.359 31.823 115.096 1.00 29.83 ATOM 179 N ASP 37 55.716 32.391 113.404 1.00 31.83 ATOM 180 CA ASP 37 54.933 31.637 112.436 1.00 32.95 ATOM 181 CB ASP 37 54.958 32.305 111.057 1.00 32.63 ATOM 182 CG ASP 37 56.341 32.377 110.461 1.00 34.16 ATOM 183 OD1 ASP 37 57.108 31.398 110.570 1.00 34.89 ATOM 184 OD2 ASP 37 56.654 33.420 109.856 1.00 35.19 ATOM 185 C ASP 37 55.351 30.181 112.305 1.00 33.57 ATOM 186 O ASP 37 54.767 29.435 111.523 1.00 33.17 ATOM 187 N GLY 38 56.362 29.775 113.065 1.00 33.49 ATOM 188 CA GLY 38 56.798 28.394 113.000 1.00 32.49 ATOM 189 C GLY 38 58.094 28.128 112.262 1.00 31.52 ATOM 190 O GLY 38 58.666 27.056 112.399 1.00 30.69 ATOM 191 N ARG 39 58.566 29.080 111.472 1.00 31.26 ATOM 192 CA ARG 39 59.810 28.869 110.752 1.00 31.69 ATOM 193 CB ARG 39 60.053 30.008 109.758 1.00 31.81 ATOM 194 CG ARG 39 59.171 29.980 108.515 1.00 32.81 ATOM 195 CD ARG 39 59.377 31.207 107.634 1.00 31.85 ATOM 196 NE ARG 39 58.932 32.417 108.317 1.00 34.13 ATOM 197 CZ ARG 39 59.088 33.652 107.847 1.00 35.53 ATOM 198 NH1 ARG 39 58.649 34.687 108.553 1.00 35.87 ATOM 199 NH2 ARG 39 59.681 33.860 106.678 1.00 35.37 ATOM 200 C ARG 39 60.973 28.797 111.732 1.00 32.08 ATOM 201 O ARG 39 60.947 29.431 112.784 1.00 32.13 ATOM 202 N VAL 40 61.991 28.008 111.395 1.00 32.00 ATOM 203 CA VAL 40 63.174 27.902 112.244 1.00 30.66 ATOM 204 CB VAL 40 63.271 26.564 112.974 1.00 29.32 ATOM 205 CG1 VAL 40 64.335 26.668 114.031 1.00 30.19 ATOM 206 CG2 VAL 40 61.961 26.210 113.611 1.00 28.68 ATOM 207 C VAL 40 64.443 28.083 111.422 1.00 29.72 ATOM 208 O VAL 40 64.609 27.476 110.374 1.00 29.97 ATOM 209 N ASP 41 65.335 28.930 111.912 1.00 28.45 ATOM 210 CA ASP 41 66.579 29.216 111.226 1.00 27.57 ATOM 211 CB ASP 41 66.326 30.164 110.058 1.00 26.38 ATOM 212 CG ASP 41 65.642 31.437 110.487 1.00 25.63 ATOM 213 OD1 ASP 41 65.557 32.379 109.683 1.00 26.72 ATOM 214 OD2 ASP 41 65.181 31.496 111.633 1.00 26.67 ATOM 215 C ASP 41 67.507 29.880 112.218 1.00 27.61 ATOM 216 O ASP 41 67.252 29.853 113.410 1.00 29.10 ATOM 217 N GLY 42 68.576 30.487 111.726 1.00 27.57 ATOM 218 CA GLY 42 69.501 31.154 112.616 1.00 27.36 ATOM 219 C GLY 42 69.678 32.631 112.314 1.00 27.75 ATOM 220 O GLY 42 69.395 33.102 111.210 1.00 27.79 ATOM 221 N VAL 43 70.142 33.363 113.319 1.00 27.36 ATOM 222 CA VAL 43 70.406 34.787 113.199 1.00 28.43 ATOM 223 CB VAL 43 69.276 35.663 113.756 1.00 27.62 ATOM 224 CG1 VAL 43 68.588 36.385 112.645 1.00 27.23 ATOM 225 CG2 VAL 43 68.308 34.824 114.551 1.00 29.14 ATOM 226 C VAL 43 71.610 35.090 114.048 1.00 29.73 ATOM 227 O VAL 43 71.684 34.675 115.197 1.00 29.49 ATOM 228 N ARG 44 72.557 35.823 113.494 1.00 32.24 ATOM 229 CA ARG 44 73.723 36.175 114.270 1.00 34.28 ATOM 230 CB ARG 44 74.868 36.543 113.347 1.00 35.61 ATOM 231 CG ARG 44 75.389 35.358 112.587 1.00 38.73 ATOM 232 CD ARG 44 76.387 35.790 111.550 1.00 40.80 ATOM 233 NE ARG 44 77.205 34.667 111.133 1.00 43.26 ATOM 234 CZ ARG 44 77.965 34.665 110.047 1.00 45.68 ATOM 235 NH1 ARG 44 78.005 35.734 109.267 1.00 46.13 ATOM 236 NH2 ARG 44 78.683 33.591 109.743 1.00 47.63 ATOM 237 C ARG 44 73.423 37.320 115.230 1.00 34.49 ATOM 238 O ARG 44 74.102 37.469 116.238 1.00 34.82 ATOM 239 N GLU 45 72.401 38.116 114.936 1.00 34.24 ATOM 240 CA GLU 45 72.063 39.234 115.806 1.00 34.89 ATOM 241 CB GLU 45 71.032 40.136 115.135 1.00 36.45 ATOM 242 CG GLU 45 71.511 40.716 113.831 1.00 38.67 ATOM 243 CD GLU 45 72.789 41.508 113.990 1.00 40.75 ATOM 244 OE1 GLU 45 73.443 41.780 112.958 1.00 40.01 ATOM 245 OE2 GLU 45 73.137 41.861 115.142 1.00 43.18 ATOM 246 C GLU 45 71.553 38.809 117.175 1.00 34.59 ATOM 247 O GLU 45 70.457 38.273 117.308 1.00 35.36 ATOM 248 N LYS 46 72.356 39.072 118.198 1.00 33.75 ATOM 249 CA LYS 46 71.997 38.715 119.565 1.00 32.50 ATOM 250 CB LYS 46 73.173 39.001 120.508 1.00 30.55 ATOM 251 CG LYS 46 72.914 38.640 121.976 1.00 29.99 ATOM 252 CD LYS 46 74.222 38.563 122.762 1.00 29.49 ATOM 253 CE LYS 46 74.038 38.100 124.212 1.00 30.06 ATOM 254 NZ LYS 46 73.784 39.231 125.169 1.00 30.34 ATOM 255 C LYS 46 70.741 39.431 120.067 1.00 32.59 ATOM 256 O LYS 46 70.109 38.991 121.028 1.00 32.11 ATOM 257 N SER 47 70.374 40.524 119.409 1.00 32.29 ATOM 258 CA SER 47 69.210 41.290 119.816 1.00 32.73 ATOM 259 CB SER 47 69.417 42.755 119.468 1.00 31.79 ATOM 260 OG SER 47 69.643 42.912 118.083 1.00 34.24 ATOM 261 C SER 47 67.913 40.793 119.192 1.00 33.36 ATOM 262 O SER 47 66.833 41.292 119.499 1.00 32.79 ATOM 263 N ASP 48 68.014 39.806 118.313 1.00 34.12 ATOM 264 CA ASP 48 66.830 39.255 117.665 1.00 34.15 ATOM 265 CB ASP 48 67.200 37.982 116.916 1.00 34.62 ATOM 266 CG ASP 48 66.148 37.573 115.922 1.00 36.63 ATOM 267 OD1 ASP 48 66.138 38.139 114.809 1.00 37.75 ATOM 268 OD2 ASP 48 65.324 36.696 116.256 1.00 37.73 ATOM 269 C ASP 48 65.756 38.933 118.701 1.00 33.53 ATOM 270 O ASP 48 66.033 38.311 119.722 1.00 35.73 ATOM 271 N PRO 49 64.514 39.347 118.449 1.00 31.91 ATOM 272 CD PRO 49 64.085 40.209 117.336 1.00 30.21 ATOM 273 CA PRO 49 63.404 39.096 119.370 1.00 31.23 ATOM 274 CB PRO 49 62.319 40.035 118.845 1.00 30.48 ATOM 275 CG PRO 49 62.596 40.079 117.398 1.00 29.71 ATOM 276 C PRO 49 62.926 37.638 119.456 1.00 31.07 ATOM 277 O PRO 49 62.094 37.291 120.299 1.00 31.40 ATOM 278 N HIS 50 63.462 36.781 118.596 1.00 30.80 ATOM 279 CA HIS 50 63.033 35.392 118.575 1.00 29.86 ATOM 280 CB HIS 50 62.436 35.068 117.216 1.00 28.95 ATOM 281 CG HIS 50 61.474 36.098 116.736 1.00 28.18 ATOM 282 CD2 HIS 50 61.543 36.966 115.701 1.00 27.42 ATOM 283 ND1 HIS 50 60.284 36.357 117.380 1.00 28.66 ATOM 284 CE1 HIS 50 59.660 37.341 116.760 1.00 28.45 ATOM 285 NE2 HIS 50 60.404 37.728 115.740 1.00 28.50 ATOM 286 C HIS 50 64.108 34.374 118.875 1.00 29.05 ATOM 287 O HIS 50 63.992 33.227 118.457 1.00 30.34 ATOM 288 N ILE 51 65.158 34.767 119.580 1.00 26.57 ATOM 289 CA ILE 51 66.172 33.794 119.882 1.00 25.39 ATOM 290 CB ILE 51 67.546 34.274 119.458 1.00 23.16 ATOM 291 CG2 ILE 51 67.625 34.288 117.949 1.00 23.31 ATOM 292 GG1 ILE 51 67.824 35.655 120.035 1.00 22.31 ATOM 293 CD1 ILE 51 69.234 36.124 119.788 1.00 19.90 ATOM 294 C ILE 51 66.179 33.368 121.343 1.00 26.50 ATOM 295 O ILE 51 66.994 32.538 121.746 1.00 27.21 ATOM 296 N LYS 52 65.263 33.914 122.137 1.00 26.83 ATOM 297 CA LYS 52 65.179 33.530 123.546 1.00 28.13 ATOM 298 CB LYS 52 64.509 34.613 124.390 1.00 28.54 ATOM 299 CG LYS 52 65.446 35.713 124.844 1.00 30.65 ATOM 300 CD LYS 52 64.666 37.003 125.105 1.00 33.21 ATOM 301 CE LYS 52 65.556 38.156 125.566 1.00 32.45 ATOM 302 NZ LYS 52 66.103 37.936 126.935 1.00 33.76 ATOM 303 C LYS 52 64.383 32.240 123.653 1.00 28.24 ATOM 304 O LYS 52 63.161 32.227 123.455 1.00 28.10 ATOM 305 N LEU 53 65.092 31.159 123.972 1.00 27.84 ATOM 306 CA LEU 53 64.492 29.835 124.095 1.00 26.95 ATOM 307 CB LEU 53 65.350 28.802 123.374 1.00 26.01 ATOM 308 CG LEU 53 65.980 29.249 122.066 1.00 24.73 ATOM 309 CD1 LEU 53 66.738 28.085 121.481 1.00 23.64 ATOM 310 CD2 LEU 53 64.907 29.757 121.120 1.00 23.87 ATOM 311 C LEU 53 64.356 29.395 125.535 1.00 26.85 ATOM 312 O LEU 53 65.211 29.695 126.369 1.00 27.66 ATOM 313 N GLN 54 63.284 28.663 125.811 1.00 25.84 ATOM 314 CA GLN 54 63.020 28.140 127.142 1.00 25.74 ATOM 315 CB GLN 54 61.586 28.471 127.535 1.00 25.45 ATOM 316 CG GLN 54 61.179 28.035 128.921 1.00 27.24 ATOM 317 CD GLN 54 61.995 28.697 130.012 1.00 29.91 ATOM 318 OE1 GLN 54 62.193 29.911 130.016 1.00 28.79 ATOM 319 NE2 GLN 54 62.462 27.896 130.960 1.00 33.80 ATOM 320 C GLN 54 63.221 26.626 127.070 1.00 25.53 ATOM 321 O GLN 54 62.354 25.906 126.584 1.00 26.86 ATOM 322 N LEU 55 64.375 26.142 127.516 1.00 24.71 ATOM 323 CA LEU 55 64.627 24.710 127.481 1.00 24.05 ATOM 324 CB LEU 55 66.127 24.421 127.413 1.00 22.59 ATOM 325 CG LEU 55 66.902 25.117 126.306 1.00 22.36 ATOM 326 CD1 LEU 55 67.955 24.190 125.754 1.00 22.98 ATOM 327 CD2 LEU 55 65.968 25.493 125.204 1.00 23.14 ATOM 328 C LEU 55 64.040 24.082 128.731 1.00 24.22 ATOM 329 O LEU 55 64.347 24.503 129.852 1.00 24.57 ATOM 330 N GLN 56 63.179 23.091 128.544 1.00 23.12 ATOM 331 CA GLN 56 62.577 22.422 129.676 1.00 24.28 ATOM 332 CB GLN 56 61.063 22.595 129.670 1.00 22.45 ATOM 333 CG GLN 56 60.349 21.779 130.733 1.00 20.68 ATOM 334 CD GLN 56 60.688 22.203 132.155 1.00 21.65 ATOM 335 OE1 GLN 56 60.452 23.345 132.552 1.00 20.04 ATOM 336 NE2 GLN 56 61.234 21.276 132.933 1.00 23.27 ATOM 337 C GLN 56 62.921 20.963 129.569 1.00 25.91 ATOM 338 O GLN 56 62.989 20.426 128.468 1.00 28.11 ATOM 339 N ALA 57 63.157 20.318 130.701 1.00 26.95 ATOM 340 CA ALA 57 63.483 18.902 130.677 1.00 28.44 ATOM 341 CB ALA 57 64.433 18.549 131.819 1.00 29.12 ATOM 342 C ALA 57 62.185 18.150 130.830 1.00 29.10 ATOM 343 O ALA 57 61.320 18.559 131.605 1.00 28.67 ATOM 344 N GLU 58 62.029 17.070 130.072 1.00 29.83 ATOM 345 CA GLU 58 60.820 16.274 130.181 1.00 30.65 ATOM 346 CB GLU 58 60.346 15.824 128.811 1.00 31.00 ATOM 347 CG GLU 58 58.857 15.539 128.757 1.00 32.60 ATOM 348 CD GLU 58 58.027 16.723 129.207 1.00 33.58 ATOM 349 OE1 GLU 58 58.392 17.869 128.858 1.00 33.56 ATOM 350 OE2 GLU 58 57.008 16.506 129.901 1.00 35.63 ATOM 351 C GLU 58 61.188 15.078 131.036 1.00 30.91 ATOM 352 O GLU 58 60.333 14.344 131.515 1.00 30.95 ATOM 353 N GLU 59 62.489 14.916 131.232 1.00 31.82 ATOM 354 CA GLU 59 63.040 13.841 132.031 1.00 31.78 ATOM 355 CB GLU 59 62.496 12.499 131.578 1.00 33.64 ATOM 356 CG GLU 59 63.031 12.038 130.260 1.00 36.93 ATOM 357 CD GLU 59 62.664 10.602 129.993 1.00 39.85 ATOM 358 OE1 GLU 59 61.461 10.331 129.790 1.00 42.02 ATOM 359 OE2 GLU 59 63.571 9.741 129.999 1.00 41.11 ATOM 360 C GLU 59 64.529 13.873 131.821 1.00 30.93 ATOM 361 O GLU 59 65.005 14.502 130.880 1.00 31.63 ATOM 362 N ARG 60 65.259 13.186 132.688 1.00 29.47 ATOM 363 CA ARG 60 66.710 13.123 132.609 1.00 28.68 ATOM 364 CB ARG 60 67.196 11.887 133.344 1.00 30.06 ATOM 365 CG ARG 60 68.340 12.140 134.272 1.00 34.02 ATOM 366 CD ARG 60 68.351 11.091 135.363 1.00 38.00 ATOM 367 NE ARG 60 68.988 9.853 134.937 1.00 41.17 ATOM 368 CZ ARG 60 70.275 9.754 134.610 1.00 43.17 ATOM 369 NH1 ARG 60 71.064 10.819 134.653 1.00 43.52 ATOM 370 NH2 ARG 60 70.787 8.579 134.266 1.00 45.60 ATOM 371 C ARG 60 67.236 13.083 131.181 1.00 27.56 ATOM 372 O ARG 60 66.915 12.163 130.420 1.00 26.74 ATOM 373 N GLY 61 68.036 14.093 130.834 1.00 25.42 ATOM 374 CA GLY 61 68.650 14.179 129.521 1.00 23.18 ATOM 375 C GLY 61 67.769 14.499 128.336 1.00 22.45 ATOM 376 O GLY 61 68.255 14.571 127.206 1.00 22.39 ATOM 377 N VAL 62 66.480 14.696 128.576 1.00 21.70 ATOM 378 CA VAL 62 65.559 14.991 127.488 1.00 21.36 ATOM 379 CB VAL 62 64.467 13.948 127.390 1.00 21.25 ATOM 380 CG1 VAL 62 63.545 14.300 126.255 1.00 20.20 ATOM 381 CG2 VAL 62 65.086 12.578 127.184 1.00 22.19 ATOM 382 C VAL 62 64.891 16.330 127.660 1.00 21.42 ATOM 383 O VAL 62 64.329 16.625 128.718 1.00 21.01 ATOM 384 N VAL 63 64.922 17.131 126.607 1.00 21.21 ATOM 385 CA VAL 63 64.331 18.451 126.684 1.00 22.02 ATOM 386 CB VAL 63 65.419 19.536 126.680 1.00 21.49 ATOM 387 CG1 VAL 63 66.481 19.213 127.704 1.00 21.73 ATOM 388 CG2 VAL 63 66.026 19.650 125.290 1.00 20.18 ATOM 389 C VAL 63 63.387 18.808 125.553 1.00 23.18 ATOM 390 O VAL 63 63.413 18.210 124.477 1.00 23.67 ATOM 391 N SER 64 62.550 19.798 125.827 1.00 23.91 ATOM 392 CA SER 64 61.649 20.350 124.839 1.00 25.35 ATOM 393 CB SER 64 60.254 20.585 125.427 1.00 25.45 ATOM 394 OG SER 64 60.157 21.858 126.047 1.00 25.74 ATOM 395 C SER 64 62.380 21.686 124.670 1.00 26.31 ATOM 396 O SER 64 63.103 22.105 125.584 1.00 26.97 ATOM 397 N ILE 65 62.243 22.333 123.516 1.00 25.31 ATOM 398 CA ILE 65 62.889 23.624 123.302 1.00 23.48 ATOM 399 CB ILE 65 63.965 23.536 122.239 1.00 21.26 ATOM 400 CG2 ILE 65 64.493 24.913 121.921 1.00 20.99 ATOM 401 CG1 ILE 65 65.087 22.637 122.730 1.00 19.95 ATOM 402 CD1 ILE 65 66.175 22.427 121.710 1.00 18.86 ATOM 403 C ILE 65 61.793 24.551 122.833 1.00 24.23 ATOM 404 O ILE 65 61.307 24.432 121.717 1.00 26.34 ATOM 405 N LYS 66 61.398 25.476 123.688 1.00 23.45 ATOM 406 CA LYS 66 60.315 26.376 123.347 1.00 24.16 ATOM 407 CB LYS 66 59.308 26.366 124.490 1.00 25.18 ATOM 408 CG LYS 66 58.083 27.234 124.309 1.00 26.80 ATOM 409 CD LYS 66 57.169 27.059 125.526 1.00 28.71 ATOM 410 CE LYS 66 56.044 28.085 125.597 1.00 29.36 ATOM 411 NZ LYS 66 55.434 28.077 126.956 1.00 30.03 ATOM 412 C LYS 66 60.743 27.801 123.049 1.00 24.99 ATOM 413 O LYS 66 61.398 28.451 123.861 1.00 26.36 ATOM 414 N GLY 67 60.383 28.288 121.871 1.00 24.39 ATOM 415 CA GLY 67 60.721 29.649 121.535 1.00 23.66 ATOM 416 C GLY 67 59.802 30.486 122.394 1.00 23.71 ATOM 417 O GLY 67 58.590 30.370 122.280 1.00 23.31 ATOM 418 N VAL 68 60.363 31.325 123.253 1.00 24.43 ATOM 419 CA VAL 68 59.538 32.137 124.143 1.00 25.58 ATOM 420 CB VAL 68 60.412 32.961 125.102 1.00 24.89 ATOM 421 CG1 VAL 68 59.547 33.906 125.913 1.00 24.50 ATOM 422 CG2 VAL 68 61.163 32.038 126.026 1.00 23.51 ATOM 423 C VAL 68 58.569 33.075 123.425 1.00 27.13 ATOM 424 O VAL 68 57.374 33.093 123.725 1.00 27.43 ATOM 425 N SER 69 59.097 33.845 122.480 1.00 27.71 ATOM 426 CA SER 69 58.318 34.802 121.706 1.00 27.80 ATOM 427 CB SER 69 59.279 35.657 120.871 1.00 26.55 ATOM 428 OG SER 69 58.652 36.153 119.712 1.00 23.62 ATOM 429 C SER 69 57.293 34.135 120.791 1.00 28.43 ATOM 430 O SER 69 56.116 34.493 120.784 1.00 27.80 ATOM 431 N ALA 70 57.754 33.161 120.019 1.00 29.44 ATOM 432 CA ALA 70 56.890 32.455 119.085 1.00 30.39 ATOM 433 CB ALA 70 57.739 31.672 118.090 1.00 30.34 ATOM 434 C ALA 70 55.911 31.526 119.793 1.00 30.53 ATOM 435 O ALA 70 54.949 31.043 119.197 1.00 30.39 ATOM 436 N ASN 71 56.147 31.285 121.071 1.00 30.77 ATOM 437 CA ASN 71 55.271 30.407 121.817 1.00 32.78 ATOM 438 CB ASN 71 53.970 31.137 122.123 1.00 32.63 ATOM 439 CG ASN 71 53.257 30.571 123.330 1.00 33.86 ATOM 440 OD1 ASN 71 53.857 30.378 124.386 1.00 35.51 ATOM 441 ND2 ASN 71 51.968 30.315 123.186 1.00 34.15 ATOM 442 C ASN 71 54.996 29.129 121.008 1.00 33.89 ATOM 443 O ASN 71 53.848 28.735 120.803 1.00 33.35 ATOM 444 N ARG 72 56.074 28.502 120.543 1.00 34.56 ATOM 445 CA ARG 72 56.014 27.271 119.764 1.00 34.30 ATOM 446 CB ARG 72 56.245 27.545 118.280 1.00 33.36 ATOM 447 CG ARG 72 55.174 28.321 117.553 1.00 33.71 ATOM 448 CD ARG 72 55.635 28.572 116.110 1.00 34.74 ATOM 449 NE ARG 72 54.624 29.232 115.290 1.00 35.27 ATOM 450 CZ ARG 72 53.545 28.632 114.798 1.00 33.89 ATOM 451 NH1 ARG 72 53.327 27.349 115.028 1.00 33.02 ATOM 452 NH2 ARG 72 52.670 29.324 114.089 1.00 34.07 ATOM 453 C ARG 72 57.138 26.369 120.242 1.00 34.85 ATOM 454 O ARG 72 58.046 26.819 120.934 1.00 35.82 ATOM 455 N TYR 73 57.092 25.102 119.846 1.00 34.88 ATOM 456 CA TYR 73 58.120 24.149 120.233 1.00 33.16 ATOM 457 CB TYR 73 57.488 22.981 120.971 1.00 29.48 ATOM 458 CG TYR 73 56.795 23.390 122.244 1.00 27.00 ATOM 459 CD1 TYR 73 55.509 23.920 122.224 1.00 25.62 ATOM 460 CE1 TYR 73 54.878 24.301 123.396 1.00 23.39 ATOM 461 CD2 TYR 73 57.432 23.258 123.474 1.00 25.71 ATOM 462 CE2 TYR 73 56.812 23.640 124.645 1.00 23.18 ATOM 463 CZ TYR 73 55.537 24.158 124.601 1.00 22.75 ATOM 464 OH TYR 73 54.923 24.525 125.770 1.00 22.37 ATOM 465 C TYR 73 58.909 23.638 119.045 1.00 33.61 ATOM 466 O TYR 73 58.339 23.297 118.019 1.00 34.53 ATOM 467 N LEU 74 60.225 23.595 119.184 1.00 33.83 ATOM 468 CA LEU 74 61.077 23.108 118.113 1.00 35.21 ATOM 469 CB LEU 74 62.538 23.322 118.471 1.00 32.63 ATOM 470 CG LEU 74 63.465 22.385 117.715 1.00 30.54 ATOM 471 CD1 LEU 74 63.375 22.702 116.241 1.00 30.96 ATOM 472 CD2 LEU 74 64.871 22.523 118.226 1.00 29.71 ATOM 473 C LEU 74 60.835 21.621 117.924 1.00 37.36 ATOM 474 O LEU 74 61.081 20.837 118.839 1.00 39.11 ATOM 475 N ALA 75 60.358 21.231 116.747 1.00 38.42 ATOM 476 CA ALA 75 60.097 19.825 116.460 1.00 39.22 ATOM 477 CB ALA 75 58.609 19.583 116.394 1.00 37.95 ATOM 478 C ALA 75 60.751 19.431 115.146 1.00 40.58 ATOM 479 O ALA 75 60.800 20.231 114.208 1.00 41.93 ATOM 480 N MET 76 61.268 18.207 115.084 1.00 41.48 ATOM 481 CA MET 76 61.908 17.717 113.868 1.00 42.71 ATOM 482 CB MET 76 63.269 17.129 114.179 1.00 41.17 ATOM 483 CG MET 76 64.039 16.797 112.949 1.00 40.91 ATOM 484 SD MET 76 65.732 16.444 113.338 1.00 43.31 ATOM 485 CE MET 76 65.586 14.747 113.794 1.00 43.79 ATOM 486 C MET 76 61.037 16.649 113.222 1.00 44.35 ATOM 487 O MET 76 60.809 15.591 113.799 1.00 44.28 ATOM 488 N LYS 77 60.554 16.941 112.019 1.00 45.83 ATOM 489 CA LYS 77 59.697 16.029 111.280 1.00 47.28 ATOM 490 CB LYS 77 59.056 16.770 110.112 1.00 47.05 ATOM 491 CG LYS 77 58.522 18.160 110.444 1.00 45.60 ATOM 492 CD LYS 77 57.128 18.135 111.039 1.00 44.56 ATOM 493 CE LYS 77 57.155 17.746 112.499 1.00 44.94 ATOM 494 NZ LYS 77 55.799 17.813 113.127 1.00 45.37 ATOM 495 C LYS 77 60.496 14.843 110.749 1.00 49.12 ATOM 496 O LYS 77 61.725 14.839 110.805 1.00 48.68 ATOM 497 N GLU 78 59.793 13.846 110.211 1.00 51.45 ATOM 498 CA GLU 78 60.444 12.643 109.690 1.00 53.04 ATOM 499 CB GLU 78 59.407 11.583 109.288 1.00 54.65 ATOM 500 CG GLU 78 58.566 11.923 108.071 1.00 58.25 ATOM 501 CD GLU 78 57.760 13.198 108.258 1.00 61.11 ATOM 502 OE1 GLU 78 57.160 13.370 109.350 1.00 62.28 ATOM 503 OE2 GLU 78 57.719 14.022 107.313 1.00 61.51 ATOM 504 C GLU 78 61.425 12.855 108.539 1.00 52.66 ATOM 505 O GLU 78 62.398 12.115 108.432 1.00 53.96 ATOM 506 N ASP 79 61.195 13.836 107.671 1.00 51.02 ATOM 507 CA ASP 79 62.141 14.049 106.579 1.00 49.50 ATOM 508 CB ASP 79 61.517 14.883 105.461 1.00 49.01 ATOM 509 CG ASP 79 60.976 16.197 105.951 1.00 48.61 ATOM 510 OD1 ASP 79 60.637 17.053 105.106 1.00 47.79 ATOM 511 OD2 ASP 79 60.885 16.368 107.182 1.00 48.70 ATOM 512 C ASP 79 63.414 14.722 107.089 1.00 48.99 ATOM 513 O ASP 79 64.396 14.861 106.356 1.00 48.58 ATOM 514 N GLY 80 63.389 15.132 108.355 1.00 48.23 ATOM 515 CA GLY 80 64.549 15.764 108.953 1.00 46.48 ATOM 516 C CLY 80 64.545 17.274 108.901 1.00 44.84 ATOM 517 O GLY 80 65.590 17.900 109.054 1.00 44.26 ATOM 518 N ARG 81 63.382 17.871 108.679 1.00 44.21 ATOM 519 CA ARG 81 63.302 19.323 108.624 1.00 43.88 ATOM 520 CB ARG 81 62.362 19.781 107.507 1.00 45.36 ATOM 521 CG ARG 81 60.896 19.485 107.762 1.00 49.01 ATOM 522 CD ARG 81 60.009 19.877 106.574 1.00 50.98 ATOM 523 NE ARG 81 58.581 19.778 106.901 1.00 53.79 ATOM 524 CZ ARG 81 57.880 18.643 106.965 1.00 55.03 ATOM 525 NH1 ARG 81 58.455 17.471 106.718 1.00 55.84 ATOM 526 NH2 ARG 81 56.593 18.676 107.294 1.00 55.29 ATOM 527 C ARG 81 62.815 19.841 109.965 1.00 42.86 ATOM 528 O ARG 81 62.109 19.139 110.693 1.00 42.39 ATOM 529 N LEU 82 63.207 21.068 110.290 1.00 41.62 ATOM 530 CA LEU 82 62.827 21.686 111.551 1.00 40.80 ATOM 531 CB LEU 82 63.985 22.512 112.111 1.00 40.02 ATOM 532 CG LEU 82 65.360 21.870 112.203 1.00 39.83 ATOM 533 CD1 LEU 82 66.278 22.836 112.890 1.00 40.26 ATOM 534 CD2 LEU 82 65.294 20.567 112.976 1.00 40.58 ATOM 535 C LEU 82 61.628 22.599 111.388 1.00 40.36 ATOM 536 O LEU 82 61.335 23.064 110.292 1.00 40.36 ATOM 537 N LEU 83 60.957 22.862 112.501 1.00 39.84 ATOM 538 CA LEU 83 59.800 23.739 112.536 1.00 40.98 ATOM 539 CB LEU 83 58.700 23.201 111.618 1.00 40.74 ATOM 540 CG LEU 83 58.065 21.838 111.904 1.00 40.46 ATOM 541 CD1 LEU 83 57.117 21.904 113.096 1.00 39.09 ATOM 542 CD2 LEU 83 57.299 21.417 110.677 1.00 40.49 ATOM 543 C LEU 83 59.319 23.791 113.980 1.00 41.84 ATOM 544 O LEU 83 59.698 22.952 114.787 1.00 42.18 ATOM 545 N ALA 84 58.490 24.764 114.320 1.00 42.49 ATOM 546 CA ALA 84 58.021 24.841 115.689 1.00 44.12 ATOM 547 CB ALA 84 58.524 26.109 116.332 1.00 44.63 ATOM 548 C ALA 84 56.506 24.738 115.812 1.00 45.19 ATOM 549 O ALA 84 55.766 25.592 115.327 1.00 45.45 ATOM 550 N SER 85 56.060 23.674 116.470 1.00 45.94 ATOM 551 CA SER 85 54.643 23.411 116.679 1.00 46.93 ATOM 552 CB SER 85 54.452 21.952 117.092 1.00 47.72 ATOM 553 OG SER 85 53.104 21.693 117.446 1.00 49.98 ATOM 554 C SER 85 54.054 24.329 117.746 1.00 47.26 ATOM 555 O SER 85 54.763 24.775 118.642 1.00 48.27 ATOM 556 N LYS 86 52.757 24.607 117.654 1.00 47.10 ATOM 557 CA LYS 86 52.108 25.478 118.624 1.00 46.39 ATOM 558 CB LYS 86 50.780 25.993 118.070 1.00 46.39 ATOM 559 CG LYS 86 50.321 27.340 118.643 1.00 46.15 ATOM 560 CD LYS 86 51.221 28.504 118.183 1.00 46.01 ATOM 561 CE LYS 86 50.611 29.888 118.462 1.00 43.88 ATOM 562 NZ LYS 86 50.529 30.273 119.903 1.00 42.01 ATOM 563 C LYS 86 51.864 24.689 119.902 1.00 46.17 ATOM 564 O LYS 86 51.822 25.250 120.997 1.00 46.38 ATOM 565 N SER 87 51.702 23.380 119.752 1.00 45.54 ATOM 566 CA SER 87 51.470 22.500 120.886 1.00 44.56 ATOM 567 CB SER 87 50.066 21.899 120.825 1.00 45.04 ATOM 568 OG SER 87 49.925 21.045 119.706 1.00 45.18 ATOM 569 C SER 87 52.502 21.390 120.842 1.00 43.71 ATOM 570 O SER 87 53.014 21.054 119.783 1.00 42.09 ATOM 571 N VAL 88 52.799 20.814 121.997 1.00 43.56 ATOM 572 CA VAL 88 53.796 19.769 122.068 1.00 43.63 ATOM 573 CB VAL 88 54.184 19.513 123.528 1.00 42.66 ATOM 574 CG1 VAL 88 55.281 18.477 123.602 1.00 42.15 ATOM 575 CG2 VAL 88 54.634 20.807 124.167 1.00 41.54 ATOM 576 C VAL 88 53.357 18.461 121.422 1.00 43.94 ATOM 577 O VAL 88 52.185 18.107 121.455 1.00 43.53 ATOM 578 N THR 89 54.318 17.765 120.816 1.00 44.55 ATOM 579 CA THR 89 54.099 16.471 120.170 1.00 44.50 ATOM 580 CB THR 89 53.913 16.585 118.633 1.00 44.01 ATOM 581 OG1 THR 89 55.144 16.271 117.973 1.00 43.88 ATOM 582 CG2 THR 89 53.496 17.982 118.240 1.00 43.75 ATOM 583 C THR 89 55.356 15.647 120.446 1.00 45.06 ATOM 584 O THR 89 56.395 16.193 120.823 1.00 45.26 ATOM 585 N ASP 90 55.272 14.338 120.249 1.00 45.27 ATOM 586 CA ASP 90 56.410 13.466 120.522 1.00 46.21 ATOM 587 CB ASP 90 56.028 12.033 120.226 1.00 47.52 ATOM 588 CG ASP 90 55.814 11.808 118.763 1.00 49.35 ATOM 589 OD1 ASP 90 55.095 12.628 118.155 1.00 50.55 ATOM 590 OD2 ASP 90 56.363 10.826 118.220 1.00 50.71 ATOM 591 C ASP 90 57.654 13.809 119.715 1.00 46.06 ATOM 592 O ASP 90 58.696 13.179 119.887 1.00 46.36 ATOM 593 N GLU 91 57.547 14.808 118.844 1.00 45.13 ATOM 594 CA GLU 91 58.662 15.210 117.996 1.00 43.57 ATOM 595 CB GLU 91 58.169 15.435 116.566 1.00 44.39 ATOM 596 CG GLU 91 57.638 14.181 115.872 1.00 43.82 ATOM 597 CD GLU 91 56.971 14.484 114.543 1.00 43.03 ATOM 598 OE1 GLU 91 55.925 15.170 114.547 1.00 41.30 ATOM 599 OE2 GLU 91 57.495 14.037 113.499 1.00 42.95 ATOM 600 C GLU 91 59.342 16.466 118.492 1.00 42.39 ATOM 601 O GLU 91 60.227 17.001 117.830 1.00 42.51 ATOM 602 N CYS 92 58.923 16.936 119.659 1.00 40.94 ATOM 603 CA CYS 92 59.488 18.143 120.243 1.00 38.73 ATOM 604 CB CYS 92 58.368 19.010 120.809 1.00 38.75 ATOM 605 SG CYS 92 57.090 19.469 119.614 1.00 38.94 ATOM 606 C CYS 92 60.472 17.819 121.353 1.00 37.23 ATOM 607 O CYS 92 60.824 18.691 122.145 1.00 38.15 ATOM 608 N PHE 93 60.920 16.569 121.405 1.00 34.63 ATOM 609 CA PHE 93 61.849 16.135 122.440 1.00 31.83 ATOM 610 CB PHE 93 61.211 15.016 123.245 1.00 29.72 ATOM 611 CG PHE 93 60.004 15.465 123.981 1.00 28.43 ATOM 612 CD1 PHE 93 60.119 16.385 125.010 1.00 27.56 ATOM 613 CD2 PHE 93 58.743 15.071 123.577 1.00 29.45 ATOM 614 CE1 PHE 93 58.998 16.919 125.623 1.00 27.01 ATOM 615 CE2 PHE 93 57.609 15.601 124.185 1.00 29.35 ATOM 616 CZ PHE 93 57.741 16.530 125.210 1.00 27.87 ATOM 617 C PHE 93 63.192 15.719 121.894 1.00 30.86 ATOM 618 O PHE 93 63.277 15.007 120.899 1.00 31.92 ATOM 619 N PHE 94 64.250 16.173 122.556 1.00 28.82 ATOM 620 CA PHE 94 65.600 15.883 122.101 1.00 26.91 ATOM 621 CB PHE 94 66.194 17.127 121.430 1.00 23.96 ATOM 622 CG PHE 94 65.297 17.758 120.413 1.00 19.13 ATOM 623 CD1 PHE 94 65.571 17.636 119.056 1.00 19.27 ATOM 624 CD2 PHE 94 64.168 18.466 120.810 1.00 17.15 ATOM 625 CE1 PHE 94 64.728 18.214 118.097 1.00 18.35 ATOM 626 CE2 PHE 94 63.323 19.043 119.874 1.00 16.33 ATOM 627 CZ PHE 94 63.601 18.919 118.509 1.00 16.51 ATOM 628 C PHE 94 66.508 15.486 123.239 1.00 27.27 ATOM 629 O PHE 94 66.255 15.840 124.392 1.00 28.75 ATOM 630 N PHE 95 67.565 14.750 122.918 1.00 26.55 ATOM 631 CA PHE 95 68.525 14.365 123.938 1.00 27.50 ATOM 632 CB PHE 95 69.277 13.085 123.576 1.00 29.60 ATOM 633 CG PHE 95 68.417 11.870 123.536 1.00 32.07 ATOM 634 CD1 PHE 95 67.912 11.399 122.330 1.00 33.27 ATOM 635 CD2 PHE 95 68.062 11.222 124.711 1.00 33.12 ATOM 636 CE1 PHE 95 67.064 10.306 122.294 1.00 33.11 ATOM 637 CE2 PHE 95 67.215 10.131 124.687 1.00 33.28 ATOM 638 CZ PHE 95 66.715 9.672 123.473 1.00 33.45 ATOM 639 C PHE 95 69.529 15.490 124.021 1.00 27.10 ATOM 640 O PHE 95 70.296 15.722 123.085 1.00 27.95 ATOM 641 N GLU 96 69.519 16.209 125.131 1.00 25.84 ATOM 642 CA GLU 96 70.471 17.287 125.287 1.00 24.93 ATOM 643 CB GLU 96 69.956 18.367 126.236 1.00 24.70 ATOM 644 CG GLU 96 70.903 19.538 126.346 1.00 23.98 ATOM 645 CD GLU 96 70.418 20.572 127.321 1.00 26.19 ATOM 646 OE1 GLU 96 70.168 20.199 128.490 1.00 27.67 ATOM 647 OE2 GLU 96 70.290 21.754 126.926 1.00 25.82 ATOM 648 C GLU 96 71.722 16.681 125.865 1.00 24.41 ATOM 649 O GLU 96 71.684 16.038 126.916 1.00 24.25 ATOM 650 N ARG 97 72.833 16.881 125.177 1.00 24.39 ATOM 651 CA ARG 97 74.077 16.334 125.657 1.00 25.15 ATOM 652 CB ARG 97 74.467 15.097 124.858 1.00 29.19 ATOM 653 CG ARG 97 75.774 14.467 125.319 1.00 32.87 ATOM 654 CD ARG 97 76.419 13.730 124.172 1.00 36.29 ATOM 655 NE ARG 97 77.556 12.929 124.599 1.00 40.01 ATOM 656 CZ ARG 97 77.479 11.948 125.492 1.00 42.01 ATOM 657 NH1 ARG 97 76.315 11.653 126.058 1.00 42.21 ATOM 658 NH2 ARG 97 78.564 11.251 125.809 1.00 42.97 ATOM 659 C ARG 97 75.217 17.312 125.608 1.00 23.59 ATOM 660 O ARG 97 75.457 17.962 124.599 1.00 23.46 ATOM 661 N LEU 98 75.919 17.410 126.724 1.00 22.64 ATOM 662 CA LEU 98 77.077 18.268 126.810 1.00 22.94 ATOM 663 CB LEU 98 77.318 18.714 128.255 1.00 20.45 ATOM 664 CG LEU 98 78.670 19.366 128.567 1.00 19.51 ATOM 665 CD1 LEU 98 79.144 20.253 127.430 1.00 19.49 ATOM 666 CD2 LEU 98 78.530 20.154 129.839 1.00 18.78 ATOM 667 C LEU 98 78.224 17.404 126.312 1.00 23.89 ATOM 668 O LEU 98 78.681 16.502 127.008 1.00 25.47 ATOM 669 N GLU 99 78.663 17.667 125.091 1.00 24.74 ATOM 670 CA GLU 99 79.739 16.904 124.484 1.00 25.77 ATOM 671 CB GLU 99 79.810 17.220 122.995 1.00 26.71 ATOM 672 CG GLU 99 78.533 16.859 122.253 1.00 27.60 ATOM 673 CD GLU 99 78.266 15.370 122.263 1.00 28.48 ATOM 674 OE1 GLU 99 77.207 14.956 121.744 1.00 28.01 ATOM 675 OE2 GLU 99 79.120 14.613 122.786 1.00 29.35 ATOM 676 C GLU 99 81.072 17.185 125.145 1.00 25.65 ATOM 677 O GLU 99 81.206 18.144 125.894 1.00 25.21 ATOM 678 N SER 100 82.053 16.333 124.864 1.00 26.16 ATOM 679 CA SER 100 83.387 16.470 125.439 1.00 26.22 ATOM 680 CB SER 100 84.270 15.298 125.018 1.00 27.81 ATOM 681 OG SER 100 84.343 15.198 123.607 1.00 31.25 ATOM 682 C SER 100 84.096 17.762 125.083 1.00 24.49 ATOM 683 O SER 100 84.991 18.181 125.796 1.00 24.71 ATOM 684 N ASN 101 83.721 18.394 123.980 1.00 23.73 ATOM 685 CA ASN 101 84.377 19.644 123.630 1.00 22.99 ATOM 686 CB ASN 101 84.550 19.800 122.115 1.00 21.76 ATOM 687 CG ASN 101 83.251 19.952 121.397 1.00 20.18 ATOM 688 OD1 ASN 101 82.199 20.037 122.022 1.00 19.80 ATOM 689 ND2 ASN 101 83.308 19.997 120.072 1.00 18.87 ATOM 690 C ASN 101 83.641 20.847 124.210 1.00 22.97 ATOM 691 O ASN 101 83.962 21.987 123.904 1.00 23.31 ATOM 692 N ASN 102 82.662 20.581 125.062 1.00 22.48 ATOM 693 CA ASN 102 81.911 21.634 125.716 1.00 22.01 ATOM 694 CB ASN 102 82.855 22.686 126.284 1.00 22.23 ATOM 695 CG ASN 102 83.420 22.294 127.629 1.00 22.57 ATOM 696 OD1 ASN 102 82.696 21.846 128.511 1.00 22.39 ATOM 697 ND2 ASN 102 84.717 22.477 127.798 1.00 23.63 ATOM 698 C ASN 102 80.813 22.334 124.934 1.00 21.28 ATOM 699 O ASN 102 80.351 23.395 125.338 1.00 21.93 ATOM 700 N TYR 103 80.402 21.777 123.809 1.00 20.20 ATOM 701 CA TYR 103 79.303 22.378 123.082 1.00 19.42 ATOM 702 CB TYR 103 79.633 22.530 121.594 1.00 18.57 ATOM 703 CG TYR 103 80.564 23.697 121.266 1.00 18.66 ATOM 704 CD1 TYR 103 80.088 24.845 120.640 1.00 18.26 ATOM 705 CE1 TYR 103 80.933 25.902 120.332 1.00 16.61 ATOM 706 CD2 TYR 103 81.920 23.642 121.576 1.00 18.47 ATOM 707 CE2 TYR 103 82.770 24.697 121.276 1.00 17.49 ATOM 708 CZ TYR 103 82.271 25.822 120.652 1.00 17.62 ATOM 709 OH TYR 103 83.116 26.864 120.326 1.00 16.79 ATOM 710 C TYR 103 78.166 21.391 123.326 1.00 20.73 ATOM 711 O TYR 103 78.393 20.289 123.818 1.00 21.64 ATOM 712 N ASN 104 76.939 21.788 123.031 1.00 21.46 ATOM 713 CA ASN 104 75.804 20.905 123.242 1.00 21.95 ATOM 714 CB ASN 104 74.694 21.645 123.992 1.00 22.16 ATOM 715 CG ASN 104 75.008 21.824 125.460 1.00 21.47 ATOM 716 OD1 ASN 104 76.162 21.957 125.837 1.00 22.13 ATOM 717 ND2 ASN 104 73.983 21.842 126.288 1.00 20.81 ATOM 718 C ASN 104 75.269 20.379 121.925 1.00 22.94 ATOM 719 O ASN 104 75.466 20.989 120.872 1.00 22.22 ATOM 720 N THR 105 74.604 19.231 121.989 1.00 23.66 ATOM 721 CA THR 105 74.026 18.620 120.802 1.00 23.95 ATOM 722 CB THR 105 74.781 17.357 120.377 1.00 22.66 ATOM 723 OG1 THR 105 74.811 16.443 121.475 1.00 24.98 ATOM 724 CG2 THR 105 76.202 17.696 119.964 1.00 21.44 ATOM 725 C THR 105 72.610 18.229 121.130 1.00 24.19 ATOM 726 O TRR 105 72.356 17.580 122.142 1.00 23.89 ATOM 727 N TYR 106 71.685 18.626 120.273 1.00 24.68 ATOM 728 CA TYR 106 70.291 18.298 120.501 1.00 25.37 ATOM 729 CB TYR 106 69.462 19.574 120.412 1.00 21.41 ATOM 730 CG TYR 106 69.796 20.501 121.544 1.00 17.07 ATOM 731 CD1 TYR 106 69.210 20.328 122.793 1.00 16.65 ATOM 732 CE1 TYR 106 69.608 21.088 123.888 1.00 15.13 ATOM 733 CD2 TYR 106 70.786 21.466 121.412 1.00 15.18 ATOM 734 CE2 TYR 106 71.196 22.232 122.502 1.00 14.37 ATOM 735 CZ TYR 106 70.604 22.033 123.736 1.00 14.28 ATOM 736 OH TYR 106 71.020 22.747 124.828 1.00 12.09 ATOM 737 C TYR 106 69.846 17.252 119.499 1.00 27.76 ATOM 738 O TYR 106 69.475 17.574 118.371 1.00 28.60 ATOM 739 N ARG 107 69.905 15.993 119.931 1.00 29.65 ATOM 740 CA ARG 107 69.552 14.846 119.103 1.00 30.86 ATOM 741 CB ARG 107 70.457 13.674 119.468 1.00 31.13 ATOM 742 CG ARG 107 70.380 12.485 118.532 1.00 32.41 ATOM 743 CD ARG 107 71.598 11.571 118.713 1.00 32.66 ATOM 744 NE ARG 107 71.750 11.094 120.090 1.00 32.94 ATOM 745 CZ ARG 107 70.903 10.264 120.697 1.00 31.97 ATOM 746 NH1 ARG 107 69.837 9.805 120.055 1.00 31.43 ATOM 747 NH2 ARG 107 71.117 9.904 121.952 1.00 31.53 ATOM 748 C ARG 107 68.105 14.445 119.279 1.00 31.79 ATOM 749 O ARG 107 67.663 14.203 120.399 1.00 33.20 ATOM 750 N SER 108 67.373 14.376 118.170 1.00 32.91 ATOM 751 CA SER 108 65.957 14.007 118.183 1.00 33.98 ATOM 752 CB SER 108 65.401 13.981 116.758 1.00 33.63 ATOM 753 OG SER 108 64.127 13.364 116.710 1.00 32.09 ATOM 754 C SER 108 65.725 12.649 118.814 1.00 34.53 ATOM 755 O SER 108 66.249 11.640 118.345 1.00 33.98 ATOM 756 N ARG 109 64.926 12.625 119.873 1.00 35.10 ATOM 757 CA ARG 109 64.636 11.375 120.543 1.00 36.45 ATOM 758 CB ARG 109 63.858 11.615 121.835 1.00 35.72 ATOM 759 CG ARG 109 63.582 10.324 122.577 1.00 36.42 ATOM 760 CD ARG 109 63.037 10.536 123.967 1.00 35.39 ATOM 761 NE ARG 109 61.713 11.129 123.936 1.00 35.74 ATOM 762 CZ ARG 109 60.951 11.273 125.011 1.00 36.28 ATOM 763 NH1 ARG 109 61.397 10.855 126.191 1.00 36.06 ATOM 764 NH2 ARG 109 59.761 11.854 124.909 1.00 36.38 ATOM 765 C ARG 109 63.841 10.444 119.641 1.00 37.21 ATOM 766 O ARG 109 63.930 9.223 119.773 1.00 36.80 ATOM 767 N LYS 110 63.068 11.019 118.723 1.00 38.39 ATOM 768 CA LYS 110 62.265 10.213 117.811 1.00 38.92 ATOM 769 CB LYS 110 61.102 11.021 117.235 1.00 38.55 ATOM 770 CG LYS 110 59.967 10.156 116.715 1.00 38.82 ATOM 771 CD LYS 110 58.748 10.977 116.290 1.00 39.89 ATOM 772 CE LYS 110 57.679 10.121 115.564 1.00 40.04 ATOM 773 NZ LYS 110 57.046 9.064 116.420 1.00 37.08 ATOM 774 C LYS 110 63.144 9.673 116.689 1.00 39.37 ATOM 775 O LYS 110 63.311 8.465 116.558 1.00 40.36 ATOM 776 N TYR 111 63.721 10.557 115.890 1.00 39.00 ATOM 777 CA TYR 111 64.593 10.121 114.810 1.00 38.93 ATOM 778 CB TYR 111 64.395 11.063 113.634 1.00 40.33 ATOM 779 CG TYR 111 62.920 11.319 113.371 1.00 41.38 ATOM 780 CD1 TYR 111 62.035 10.264 113.185 1.00 41.70 ATOM 781 CE1 TYR 111 60.680 10.487 112.971 1.00 41.29 ATOM 782 CD2 TYR 111 62.406 12.611 113.337 1.00 41.72 ATOM 783 CE2 TYR 111 61.055 12.842 113.126 1.00 41.20 ATOM 784 CZ TYR 111 60.197 11.775 112.943 1.00 41.51 ATOM 785 OH TYR 111 58.855 11.995 112.729 1.00 41.98 ATOM 786 C TYR 111 66.037 10.119 115.322 1.00 38.59 ATOM 787 O TYR 111 66.914 10.793 114.796 1.00 38.33 ATOM 788 N THR 112 66.232 9.325 116.368 1.00 38.84 ATOM 789 CA THR 112 67.476 9.136 117.111 1.00 39.06 ATOM 790 CB THR 112 67.467 7.763 117.777 1.00 38.66 ATOM 791 OG1 THR 112 67.757 6.756 116.796 1.00 38.25 ATOM 792 CG2 THR 112 66.102 7.496 118.398 1.00 38.36 ATOM 793 C THR 112 68.856 9.287 116.478 1.00 39.58 ATOM 794 O THR 112 69.862 9.252 117.191 1.00 39.45 ATOM 795 N SER 113 68.936 9.443 115.168 1.00 39.83 ATOM 796 CA SER 113 70.246 9.565 114.543 1.00 39.71 ATOM 797 CB SER 113 70.385 8.511 113.448 1.00 38.44 ATOM 798 OG SER 113 69.216 8.475 112.648 1.00 37.77 ATOM 799 C SER 113 70.488 10.947 113.967 1.00 39.75 ATOM 800 O SER 113 71.540 11.213 113.393 1.00 39.88 ATOM 801 N TRP 114 69.514 11.830 114.142 1.00 39.62 ATOM 802 CA TRP 114 69.609 13.181 113.618 1.00 39.62 ATOM 803 CB TRP 114 68.412 13.458 112.729 1.00 41.59 ATOM 804 CG TRP 114 68.217 12.435 111.675 1.00 42.65 ATOM 805 CD2 TRP 114 67.041 12.237 110.895 1.00 42.92 ATOM 806 CE2 TRP 114 67.335 11.235 109.948 1.00 43.49 ATOM 807 CE3 TRP 114 65.767 12.814 110.899 1.00 42.96 ATOM 808 CD1 TRP 114 69.150 11.568 111.193 1.00 43.51 ATOM 809 NE1 TRP 114 68.631 10.845 110.154 1.00 44.02 ATOM 810 CZ2 TRP 114 66.399 10.793 109.010 1.00 42.90 ATOM 811 CZ3 TRP 114 64.838 12.379 109.968 1.00 43.00 ATOM 812 CH2 TRP 114 65.160 11.376 109.033 1.00 43.09 ATOM 813 C TRP 114 69.673 14.249 114.686 1.00 38.97 ATOM 814 O TRP 114 69.102 14.104 115.760 1.00 38.94 ATOM 815 N TYR 115 70.350 15.342 114.370 1.00 38.45 ATOM 816 CA TYR 115 70.500 16.439 115.312 1.00 37.45 ATOM 817 CB TYR 115 71.981 16.730 115.566 1.00 38.19 ATOM 818 CG TYR 115 72.769 15.592 116.159 1.00 38.70 ATOM 819 CD1 TYR 115 73.235 14.555 115.364 1.00 40.21 ATOM 820 CE1 TYR 115 73.971 13.518 115.901 1.00 40.15 ATOM 821 CD2 TYR 115 73.059 15.559 117.513 1.00 38.42 ATOM 822 CE2 TYR 115 73.792 14.530 118.057 1.00 38.96 ATOM 823 CZ TYR 115 74.247 13.512 117.246 1.00 39.54 ATOM 824 OH TYR 115 74.993 12.488 117.782 1.00 40.88 ATOM 825 C TYR 115 69.860 17.725 114.825 1.00 35.83 ATOM 826 O TYR 115 69.512 17.869 113.657 1.00 36.40 ATOM 827 N VAL 116 69.704 18.661 115.745 1.00 33.23 ATOM 828 CA VAL 116 69.180 19.953 115.392 1.00 31.90 ATOM 829 CB VAL 116 68.616 20.675 116.608 1.00 29.60 ATOM 830 CG1 VAL 116 68.190 22.046 116.218 1.00 29.66 ATOM 831 CG2 VAL 116 67.448 19.915 117.165 1.00 28.27 ATOM 832 C VAL 116 70.443 20.660 114.934 1.00 32.35 ATOM 833 O VAL 116 71.470 20.575 115.609 1.00 33.68 ATOM 834 N ALA 117 70.402 21.326 113.787 1.00 31.51 ATOM 835 CA ALA 117 71.596 22.021 113.329 1.00 30.34 ATOM 836 CB ALA 117 72.566 21.035 112.689 1.00 29.37 ATOM 837 C ALA 117 71.322 23.168 112.381 1.00 30.52 ATOM 838 O ALA 117 70.261 23.270 111.785 1.00 29.89 ATOM 839 N LEU 118 72.301 24.044 112.254 1.00 31.70 ATOM 840 CA LEU 118 72.171 25.171 111.365 1.00 33.07 ATOM 841 CB LEU 118 72.120 26.469 112.177 1.00 31.15 ATOM 842 CG LEU 118 70.863 26.628 113.034 1.00 29.10 ATOM 843 CD1 LEU 118 70.940 27.882 113.846 1.00 29.11 ATOM 844 CD2 LEU 118 69.653 26.689 112.142 1.00 29.28 ATOM 845 C LEU 118 73.336 25.179 110.382 1.00 34.94 ATOM 846 O LEU 118 74.452 24.780 110.717 1.00 34.42 ATOM 847 N LYS 119 73.061 25.606 109.155 1.00 37.22 ATOM 848 CA LYS 119 74.088 25.682 108.127 1.00 39.12 ATOM 849 CB LYS 119 73.449 25.678 106.742 1.00 39.24 ATOM 850 CG LYS 119 72.650 24.423 106.458 1.00 39.74 ATOM 851 CD LYS 119 72.649 24.116 104.977 1.00 41.15 ATOM 852 CE LYS 119 71.540 24.836 104.224 1.00 42.85 ATOM 853 NZ LYS 119 79.288 24.014 104.176 1.00 43.50 ATOM 854 C LYS 119 74.874 26.962 108.339 1.00 40.49 ATOM 855 O LYS 119 74.448 27.835 109.104 1.00 41.69 ATOM 856 N ARG 120 76.023 27.094 107.686 1.00 41.30 ATOM 857 CA ARG 120 76.798 28.313 107.878 1.00 42.48 ATOM 858 CB ARG 120 78.283 28.124 107.520 1.00 42.64 ATOM 859 CG ARG 120 78.605 27.689 106.101 1.00 43.83 ATOM 860 CD ARG 120 78.594 26.175 105.955 1.00 43.47 ATOM 861 NE ARG 120 79.014 25.722 104.629 1.00 43.21 ATOM 862 CZ ARG 120 80.246 25.846 104.151 1.00 44.61 ATOM 863 NH1 ARG 120 81.190 26.415 104.884 1.00 46.17 ATOM 864 NH2 ARG 120 80.539 25.382 102.949 1.00 45.84 ATOM 865 C ARG 120 76.183 29.446 107.075 1.00 43.28 ATOM 866 O ARG 120 76.752 30.531 106.968 1.00 43.69 ATOM 867 N THR 121 74.994 29.186 106.539 1.00 43.43 ATOM 868 CA THR 121 74.271 30.170 105.756 1.00 42.23 ATOM 869 CB THR 121 73.772 29.564 104.465 1.00 41.98 ATOM 870 OG1 THR 121 72.714 28.640 104.743 1.00 42.99 ATOM 871 CG2 THR 121 74.896 28.826 103.795 1.00 43.36 ATOM 872 C THR 121 73.082 30.735 106.518 1.00 42.08 ATOM 873 O THR 121 72.351 31.573 106.001 1.00 42.51 ATOM 874 N GLY 122 72.873 30.264 107.740 1.00 41.44 ATOM 875 CA GLY 122 71.779 30.792 108.525 1.00 41.27 ATOM 876 C GLY 122 70.490 30.014 108.498 1.00 40.70 ATOM 877 O GLY 122 69.527 30.412 109.143 1.00 40.68 ATOM 878 N GLN 123 70.451 28.922 107.746 1.00 41.11 ATOM 879 CA GLN 123 69.242 28.100 107.697 1.00 41.82 ATOM 880 CB GLN 123 68.797 27.824 106.270 1.00 43.37 ATOM 881 CG GLN 123 68.604 29.048 105.438 1.00 46.68 ATOM 882 CD GLN 123 68.160 28.697 104.051 1.00 49.75 ATOM 883 OE1 GLN 123 68.680 27.753 103.442 1.00 52.33 ATOM 884 NE2 GLN 123 67.200 29.456 103.526 1.00 51.17 ATOM 885 C GLN 123 69.566 26.783 108.348 1.00 40.53 ATOM 886 O GLN 123 70.731 26.404 108.432 1.00 40.36 ATOM 887 N TYR 124 68.544 26.071 108.797 1.00 39.08 ATOM 888 CA TYR 124 68.801 24.797 109.443 1.00 38.47 ATOM 889 CB TYR 124 67.533 24.254 110.123 1.00 34.77 ATOM 890 CG TYR 124 66.425 23.813 109.199 1.00 32.38 ATOM 891 CD1 TYR 124 66.589 22.732 108.348 1.00 31.29 ATOM 892 CE1 TYR 124 65.565 22.315 107.502 1.00 30.22 ATOM 893 CD2 TYR 124 65.201 24.472 109.185 1.00 32.42 ATOM 894 CE2 TYR 124 64.168 24.061 108.345 1.00 31.68 ATOM 895 CZ TYR 124 64.361 22.981 107.504 1.00 30.66 ATOM 896 OH TYR 124 63.359 22.578 106.654 1.00 30.68 ATOM 897 C TYR 124 69.346 23.782 108.447 1.00 39.35 ATOM 898 O TYR 124 69.467 24.066 107.256 1.00 39.98 ATOM 899 N LYS 125 69.696 22.604 108.948 1.00 39.17 ATOM 900 CA LYS 125 70.204 21.536 108.111 1.00 37.57 ATOM 901 CB LYS 125 71.654 21.227 108.452 1.00 35.65 ATOM 902 CG LYS 125 72.138 19.941 107.813 1.00 34.29 ATOM 903 CD LYS 125 73.516 19.523 108.292 1.00 33.86 ATOM 904 CE LYS 125 74.590 20.498 107.865 1.00 33.07 ATOM 905 NZ LYS 125 75.942 19.930 108.107 1.00 32.09 ATOM 906 C LYS 125 69.363 20.302 108.358 1.00 38.02 ATOM 907 O LYS 125 69.148 19.914 109.500 1.00 37.99 ATOM 908 N LEU 126 68.886 19.688 107.285 1.00 38.80 ATOM 909 CA LEU 126 68.070 18.487 107.399 1.00 39.48 ATOM 910 CB LEU 126 67.865 17.850 106.026 1.00 38.69 ATOM 911 CG LEU 126 66.712 18.390 105.187 1.00 37.82 ATOM 912 CD1 LEU 126 66.513 17.471 104.001 1.00 37.53 ATOM 913 CD2 LEU 126 65.434 18.447 106.011 1.00 38.14 ATOM 914 C LEU 126 68.699 17.464 108.324 1.00 39.57 ATOM 915 O LEU 126 69.841 17.073 108.122 1.00 39.43 ATOM 916 N GLY 127 67.949 17.037 109.334 1.00 40.17 ATOM 917 CA GLY 127 68.463 16.056 110.269 1.00 42.23 ATOM 918 C GLY 127 69.083 14.909 109.501 1.00 43.38 ATOM 919 O GLY 127 70.170 14.426 109.827 1.00 43.71 ATOM 920 N SER 128 68.386 14.480 108.458 1.00 43.71 ATOM 921 CA SER 128 68.864 13.391 107.618 1.00 43.74 ATOM 922 CB SER 128 67.888 13.146 106.458 1.00 43.62 ATOM 923 OG SER 128 67.540 14.343 105.778 1.00 42.70 ATOM 924 C SER 128 70.252 13.668 107.063 1.00 43.90 ATOM 925 O SER 128 70.899 12.781 106.524 1.00 44.67 ATOM 926 N LYS 129 70.710 14.901 107.216 1.00 44.72 ATOM 927 CA LYS 129 72.011 15.315 106.717 1.00 45.28 ATOM 928 CB LYS 129 71.787 16.519 105.792 1.00 46.93 ATOM 929 CG LYS 129 73.011 17.141 105.138 1.00 52.08 ATOM 930 CD LYS 129 72.582 18.374 104.302 1.00 55.55 ATOM 931 CE LYS 129 73.575 19.559 104.376 1.00 57.33 ATOM 932 NZ LYS 129 74.751 19.461 103.456 1.00 57.35 ATOM 933 C LYS 129 72.975 15.644 107.871 1.00 44.19 ATOM 934 O LYS 129 74.142 15.968 107.645 1.00 43.60 ATOM 935 N THR 130 72.490 15.542 109.106 1.00 42.55 ATOM 936 CA THR 130 73.315 15.846 110.268 1.00 42.68 ATOM 937 CB THR 130 72.451 16.296 111.446 1.00 42.81 ATOM 938 OG1 THR 130 71.463 15.299 111.729 1.00 43.32 ATOM 939 CG2 THR 130 71.765 17.599 111.113 1.00 42.84 ATOM 940 C THR 130 74.163 14.656 110.691 1.00 42.45 ATOM 941 O THR 130 73.840 13.517 110.369 1.00 42.53 ATOM 942 N GLY 131 75.248 14.925 111.415 1.00 42.09 ATOM 943 CA GLY 131 76.129 13.852 111.842 1.00 41.59 ATOM 944 C GLY 131 77.166 14.229 112.887 1.00 40.79 ATOM 945 O GLY 131 77.635 15.363 112.932 1.00 40.05 ATOM 946 N PRO 132 77.557 13.268 113.732 1.00 40.57 ATOM 947 CD PRO 132 77.066 11.884 113.594 1.00 39.61 ATOM 948 CA PRO 132 78.526 13.349 114.825 1.00 40.58 ATOM 949 CB PRO 132 78.920 11.898 115.009 1.00 40.55 ATOM 950 CG PRO 132 77.615 11.214 114.830 1.00 39.59 ATOM 951 C PRO 132 79.736 14.258 114.635 1.00 40.69 ATOM 952 O PRO 132 80.051 15.084 115.501 1.00 40.87 ATOM 953 N GLY 133 80.424 14.106 113.512 1.00 40.45 ATOM 954 CA GLY 133 81.594 14.935 113.282 1.00 40.40 ATOM 955 C GLY 133 81.340 16.358 112.800 1.00 39.70 ATOM 956 O GLY 133 82.288 17.133 112.660 1.00 39.58 ATOM 957 N GLN 134 80.076 16.711 112.566 1.00 39.01 ATOM 958 CA GLN 134 79.709 18.038 112.056 1.00 38.30 ATOM 959 CB GLN 134 78.320 17.985 111.431 1.00 38.69 ATOM 960 CG GLN 134 78.259 17.176 110.162 1.00 40.00 ATOM 961 CD GLN 134 76.850 17.017 109.655 1.00 40.48 ATOM 962 OE1 GLN 134 76.103 17.988 109.552 1.00 40.40 ATOM 963 NE2 GLN 134 76.478 15.787 109.325 1.00 40.61 ATOM 964 C GLN 134 79.736 19.205 113.031 1.00 37.24 ATOM 965 O GLN 134 79.481 19.039 114.222 1.00 37.79 ATOM 966 N LYS 135 80.032 20.390 112.494 1.00 35.77 ATOM 967 CA LYS 135 80.076 21.634 113.258 1.00 34.42 ATOM 968 CB LYS 135 80.967 22.667 112.580 1.00 36.21 ATOM 969 CG LYS 135 82.413 22.278 112.522 1.00 40.14 ATOM 970 CD LYS 135 83.278 23.415 112.041 1.00 41.89 ATOM 971 CE LYS 135 84.747 22.995 112.065 1.00 45.11 ATOM 972 NZ LYS 135 85.048 21.792 111.216 1.00 47.95 ATOM 973 C LYS 135 78.694 22.231 113.366 1.00 32.96 ATOM 974 O LYS 135 78.436 23.039 114.242 1.00 32.00 ATOM 975 N ALA 136 77.810 21.831 112.461 1.00 32.01 ATOM 976 CA ALA 136 76.441 22.329 112.437 1.00 30.91 ATOM 977 CB ALA 136 75.736 21.844 111.179 1.00 29.19 ATOM 978 C ALA 136 75.631 21.921 113.655 1.00 30.28 ATOM 979 O ALA 136 74.732 22.640 114.072 1.00 31.03 ATOM 980 N ILE 137 75.950 20.770 114.228 1.00 29.98 ATOM 981 CA ILE 137 75.199 20.272 115.380 1.00 28.90 ATOM 982 CB ILE 137 75.272 18.738 115.500 1.00 28.83 ATOM 983 CG2 ILE 137 74.575 18.091 114.307 1.00 28.65 ATOM 984 CG1 ILE 137 76.736 18.310 115.642 1.00 28.11 ATOM 985 CD1 ILE 137 76.919 16.849 115.872 1.00 28.77 ATOM 986 C ILE 137 75.599 20.833 116.726 1.00 27.60 ATOM 987 O ILE 137 74.818 20.762 117.668 1.00 28.34 ATOM 988 N LEU 138 76.803 21.388 116.818 1.00 25.80 ATOM 989 CA LEU 138 77.297 21.939 118.078 1.00 24.32 ATOM 990 CB LEU 138 78.804 22.137 118.003 1.00 20.98 ATOM 991 CG LEU 138 79.595 20.913 117.602 1.00 17.84 ATOM 992 CD1 LEU 138 81.051 21.189 117.842 1.00 16.51 ATOM 993 CD2 LEU 138 79.128 19.720 118.404 1.00 17.39 ATOM 994 C LEU 138 76.665 23.262 118.478 1.00 24.83 ATOM 995 O LEU 138 76.710 24.234 117.727 1.00 26.01 ATOM 996 N PHE 139 76.089 23.307 119.673 1.00 24.34 ATOM 997 CA PHE 139 75.464 24.529 120.156 1.00 23.84 ATOM 998 CB PHE 139 73.953 24.367 120.264 1.00 22.28 ATOM 999 CG PHE 139 73.261 24.395 118.957 1.00 22.93 ATOM 1000 CD1 PHE 139 73.124 23.241 118.209 1.00 22.66 ATOM 1001 CD2 PHE 139 72.787 25.599 118.441 1.00 23.82 ATOM 1002 CE1 PHE 139 72.528 23.280 116.959 1.00 23.77 ATOM 1003 CE2 PHE 139 72.187 25.657 117.188 1.00 23.07 ATOM 1004 CZ PHE 139 72.057 24.496 116.447 1.00 24.52 ATOM 1005 C PHE 139 76.000 24.938 121.508 1.00 24.57 ATOM 1006 O PHE 139 76.331 24.088 122.331 1.00 25.29 ATOM 1007 N LEU 140 76.080 26.246 121.734 1.00 24.86 ATOM 1008 CA LEU 140 76.561 26.778 123.000 1.00 24.03 ATOM 1009 CB LEU 140 77.732 27.720 122.767 1.00 23.49 ATOM 1010 CG LEU 140 78.316 28.286 124.056 1.00 24.43 ATOM 1011 CD1 LEU 140 78.869 27.149 124.901 1.00 24.94 ATOM 1012 CD2 LEU 140 79.403 29.293 123.725 1.00 25.05 ATOM 1013 C LEU 140 75.442 27.528 123.696 1.00 23.97 ATOM 1014 O LEU 140 74.984 28.559 123.218 1.00 24.09 ATOM 1015 N PRO 141 74.972 27.012 124.835 1.00 25.23 ATOM 1016 CD PRO 141 75.348 25.765 125.523 1.00 26.10 ATOM 1017 CA PRO 141 73.893 27.692 125.550 1.00 24.64 ATOM 1018 CB PRO 141 73.431 26.642 126.546 1.00 24.01 ATOM 1019 CG PRO 141 74.697 25.950 126.879 1.00 25.83 ATOM 1020 C PRO 141 74.411 28.940 126.225 1.00 24.54 ATOM 1021 O PRO 141 75.468 28.921 126.840 1.00 24.16 ATOM 1022 N MET 142 73.656 30.023 126.095 1.00 25.83 ATOM 1023 CA MET 142 74.021 31.302 126.684 1.00 26.94 ATOM 1024 CB MET 142 74.467 32.259 125.590 1.00 26.73 ATOM 1025 CG MET 142 75.681 31.797 124.828 1.00 26.52 ATOM 1026 SD MET 142 75.825 32.695 123.291 1.00 28.68 ATOM 1027 CE MET 142 76.028 34.375 123.889 1.00 30.05 ATOM 1028 C MET 142 72.841 31.898 127.439 1.00 28.78 ATOM 1029 O MET 142 71.691 31.797 127.008 1.00 30.16 ATOM 1030 N SER 143 73.144 32.533 128.561 1.00 30.18 ATOM 1031 CA SER 143 72.141 33.137 129.428 1.00 31.33 ATOM 1032 CB SER 143 72.815 33.782 130.635 1.00 33.94 ATOM 1033 OG SER 143 73.513 34.964 130.241 1.00 34.85 ATOM 1034 C SER 143 71.316 34.201 128.753 1.00 32.07 ATOM 1035 O SER 143 71.709 34.760 127.723 1.00 33.01 ATOM 1036 N ALA 144 70.184 34.504 129.378 1.00 32.11 ATOM 1037 CA ALA 144 69.272 35.514 128.877 1.00 33.33 ATOM 1038 CB ALA 144 68.459 34.950 127.712 1.00 31.68 ATOM 1039 C ALA 144 68.354 35.953 130.012 1.00 33.81 ATOM 1040 O ALA 144 68.722 36.947 130.676 1.00 35.06 ATOM 1041 CB HIS 1016 101.518 8.804 140.892 1.00 59.01 ATOM 1042 CG HIS 1016 101.606 8.263 142.280 1.00 61.41 ATOM 1043 CD2 HIS 1016 101.132 7.115 142.818 1.00 62.71 ATOM 1044 ND1 HIS 1016 102.190 8.962 143.315 1.00 61.90 ATOM 1045 CE1 HIS 1016 102.065 8.269 144.433 1.00 63.14 ATOM 1046 NE2 HIS 1016 101.428 7.145 144.159 1.00 63.99 ATOM 1047 C HIS 1016 101.836 11.252 141.291 1.00 57.42 ATOM 1048 O HIS 1016 102.845 11.510 140.626 1.00 56.67 ATOM 1049 N HIS 1016 100.399 10.408 139.406 1.00 56.36 ATOM 1050 CA HIS 1016 100.844 10.175 140.811 1.00 57.59 ATOM 1051 N PHE 1017 101.561 11.859 142.448 1.00 57.43 ATOM 1052 CA PHE 1017 102.428 12.900 143.019 1.00 57.26 ATOM 1053 CB PHE 1017 101.756 13.525 144.262 1.00 59.29 ATOM 1054 CG PHE 1017 101.888 12.691 145.536 1.00 61.69 ATOM 1055 CD1 PHE 1017 103.100 12.628 146.234 1.00 62.85 ATOM 1056 CD2 PHE 1017 100.804 11.962 146.029 1.00 61.97 ATOM 1057 CE1 PHE 1017 103.226 11.848 147.402 1.00 63.09 ATOM 1058 CE2 PHE 1017 100.922 11.184 147.193 1.00 62.16 ATOM 1059 CZ PHE 1017 102.134 11.128 147.877 1.00 62.36 ATOM 1060 C PHE 1017 103.817 12.377 143.418 1.00 56.18 ATOM 1061 O PHE 1017 104.793 13.137 143.454 1.00 56.25 ATOM 1062 N LYS 1018 103.893 11.084 143.738 1.00 54.65 ATOM 1063 CA LYS 1018 105.148 10.462 144.160 1.00 52.68 ATOM 1064 CS LYS 1018 104.867 9.246 145.051 1.00 51.33 ATOM 1065 C LYS 1018 106.050 10.046 142.998 1.00 51.79 ATOM 1066 O LYS 1018 107.274 10.033 143.143 1.00 52.60 ATOM 1067 N ASP 1019 105.452 9.703 141.856 1.00 50.23 ATOM 1068 CA ASP 1019 106.215 9.298 140.669 1.00 48.35 ATOM 1069 CB ASP 1019 105.298 8.704 139.591 1.00 48.73 ATOM 1070 CG ASP 1019 104.915 7.266 139.862 1.00 49.14 ATOM 1071 OD1 ASP 1019 105.830 6.437 140.063 1.00 49.01 ATOM 1072 OD2 ASP 1019 103.698 6.968 139.856 1.00 49.31 ATOM 1073 C ASP 1019 106.930 10.486 140.040 1.00 46.68 ATOM 1074 O ASP 1019 106.536 11.632 140.237 1.00 47.50 ATOM 1075 N PRO 1020 107.992 10.227 139.266 1.00 44.76 ATOM 1076 CD PRO 1020 108.718 8.957 139.111 1.00 45.04 ATOM 1077 CA PRO 1020 108.724 11.314 138.618 1.00 43.38 ATOM 1078 CB PRO 1020 109.937 10.609 138.016 1.00 43.53 ATOM 1079 CG PRO 1020 110.133 9.436 138.912 1.00 44.61 ATOM 1080 C PRO 1020 107.838 11.904 137.532 1.00 41.94 ATOM 1081 O PRO 1020 106.804 11.332 137.188 1.00 42.82 ATOM 1082 N LYS 1021 108.251 13.040 136.990 1.00 39.67 ATOM 1083 CA LYS 1021 107.504 13.687 135.931 1.00 37.28 ATOM 1084 CB LYS 1021 106.621 14.775 136.527 1.00 37.64 ATOM 1085 CG LYS 1021 105.772 14.264 137.667 1.00 38.77 ATOM 1086 CD LYS 1021 104.743 15.284 138.098 1.00 39.71 ATOM 1087 CE LYS 1021 103.909 14.744 139.244 1.00 40.35 ATOM 1088 NZ LYS 1021 102.948 15.773 139.724 1.00 42.34 ATOM 1089 C LYS 1021 108.473 14.287 134.927 1.00 35.45 ATOM 1090 O LYS 1021 109.651 14.454 135.221 1.00 34.78 ATOM 1091 N ARG 1022 107.986 14.569 133.728 1.00 34.49 ATOM 1092 CA ARG 1022 108.807 15.208 132.703 1.00 33.99 ATOM 1093 CB ARG 1022 108.688 14.506 131.346 1.00 35.90 ATOM 1094 CG ARG 1022 108.969 13.004 131.299 1.00 38.98 ATOM 1095 CD ARG 1022 108.848 12.540 129.843 1.00 41.25 ATOM 1096 NE ARG 1022 108.420 11.152 129.670 1.00 42.83 ATOM 1097 CZ ARG 1022 109.222 10.093 129.748 1.00 44.82 ATOM 1098 NH1 ARG 1022 110.518 10.248 130.005 1.00 46.32 ATOM 1099 NH2 ARG 1022 108.731 8.875 129.547 1.00 44.61 ATOM 1100 C ARG 1022 108.168 16.588 132.589 1.00 32.26 ATOM 1101 O ARG 1022 106.947 16.714 132.720 1.00 32.02 ATOM 1102 N LEU 1023 108.960 17.629 132.361 1.00 29.70 ATOM 1103 CA LEU 1023 108.364 18.952 132.240 1.00 27.31 ATOM 1104 CB LEU 1023 109.045 19.915 133.216 1.00 27.24 ATOM 1105 CG LEU 1023 108.723 19.725 134.711 1.00 26.31 ATOM 1106 CD1 LEU 1023 109.524 20.709 135.531 1.00 25.75 ATOM 1107 CD2 LEU 1023 107.240 19.937 134.980 1.00 23.99 ATOM 1108 C LEU 1023 108.418 19.486 130.810 1.00 25.84 ATOM 1109 O LEU 1023 109.410 20.081 130.399 1.00 26.23 ATOM 1110 N TYR 1024 107.339 19.264 130.064 1.00 23.83 ATOM 1111 CA TYR 1024 107.228 19.690 128.671 1.00 22.57 ATOM 1112 CB TYR 1024 106.120 18.899 127.983 1.00 20.06 ATOM 1113 CG TYR 1024 105.878 19.250 126.529 1.00 19.18 ATOM 1114 CD1 TYR 1024 105.143 20.378 126.169 1.00 18.27 ATOM 1115 CE1 TYR 1024 104.860 20.657 124.833 1.00 18.14 ATOM 1116 CD2 TYR 1024 106.335 18.414 125.509 1.00 18.75 ATOM 1117 CE2 TYR 1024 106.062 18.684 124.172 1.00 18.37 ATOM 1118 CZ TYR 1024 105.324 19.802 123.836 1.00 19.29 ATOM 1119 OH TYR 1024 105.039 20.050 122.506 1.00 19.56 ATOM 1120 C TYR 1024 106.929 21.173 128.558 1.00 23.20 ATOM 1121 O TYR 1024 105.830 21.614 128.880 1.00 22.70 ATOM 1122 N CYS 1025 107.905 21.939 128.087 1.00 23.90 ATOM 1123 CA CYS 1025 107.724 23.378 127.947 1.00 24.69 ATOM 1124 CB CYS 1025 109.076 24.078 127.978 1.00 24.85 ATOM 1125 SG CYS 1025 108.936 25.801 127.521 1.00 28.12 ATOM 1126 C CYS 1025 106.977 23.755 126.675 1.00 24.46 ATOM 1127 O CYS 1025 107.374 23.377 125.577 1.00 25.06 ATOM 1128 N LYS 1026 105.902 24.519 126.825 1.00 24.76 ATOM 1129 CA LYS 1026 105.080 24.932 125.686 1.00 25.07 ATOM 1130 CB LYS 1026 103.983 25.901 126.131 1.00 23.49 ATOM 1131 CG LYS 1026 103.154 26.435 124.979 1.00 21.62 ATOM 1132 CD LYS 1026 102.026 27.292 125.466 1.00 20.45 ATOM 1133 CE LYS 1026 101.077 27.578 124.341 1.00 20.75 ATOM 1134 NZ LYS 1026 99.757 27.987 124.874 1.00 20.11 ATOM 1135 C LYS 1026 105.858 25.574 124.543 1.00 25.60 ATOM 1136 O LYS 1026 105.474 25.466 123.381 1.00 24.78 ATOM 1137 N ASN 1027 106.954 26.238 124.877 1.00 26.80 ATOM 1138 CA ASN 1027 107.759 26.920 123.879 1.00 27.49 ATOM 1139 CB ASN 1027 108.581 28.012 124.561 1.00 29.75 ATOM 1140 CG ASN 1027 109.111 29.032 123.586 1.00 31.30 ATOM 1141 OD1 ASN 1027 109.855 28.701 122.672 1.00 32.40 ATOM 1142 ND2 ASN 1027 108.722 30.283 123.776 1.00 32.49 ATOM 1143 C ASN 1027 108.688 25.993 123.109 1.00 27.16 ATOM 1144 O ASN 1027 109.874 25.906 123.416 1.00 26.88 ATOM 1145 N GLY 1028 108.157 25.307 122.104 1.00 26.67 ATOM 1146 CA GLY 1028 108.997 24.423 121.318 1.00 25.66 ATOM 1147 C GLY 1028 108.874 22.946 121.623 1.00 25.00 ATOM 1148 O GLY 1028 109.349 22.114 120.856 1.00 24.79 ATOM 1149 N GLY 1029 108.247 22.611 122.742 1.00 24.17 ATOM 1150 CA GLY 1029 108.083 21.215 123.077 1.00 23.89 ATOM 1151 C GLY 1029 109.342 20.605 123.639 1.00 24.58 ATOM 1152 O GLY 1029 109.561 19.394 123.530 1.00 25.56 ATOM 1153 N PHE 1030 110.185 21.438 124.234 1.00 24.21 ATOM 1154 CA PHE 1030 111.408 20.923 124.818 1.00 24.60 ATOM 1155 CB PHE 1030 112.506 21.994 124.833 1.00 27.19 ATOM 1156 CG PHE 1030 113.013 22.370 123.471 1.00 28.03 ATOM 1157 CD1 PHE 1030 112.293 23.243 122.656 1.00 28.82 ATOM 1158 CD2 PHE 1030 114.186 21.810 122.977 1.00 28.15 ATOM 1159 CE1 PHE 1030 112.735 23.547 121.361 1.00 28.58 ATOM 1160 CE2 PHE 1030 114.634 22.104 121.688 1.00 27.55 ATOM 1161 CZ PHE 1030 113.905 22.975 120.879 1.00 28.04 ATOM 1162 C PHE 1030 111.114 20.483 126.240 1.00 24.03 ATOM 1163 O PHE 1030 110.433 21.194 126.984 1.00 24.19 ATOM 1164 N PHE 1031 111.607 19.306 126.606 1.00 23.11 ATOM 1165 CA PHE 1031 111.420 18.799 127.957 1.00 23.93 ATOM 1166 CB PHE 1031 111.553 17.284 127.985 1.00 23.81 ATOM 1167 CG PHE 1031 110.423 16.563 127.342 1.00 24.08 ATOM 1168 CD1 PHE 1031 109.186 16.491 127.965 1.00 24.04 ATOM 1169 CD2 PHE 1031 110.609 15.902 126.133 1.00 24.06 ATOM 1170 CE1 PHE 1031 108.138 15.759 127.392 1.00 25.00 ATOM 1171 CE2 PHE 1031 109.578 15.171 125.551 1.00 23.76 ATOM 1172 CZ PHE 1031 108.336 15.096 126.181 1.00 24.63 ATOM 1173 C PHE 1031 112.544 19.391 128.782 1.00 24.04 ATOM 1174 O PHE 1031 113.694 19.372 128.348 1.00 24.45 ATOM 1175 N LEU 1032 112.222 19.914 129.962 1.00 24.19 ATOM 1176 CA LEU 1032 113.249 20.483 130.828 1.00 24.56 ATOM 1177 CB LEU 1032 112.627 21.058 132.102 1.00 25.47 ATOM 1178 CG LEU 1032 113.620 21.473 133.186 1.00 25.35 ATOM 1179 CD1 LEU 1032 114.612 22.467 132.624 1.00 25.37 ATOM 1180 CD2 LEU 1032 112.856 22.069 134.351 1.00 26.44 ATOM 1181 C LEU 1032 114.227 19.382 131.204 1.00 24.51 ATOM 1182 O LEU 1032 113.820 18.325 131.683 1.00 24.03 ATOM 1183 N ARG 1033 115.513 19.618 130.988 1.00 25.35 ATOM 1184 CA ARG 1033 116.480 18.600 131.333 1.00 27.36 ATOM 1185 CB ARG 1033 117.053 17.938 130.099 1.00 29.33 ATOM 1186 CG ARG 1033 118.195 17.018 130.427 1.00 30.80 ATOM 1187 CD ARG 1033 118.837 16.584 129.155 1.00 33.61 ATOM 1188 NE ARG 1033 119.158 17.738 128.327 1.00 34.72 ATOM 1189 CZ ARG 1033 119.497 17.657 127.047 1.00 36.13 ATOM 1190 NH1 ARG 1033 119.557 16.469 126.453 1.00 35.83 ATOM 1191 NH2 ARG 1033 119.766 18.764 126.363 1.00 36.25 ATOM 1192 C ARG 1033 117.617 19.067 132.206 1.00 28.28 ATOM 1193 O ARG 1033 118.128 20.192 132.074 1.00 27.87 ATOM 1194 N ILE 1034 118.004 18.165 133.102 1.00 28.57 ATOM 1195 CA ILE 1034 119.077 18.413 134.042 1.00 29.81 ATOM 1196 CB ILE 1034 118.602 18.182 135.503 1.00 29.73 ATOM 1197 CG2 ILE 1034 119.672 18.645 136.479 1.00 29.55 ATOM 1198 CG1 ILE 1034 117.292 18.927 135.770 1.00 28.20 ATOM 1199 CD1 ILE 1034 117.417 20.419 135.788 1.00 28.36 ATOM 1200 C ILE 1034 120.197 17.427 133.741 1.00 31.51 ATOM 1201 O ILE 1034 120.023 16.216 133.901 1.00 32.11 ATOM 1202 N HIS 1035 121.337 17.951 133.297 1.00 33.05 ATOM 1203 CA HIS 1035 122.508 17.136 132.989 1.00 34.19 ATOM 1204 CB HIS 1035 123.489 17.942 132.145 1.00 36.64 ATOM 1205 CG HIS 1035 123.020 18.181 130.747 1.00 40.58 ATOM 1206 CD2 HIS 1035 122.613 19.311 130.122 1.00 42.17 ATOM 1207 ND1 HIS 1035 122.911 17.166 129.818 1.00 42.83 ATOM 1208 CE1 HIS 1035 122.456 17.663 128.679 1.00 43.39 ATOM 1209 NE2 HIS 1035 122.267 18.962 128.837 1.00 44.24 ATOM 1210 C HIS 1035 123.177 16.729 134.292 1.00 33.79 ATOM 1211 O HIS 1035 123.072 17.435 135.292 1.00 33.45 ATOM 1212 N PRO 1036 123.857 15.576 134.306 1.00 34.09 ATOM 1213 CD PRO 1036 123.803 14.488 133.312 1.00 34.23 ATOM 1214 CA PRO 1036 124.531 15.133 135.535 1.00 34.98 ATOM 1215 CB PRO 1036 125.088 13.763 135.148 1.00 34.75 ATOM 1216 CG PRO 1036 124.066 13.264 134.168 1.00 34.74 ATOM 1217 C PRO 1036 125.630 16.116 135.968 1.00 35.63 ATOM 1218 O PRO 1036 126.026 16.155 137.137 1.00 34.88 ATOM 1219 N ASP 1037 126.104 16.916 135.017 1.00 36.45 ATOM 1220 CA ASP 1037 127.151 17.890 135.289 1.00 38.23 ATOM 1221 CB ASP 1037 127.973 18.131 134.024 1.00 40.95 ATOM 1222 CG ASP 1037 127.209 18.925 132.975 1.00 43.34 ATOM 1223 OD1 ASP 1037 126.783 20.060 133.279 1.00 44.61 ATOM 1224 OD2 ASP 1037 127.039 18.418 131.844 1.00 44.86 ATOM 1225 C ASP 1037 126.621 19.233 135.793 1.00 39.23 ATOM 1226 O ASP 1037 127.403 20.138 136.091 1.00 40.23 ATOM 1227 N GLY 1038 125.301 19.382 135.863 1.00 39.39 ATOM 1228 CA GLY 1038 124.740 20.635 136.342 1.00 38.48 ATOM 1229 C GLY 1038 124.132 21.533 135.278 1.00 38.00 ATOM 1230 O GLY 1038 123.409 22.474 135.606 1.00 37.99 ATOM 1231 N ARG 1039 124.419 21.273 134.008 1.00 37.82 ATOM 1232 CA ARG 1039 123.848 22.100 132.951 1.00 38.07 ATOM 1233 CB ARG 1039 124.432 21.739 131.591 1.00 40.33 ATOM 1234 CG ARG 1039 125.856 22.173 131.337 1.00 42.49 ATOM 1235 CD ARG 1039 126.235 21.758 129.924 1.00 45.35 ATOM 1236 NE ARG 1039 126.170 20.303 129.755 1.00 48.54 ATOM 1237 CZ ARG 1039 125.744 19.683 128.653 1.00 49.62 ATOM 1238 NH1 ARG 1039 125.735 18.354 128.605 1.00 49.36 ATOM 1239 NH2 ARG 1039 125.311 20.383 127.606 1.00 48.98 ATOM 1240 C ARG 1039 122.346 21.882 132.887 1.00 37.46 ATOM 1241 O ARG 1039 121.852 20.793 133.187 1.00 37.66 ATOM 1242 N VAL 1040 121.620 22.917 132.487 1.00 36.66 ATOM 1243 CA VAL 1040 120.168 22.832 132.359 1.00 35.75 ATOM 1244 CB VAL 1040 119.461 23.634 133.479 1.00 35.63 ATOM 1245 CG1 VAL 1040 117.970 23.515 133.343 1.00 35.65 ATOM 1246 CG2 VAL 1040 119.904 23.138 134.832 1.00 35.67 ATOM 1247 C VAL 1040 119.737 23.392 130.994 1.00 35.53 ATOM 1248 O VAL 1040 120.135 24.496 130.596 1.00 36.39 ATOM 1249 N ASP 1041 118.929 22.626 130.274 1.00 33.97 ATOM 1250 CA ASP 1041 118.447 23.046 128.967 1.00 32.42 ATOM 1251 CB ASP 1041 119.534 22.848 127.916 1.00 32.62 ATOM 1252 CG ASP 1041 120.015 21.411 127.843 1.00 32.94 ATOM 1253 OD1 ASP 1041 120.810 21.104 126.933 1.00 33.43 ATOM 1254 OD2 ASP 1041 119.605 20.591 128.695 1.00 32.32 ATOM 1255 C ASP 1041 117.255 22.175 128.632 1.00 31.66 ATOM 1256 O ASP 1041 116.714 21.500 129.510 1.00 32.29 ATOM 1257 N GLY 1042 116.853 22.177 127.367 1.00 30.54 ATOM 1258 CA GLY 1042 115.727 21.364 126.962 1.00 29.69 ATOM 1259 C GLY 1042 116.060 20.372 125.866 1.00 29.53 ATOM 1260 O GLY 1042 117.030 20.527 125.146 1.00 29.47 ATOM 1261 N VAL 1043 115.248 19.334 125.756 1.00 30.48 ATOM 1262 CA VAL 1043 115.418 18.319 124.732 1.00 31.18 ATOM 1263 CB VAL 1043 116.175 17.097 125.222 1.00 30.95 ATOM 1264 CG1 VAL 1043 117.582 17.153 124.723 1.00 31.45 ATOM 1265 CG2 VAL 1043 116.136 17.031 126.740 1.00 31.50 ATOM 1266 C VAL 1043 114.048 17.855 124.350 1.00 33.51 ATOM 1267 O VAL 1043 113.209 17.590 125.212 1.00 35.18 ATOM 1268 N ARG 1044 113.814 17.763 123.054 1.00 34.82 ATOM 1269 CA ARG 1044 112.530 17.319 122.564 1.00 36.01 ATOM 1270 CB ARG 1044 112.392 17.677 121.088 1.00 35.77 ATOM 1271 CG ARG 1044 112.204 19.145 120.799 1.00 36.67 ATOM 1272 CD ARG 1044 111.240 19.275 119.629 1.00 36.95 ATOM 1273 NE ARG 1044 111.264 20.585 118.999 1.00 36.46 ATOM 1274 CZ ARG 1044 112.322 21.071 118.376 1.00 37.37 ATOM 1275 NH1 ARG 1044 113.429 20.344 118.317 1.00 38.72 ATOM 1276 NH2 ARG 1044 112.269 22.265 117.804 1.00 38.11 ATOM 1277 C ARG 1044 112.379 15.806 122.730 1.00 36.56 ATOM 1278 O ARG 1044 111.267 15.293 122.861 1.00 37.22 ATOM 1279 N GLU 1045 113.501 15.098 122.725 1.00 37.07 ATOM 1280 CA GLU 1045 113.479 13.648 122.830 1.00 39.00 ATOM 1281 CB GLU 1045 114.880 13.103 122.589 1.00 41.67 ATOM 1282 CG GLU 1045 114.959 11.601 122.703 1.00 45.67 ATOM 1283 CD GLU 1045 113.987 10.909 121.774 1.00 47.99 ATOM 1284 OE1 GLU 1045 114.065 11.168 120.552 1.00 48.20 ATOM 1285 OE2 GLU 1045 113.152 10.112 122.266 1.00 49.71 ATOM 1286 C GLU 1045 112.934 13.125 124.157 1.00 39.22 ATOM 1287 O GLU 1045 113.573 13.254 125.204 1.00 39.70 ATOM 1288 N LYS 1046 111.755 12.511 124.098 1.00 39.02 ATOM 1289 CA LYS 1046 111.095 11.980 125.284 1.00 38.99 ATOM 1290 CB LYS 1046 109.712 11.453 124.903 1.00 40.13 ATOM 1291 CG LYS 1046 108.760 11.275 126.072 1.00 41.18 ATOM 1292 CD LYS 1046 107.452 10.664 125.597 1.00 41.92 ATOM 1293 CE LYS 1046 106.445 10.538 126.724 1.00 42.22 ATOM 1294 NZ LYS 1046 105.377 9.565 126.377 1.00 41.59 ATOM 1295 C LYS 1046 111.895 10.869 125.947 1.00 38.27 ATOM 1296 O LYS 1046 111.705 10.572 127.127 1.00 38.11 ATOM 1297 N SER 1047 112.798 10.257 125.194 1.00 37.78 ATOM 1298 CA SER 1047 113.587 9.169 125.745 1.00 37.54 ATOM 1299 CB SER 1047 113.930 8.157 124.653 1.00 37.91 ATOM 1300 OG SER 1047 114.816 8.722 123.704 1.00 38.67 ATOM 1301 C SER 1047 114.865 9.632 126.425 1.00 37.38 ATOM 1302 O SER 1047 115.596 8.818 126.987 1.00 37.63 ATOM 1303 N ASP 1048 115.142 10.931 126.391 1.00 37.33 ATOM 1304 CA ASP 1048 116.364 11.406 127.023 1.00 37.51 ATOM 1305 CB ASP 1048 116.451 12.924 127.034 1.00 38.35 ATOM 1306 CG ASP 1048 117.766 13.401 127.603 1.00 39.91 ATOM 1307 OD1 ASP 1048 118.706 13.622 126.817 1.00 41.96 ATOM 1308 OD2 ASP 1048 117.878 13.519 128.841 1.00 39.65 ATOM 1309 C ASP 1048 116.464 10.892 128.456 1.00 36.69 ATOM 1310 O ASP 1048 115.500 10.915 129.213 1.00 37.46 ATOM 1311 N PRO 1049 117.648 10.436 128.855 1.00 36.45 ATOM 1312 CD PRO 1049 118.917 10.515 128.109 1.00 37.50 ATOM 1313 CA PRO 1049 117.871 9.905 130.203 1.00 36.97 ATOM 1314 CB PRO 1049 119.215 9.221 130.069 1.00 37.74 ATOM 1315 CG PRO 1049 119.951 10.220 129.195 1.00 38.33 ATOM 1316 C PRO 1049 117.900 10.947 131.327 1.00 37.11 ATOM 1317 O PRO 1049 117.942 10.590 132.506 1.00 36.40 ATOM 1318 N HIS 1050 117.872 12.227 130.971 1.00 36.89 ATOM 1319 CA HIS 1050 117.946 13.275 131.978 1.00 36.16 ATOM 1320 CB HIS 1050 119.217 14.092 131.740 1.00 38.30 ATOM 1321 CG HIS 1050 120.450 13.251 131.642 1.00 41.46 ATOM 1322 CD2 HIS 1050 121.244 12.953 130.588 1.00 42.61 ATOM 1323 ND1 HIS 1050 120.952 12.537 132.710 1.00 42.99 ATOM 1324 CE1 HIS 1050 121.998 11.833 132.319 1.00 41.93 ATOM 1325 NE2 HIS 1050 122.197 12.067 131.035 1.00 42.82 ATOM 1326 C HIS 1050 116.731 14.194 132.059 1.00 35.30 ATOM 1327 O HIS 1050 116.842 15.336 132.526 1.00 35.31 ATOM 1328 N ILE 1051 115.572 13.714 131.617 1.00 33.53 ATOM 1329 CA ILE 1051 114.381 14.550 131.688 1.00 32.37 ATOM 1330 CB ILE 1051 113.604 14.576 130.346 1.00 32.31 ATOM 1331 CG2 ILE 1051 114.456 15.166 129.279 1.00 33.43 ATOM 1332 CG1 ILE 1051 113.173 13.168 129.944 1.00 33.19 ATOM 1333 CD1 ILE 1051 112.059 13.153 128.925 1.00 35.55 ATOM 1334 C ILE 1051 113.420 14.119 132.800 1.00 31.45 ATOM 1335 O ILE 1051 112.386 14.766 133.007 1.00 30.74 ATOM 1336 N LYS 1052 113.753 13.031 133.499 1.00 30.01 ATOM 1337 CA LYS 1052 112.911 12.539 134.589 1.00 29.82 ATOM 1338 CB LYS 1052 113.178 11.056 134.836 1.00 29.20 ATOM 1339 CG LYS 1052 112.119 10.160 134.223 1.00 30.35 ATOM 1340 CD LYS 1052 112.543 8.688 134.198 1.00 32.59 ATOM 1341 CE LYS 1052 111.398 7.744 133.745 1.00 33.09 ATOM 1342 NZ LYS 1052 110.379 7.422 134.818 1.00 32.19 ATOM 1343 C LYS 1052 113.178 13.355 135.856 1.00 30.43 ATOM 1344 O LYS 1052 114.215 13.204 136.507 1.00 30.77 ATOM 1345 N LEU 1053 112.225 14.219 136.198 1.00 29.79 ATOM 1346 CA LEU 1053 112.352 15.100 137.349 1.00 29.36 ATOM 1347 CB LEU 1053 111.990 16.532 136.939 1.00 29.08 ATOM 1348 CG LEU 1053 112.364 16.937 135.507 1.00 28.41 ATOM 1349 CD1 LEU 1053 111.923 18.366 135.238 1.00 28.73 ATOM 1350 CD2 LEU 1053 113.852 16.785 135.299 1.00 27.13 ATOM 1351 C LEU 1053 111.474 14.680 138.518 1.00 29.19 ATOM 1352 O LEU 1053 110.356 14.209 138.337 1.00 30.04 ATOM 1353 N GLN 1054 111.988 14.865 139.725 1.00 28.59 ATOM 1354 CA GLN 1054 111.252 14.522 140.927 1.00 27.99 ATOM 1355 CB GLN 1054 112.114 13.674 141.848 1.00 30.24 ATOM 1356 CG GLN 1054 111.328 12.989 142.939 1.00 33.29 ATOM 1357 CD GLN 1054 110.286 12.031 142.386 1.00 35.36 ATOM 1358 OE1 GLN 1054 110.615 11.090 141.656 1.00 35.98 ATOM 1359 NE2 GLN 1054 109.020 12.263 142.733 1.00 37.07 ATOM 1360 C GLN 1054 110.877 15.823 141.615 1.00 27.38 ATOM 1361 O GLN 1054 111.707 16.470 142.255 1.00 26.70 ATOM 1362 N LEU 1055 109.624 16.224 141.455 1.00 27.43 ATOM 1363 CA LEU 1055 109.174 17.464 142.062 1.00 27.22 ATOM 1364 CB LEU 1055 108.036 18.086 141.253 1.00 26.41 ATOM 1365 CG LEU 1055 108.096 18.061 139.724 1.00 25.53 ATOM 1366 CD1 LEU 1055 107.477 19.348 139.210 1.00 26.11 ATOM 1367 CD2 LEU 1055 109.516 17.932 139.224 1.00 25.01 ATOM 1368 C LEU 1055 108.717 17.155 143.477 1.00 27.58 ATOM 1369 O LEU 1055 107.894 16.266 143.705 1.00 28.23 ATOM 1370 N GLN 1056 109.282 17.883 144.430 1.00 27.30 ATOM 1371 CA GLN 1056 108.973 17.686 145.834 1.00 26.90 ATOM 1372 CB GLN 1056 110.237 17.290 146.587 1.00 25.90 ATOM 1373 CG GLN 1056 110.053 17.177 148.068 1.00 25.61 ATOM 1374 CD GLN 1056 109.254 15.962 148.458 1.00 25.90 ATOM 1375 OE1 GLN 1056 109.647 14.830 148.180 1.00 26.01 ATOM 1376 NE2 GLN 1056 108.125 16.188 149.109 1.00 26.29 ATOM 1377 C GLN 1056 108.470 18.997 146.373 1.00 27.81 ATOM 1378 O GLN 1056 108.977 20.057 146.004 1.00 28.43 ATOM 1379 N ALA 1057 107.470 18.942 147.239 1.00 28.38 ATOM 1380 CA ALA 1057 106.955 20.170 147.813 1.00 29.08 ATOM 1381 CB ALA 1057 105.489 20.034 148.133 1.00 28.76 ATOM 1382 C ALA 1057 107.733 20.419 149.080 1.00 29.91 ATOM 1383 O ALA 1057 108.043 19.482 149.818 1.00 28.98 ATOM 1384 N GLU 1058 108.083 21.674 149.326 1.00 31.39 ATOM 1385 CA GLU 1058 108.793 21.986 150.553 1.00 32.34 ATOM 1386 CB GLU 1058 109.930 22.975 150.309 1.00 32.18 ATOM 1387 CG GLU 1058 110.960 22.983 151.429 1.00 31.46 ATOM 1388 CD GLU 1058 111.597 21.618 151.657 1.00 32.73 ATOM 1389 OE1 GLU 1058 111.898 20.928 150.655 1.00 33.37 ATOM 1390 OE2 GLU 1058 111.810 21.239 152.833 1.00 31.34 ATOM 1391 C GLU 1058 107.741 22.574 151.478 1.00 32.21 ATOM 1392 O GLU 1058 107.961 22.715 152.672 1.00 33.06 ATOM 1393 N GLU 1059 106.586 22.889 150.896 1.00 32.19 ATOM 1394 CA GLU 1059 105.437 23.419 151.617 1.00 32.10 ATOM 1395 CB GLU 1059 105.829 24.600 152.491 1.00 35.18 ATOM 1396 CG GLU 1059 106.378 25.769 151.712 1.00 40.63 ATOM 1397 CD GLU 1059 106.664 26.957 152.598 1.00 43.35 ATOM 1398 OE1 GLU 1059 107.449 26.789 153.562 1.00 44.97 ATOM 1399 OE2 GLU 1059 106.106 28.048 152.331 1.00 45.15 ATOM 1400 C GLU 1059 104.420 23.858 150.589 1.00 30.54 ATOM 1401 O GLU 1059 104.743 23.981 149.414 1.00 30.71 ATOM 1402 N ARG 1060 103.192 24.094 151.027 1.00 29.55 ATOM 1403 CA ARG 1060 102.133 24.519 150.117 1.00 29.30 ATOM 1404 CB ARG 1060 101.011 25.229 150.866 1.00 30.12 ATOM 1405 CG ARG 1060 100.039 24.290 151.508 1.00 35.96 ATOM 1406 CD ARG 1060 98.847 25.021 152.089 1.00 40.51 ATOM 1407 NE ARG 1060 98.154 25.824 151.087 1.00 44.34 ATOM 1408 CZ ARG 1060 96.887 26.214 151.196 1.00 46.43 ATOM 1409 NH1 ARG 1060 96.173 25.870 152.264 1.00 47.36 ATOM 1410 NH2 ARG 1060 96.330 26.944 150.236 1.00 47.74 ATOM 1411 C ARG 1060 102.596 25.440 149.009 1.00 28.18 ATOM 1412 O ARG 1060 103.131 26.515 149.271 1.00 28.69 ATOM 1413 N GLY 1061 102.386 24.997 147.772 1.00 26.61 ATOM 1414 CA GLY 1061 102.726 25.789 146.607 1.00 23.35 ATOM 1415 C GLY 1061 104.187 25.978 146.276 1.00 22.25 ATOM 1416 O GLY 1061 104.512 26.659 145.297 1.00 22.12 ATOM 1417 N VAL 1062 105.073 25.379 147.063 1.00 20.62 ATOM 1418 CA VAL 1062 106.500 25.543 146.817 1.00 20.40 ATOM 1419 CB VAL 1062 107.221 26.212 148.004 1.00 20.05 ATOM 1420 CG1 VAL 1062 108.671 26.449 147.641 1.00 19.63 ATOM 1421 CG2 VAL 1062 106.542 27.513 148.382 1.00 19.04 ATOM 1422 C VAL 1062 107.181 24.225 146.593 1.00 20.43 ATOM 1423 O VAL 1062 107.045 23.306 147.398 1.00 22.34 ATOM 1424 N VAL 1063 107.946 24.133 145.520 1.00 19.65 ATOM 1425 CA VAL 1063 108.633 22.895 145.251 1.00 20.40 ATOM 1426 CB VAL 1063 107.990 22.162 144.062 1.00 20.01 ATOM 1427 CG1 VAL 1063 106.540 21.905 144.340 1.00 19.91 ATOM 1428 CG2 VAL 1063 108.143 22.981 142.797 1.00 19.44 ATOM 1429 C VAL 1063 110.117 23.034 144.955 1.00 21.75 ATOM 1430 O VAL 1063 110.634 24.123 144.701 1.00 20.92 ATOM 1431 N SER 1064 110.792 21.895 145.024 1.00 22.70 ATOM 1432 CA SER 1064 112.197 21.774 144.683 1.00 24.22 ATOM 1433 CB SER 1064 112.945 20.909 145.687 1.00 24.50 ATOM 1434 OG SER 1064 112.712 19.526 145.427 1.00 25.23 ATOM 1435 C SER 1064 112.001 20.949 143.418 1.00 26.06 ATOM 1436 O SER 1064 110.987 20.260 143.287 1.00 27.26 ATOM 1437 N ILE 1065 112.936 21.019 142.481 1.00 26.78 ATOM 1438 CA ILE 1065 112.830 20.241 141.244 1.00 26.41 ATOM 1439 CB ILE 1065 112.670 21.159 140.002 1.00 26.08 ATOM 1440 CG2 ILE 1065 112.846 20.365 138.726 1.00 25.26 ATOM 1441 CG1 ILE 1065 111.283 21.810 140.014 1.00 26.82 ATOM 1442 CD1 ILE 1065 111.098 22.875 138.958 1.00 25.95 ATOM 1443 C ILE 1065 114.137 19.494 141.164 1.00 26.94 ATOM 1444 O ILE 1065 115.187 20.095 140.953 1.00 27.36 ATOM 1445 N LYS 1066 114.078 18.184 141.350 1.00 27.63 ATOM 1446 CA LYS 1066 115.291 17.384 141.338 1.00 28.04 ATOM 1447 CB LYS 1066 115.335 16.508 142.587 1.00 29.73 ATOM 1448 CG LYS 1066 116.610 15.692 142.743 1.00 32.05 ATOM 1449 CD LYS 1066 116.683 15.055 144.129 1.00 33.02 ATOM 1450 CE LYS 1066 117.803 14.032 144.218 1.00 34.21 ATOM 1451 NZ LYS 1066 117.779 13.299 145.517 1.00 35.54 ATOM 1452 C LYS 1066 115.442 16.506 140.127 1.00 27.29 ATOM 1453 O LYS 1066 114.572 15.695 139.858 1.00 28.65 ATOM 1454 N GLY 1067 116.543 16.670 139.394 1.00 26.76 ATOM 1455 CA GLY 1067 116.786 15.826 138.237 1.00 26.32 ATOM 1456 C GLY 1067 117.139 14.470 138.810 1.00 25.76 ATOM 1457 O GLY 1067 118.123 14.341 139.526 1.00 25.98 ATOM 1458 N VAL 1068 116.329 13.461 138.527 1.00 26.18 ATOM 1459 CA VAL 1068 116.568 12.125 139.068 1.00 26.58 ATOM 1460 CB VAL 1068 115.472 11.134 138.596 1.00 24.83 ATOM 1461 CG1 VAL 1068 115.872 9.712 138.916 1.00 22.24 ATOM 1462 CG2 VAL 1068 114.157 11.472 139.260 1.00 22.15 ATOM 1463 C VAL 1068 117.938 11.549 138.723 1.00 28.21 ATOM 1464 O VAL 1068 118.682 11.132 139.614 1.00 27.21 ATOM 1465 N SER 1069 118.273 11.530 137.434 1.00 30.07 ATOM 1466 CA SER 1069 119.557 10.969 137.008 1.00 32.16 ATOM 1467 CB SER 1069 119.589 10.758 135.492 1.00 32.96 ATOM 1468 OG SER 1069 119.730 11.997 134.813 1.00 35.81 ATOM 1469 C SER 1069 120.761 11.815 137.429 1.00 32.02 ATOM 1470 O SER 1069 121.749 11.284 137.930 1.00 31.07 ATOM 1471 N ALA 1070 120.668 13.125 137.230 1.00 32.98 ATOM 1472 CA ALA 1070 121.747 14.042 137.577 1.00 33.74 ATOM 1473 CB ALA 1070 121.487 15.401 136.955 1.00 35.08 ATOM 1474 C ALA 1070 121.892 14.196 139.076 1.00 34.28 ATOM 1475 O ALA 1070 122.900 14.702 139.563 1.00 33.83 ATOM 1476 N AEN 1071 120.884 13.749 139.811 1.00 35.69 ATOM 1477 CA ASN 1071 120.904 13.876 141.256 1.00 36.90 ATOM 1478 CB ASN 1071 121.828 12.840 141.884 1.00 38.21 ATOM 1479 CG ASN 1071 121.792 12.885 143.398 1.00 40.11 ATOM 1480 OD1 ASN 1071 120.725 12.788 144.008 1.00 39.64 ATOM 1481 ND2 ASN 1071 122.960 13.037 144.016 1.00 42.09 ATOM 1482 C ASN 1071 121.364 15.278 141.641 1.00 37.10 ATOM 1483 O ASN 1071 122.301 15.452 142.418 1.00 36.45 ATOM 1484 N ARG 1072 120.699 16.273 141.063 1.00 38.23 ATOM 1485 CA ARG 1072 120.979 17.681 141.333 1.00 40.56 ATOM 1486 CB ARG 1072 121.832 18.286 140.214 1.00 43.40 ATOM 1487 CG ARG 1072 123.263 17.796 140.149 1.00 47.03 ATOM 1488 CD ARG 1072 124.011 18.408 138.956 1.00 49.83 ATOM 1489 NE ARG 1072 125.429 18.055 138.983 1.00 53.54 ATOM 1490 CZ ARG 1072 126.318 18.595 139.814 1.00 55.37 ATOM 1491 NH1 ARG 1072 125.947 19.528 140.684 1.00 56.73 ATOM 1492 NH2 ARG 1072 127.575 18.177 139.802 1.00 56.12 ATOM 1493 C ARG 1072 119.645 18.430 141.412 1.00 40.46 ATOM 1494 O ARG 1072 118.611 17.911 140.997 1.00 40.54 ATOM 1495 N TYR 1073 119.672 19.653 141.926 1.00 40.46 ATOM 1496 CA TYR 1073 118.462 20.456 142.055 1.00 40.39 ATOM 1497 CB TYR 1073 118.286 20.915 143.499 1.00 42.52 ATOM 1498 CG TYR 1073 118.051 19.769 144.437 1.00 46.38 ATOM 1499 CD1 TYR 1073 119.089 18.919 144.805 1.00 47.67 ATOM 1500 CE1 TYR 1073 118.856 17.824 145.630 1.00 49.63 ATOM 1501 CD2 TYR 1073 116.773 19.495 144.918 1.00 47.71 ATOM 1502 CE2 TYR 1073 116.530 18.402 145.738 1.00 48.59 ATOM 1503 CZ TYR 1073 117.571 17.571 146.093 1.00 49.39 ATOM 1504 OH TYR 1073 117.320 16.483 146.903 1.00 50.55 ATOM 1505 C TYR 1073 118.474 21.673 141.161 1.00 39.53 ATOM 1506 O TYR 1073 119.457 22.397 141.092 1.00 38.34 ATOM 1507 N LEU 1074 117.368 21.910 140.477 1.00 39.81 ATOM 1508 CA LEU 1074 117.285 23.072 139.607 1.00 40.61 ATOM 1509 CB LEU 1074 116.026 23.010 138.750 1.00 41.25 ATOM 1510 CG LEU 1074 115.821 24.151 137.755 1.00 41.64 ATOM 1511 CD1 LEU 1074 116.927 24.113 136.718 1.00 42.78 ATOM 1512 CD2 LEU 1074 114.461 24.018 137.074 1.00 42.53 ATOM 1513 C LEU 1074 117.258 24.334 140.460 1.00 41.43 ATOM 1514 O LEU 1074 116.326 24.548 141.243 1.00 41.50 ATOM 1515 N ALA 1075 118.289 25.161 140.311 1.00 42.19 ATOM 1516 CA ALA 1075 118.391 26.412 141.058 1.00 42.44 ATOM 1517 CB ALA 1075 119.536 26.329 142.046 1.00 41.88 ATOM 1518 C ALA 1075 118.608 27.590 140.106 1.00 43.17 ATOM 1519 O ALA 1075 119.308 27.459 139.101 1.00 42.34 ATOM 1520 N MET 1076 117.993 28.732 140.416 1.00 44.63 ATOM 1521 CA MET 1076 118.134 29.932 139.595 1.00 46.04 ATOM 1522 CB MET 1076 116.769 30.543 139.269 1.00 47.68 ATOM 1523 CG MET 1076 116.832 31.817 138.414 1.00 49.54 ATOM 1524 SD MET 1076 115.200 32.466 137.860 1.00 50.79 ATOM 1525 CE MET 1076 114.834 33.601 139.156 1.00 48.61 ATOM 1526 C MET 1076 118.972 30.942 140.354 1.00 47.36 ATOM 1527 O MET 1076 118.577 31.417 141.422 1.00 47.71 ATOM 1528 N LYS 1077 120.138 31.257 139.799 1.00 48.65 ATOM 1529 CA LYS 1077 121.054 32.204 140.411 1.00 50.09 ATOM 1530 CB LYS 1077 122.428 32.063 139.774 1.00 49.88 ATOM 1531 CG LYS 1077 122.892 30.620 139.686 1.00 49.37 ATOM 1532 CD LYS 1077 122.854 29.934 141.044 1.00 49.96 ATOM 1533 CE LYS 1077 123.705 30.668 142.081 1.00 49.24 ATOM 1534 NZ LYS 1077 123.839 29.874 143.343 1.00 49.00 ATOM 1535 C LYS 1077 120.536 33.627 140.256 1.00 51.61 ATOM 1536 O LYS 1077 119.554 33.863 139.548 1.00 51.81 ATOM 1537 N GLU 1078 121.202 34.570 140.918 1.00 53.33 ATOM 1538 CA GLU 1078 120.805 35.980 140.892 1.00 54.67 ATOM 1539 CB GLU 1078 121.730 36.793 141.789 1.00 56.39 ATOM 1540 CG GLU 1078 123.154 36.855 141.286 1.00 60.41 ATOM 1541 CD GLU 1078 124.030 37.707 142.175 1.00 63.75 ATOM 1542 OE1 GLU 1078 123.617 38.851 142.485 1.00 64.51 ATOM 1543 OE2 GLU 1078 125.127 37.234 142.559 1.00 65.35 ATOM 1544 C GLU 1078 120.756 36.641 139.512 1.00 54.55 ATOM 1545 O GLU 1078 119.907 37.499 139.270 1.00 54.10 ATOM 1546 N ASP 1079 121.663 36.269 138.612 1.00 53.83 ATOM 1547 CA ASP 1079 121.658 36.875 137.279 1.00 53.00 ATOM 1548 CB ASP 1079 122.962 36.564 136.539 1.00 52.34 ATOM 1549 CG ASP 1079 123.172 35.087 136.347 1.00 52.66 ATOM 1550 OD1 ASP 1079 124.074 34.708 135.574 1.00 52.13 ATOM 1551 OD2 ASP 1079 122.434 34.304 136.981 1.00 52.70 ATOM 1552 C ASP 1079 120.472 36.359 136.460 1.00 52.05 ATOM 1553 O ASP 1079 120.171 36.877 135.377 1.00 51.50 ATOM 1554 N GLY 1080 119.807 35.331 136.984 1.00 50.75 ATOM 1555 CA GLY 1080 118.668 34.752 136.295 1.00 48.77 ATOM 1556 C GLY 1080 119.015 33.559 135.426 1.00 47.34 ATOM 1557 O GLY 1080 118.249 33.205 134.532 1.00 46.65 ATOM 1558 N ARG 1081 120.165 32.939 135.679 1.00 46.16 ATOM 1559 CA ARG 1081 120.579 31.780 134.903 1.00 45.71 ATOM 1560 CB ARG 1081 122.084 31.834 134.626 1.00 47.53 ATOM 1561 CG ARG 1081 122.955 31.772 135.864 1.00 49.72 ATOM 1562 CD ARG 1081 124.439 31.920 135.531 1.00 50.75 ATOM 1563 NE ARG 1081 125.286 31.647 136.692 1.00 52.82 ATOM 1564 CZ ARG 1081 125.373 32.422 137.772 1.00 53.14 ATOM 1565 NH1 ARG 1081 124.671 33.542 137.858 1.00 52.95 ATOM 1566 NH2 ARG 1081 126.154 32.064 138.783 1.00 54.10 ATOM 1567 C ARG 1081 120.229 30.518 135.671 1.00 43.90 ATOM 1568 O ARG 1081 120.166 30.535 136.891 1.00 44.30 ATOM 1569 N LEU 1082 119.988 29.430 134.953 1.00 42.56 ATOM 1570 CA LEU 1082 119.632 28.168 135.586 1.00 41.88 ATOM 1571 CB LEU 1082 118.513 27.464 134.804 1.00 39.65 ATOM 1572 CG LEU 1082 117.245 28.286 134.563 1.00 38.35 ATOM 1573 CD1 LEU 1082 116.291 27.517 133.699 1.00 36.79 ATOM 1574 CD2 LEU 1082 116.597 28.642 135.889 1.00 38.70 ATOM 1575 C LEU 1082 120.830 27.246 135.682 1.00 41.96 ATOM 1576 O LEU 1082 121.814 27.411 134.972 1.00 41.58 ATOM 1577 N LEU 1083 120.725 26.275 136.576 1.00 43.51 ATOM 1578 CA LEU 1083 121.767 25.277 136.804 1.00 45.29 ATOM 1579 CB LEU 1083 123.088 25.941 137.202 1.00 47.13 ATOM 1580 CG LEU 1083 123.080 26.795 138.471 1.00 49.20 ATOM 1581 CD1 LEU 1083 123.140 25.887 139.699 1.00 50.34 ATOM 1582 CD2 LEU 1083 124.273 27.751 138.452 1.00 49.30 ATOM 1583 C LEU 1083 121.282 24.366 137.917 1.00 45.30 ATOM 1584 O LEU 1083 120.358 24.719 138.655 1.00 45.86 ATOM 1585 N ALA 1084 121.904 23.204 138.057 1.00 45.08 ATOM 1586 CA ALA 1084 121.466 22.273 139.082 1.00 46.14 ATOM 1587 CB ALA 1084 121.001 20.983 138.434 1.00 45.94 ATOM 1588 C ALA 1084 122.528 21.980 140.128 1.00 46.93 ATOM 1589 O ALA 1084 123.569 21.401 139.822 1.00 47.13 ATOM 1590 N SER 1085 122.246 22.383 141.366 1.00 48.12 ATOM 1591 CA SER 1085 123.152 22.174 142.489 1.00 48.98 ATOM 1592 CB SER 1085 122.752 23.072 143.655 1.00 48.95 ATOM 1593 OG SER 1085 123.625 22.857 144.751 1.00 52.03 ATOM 1594 C SER 1085 123.143 20.717 142.954 1.00 49.51 ATOM 1595 O SER 1085 122.150 20.008 142.780 1.00 50.20 ATOM 1596 N LYS 1086 124.246 20.270 143.550 1.00 49.42 ATOM 1597 CA LYS 1086 124.327 18.897 144.022 1.00 49.13 ATOM 1598 CB LYS 1086 125.782 18.477 144.221 1.00 50.70 ATOM 1599 CG LYS 1086 125.969 16.970 144.344 1.00 52.87 ATOM 1600 CD LYS 1086 125.581 16.261 143.049 1.00 54.61 ATOM 1601 CE LYS 1086 125.953 14.777 143.073 1.00 55.42 ATOM 1602 NZ LYS 1086 125.678 14.111 141.762 1.00 55.89 ATOM 1603 C LYS 1086 123.573 18.783 145.334 1.00 48.17 ATOM 1604 O LYS 1086 123.048 17.721 145.671 1.00 48.36 ATOM 1605 N SER 1087 123.528 19.883 146.076 1.00 46.90 ATOM 1606 CA SER 1087 122.822 19.917 147.351 1.00 46.76 ATOM 1607 CB SER 1087 123.809 20.024 148.523 1.00 47.35 ATOM 1608 OG SER 1087 124.816 20.994 148.282 1.00 49.65 ATOM 1609 C SER 1087 121.857 21.088 147.336 1.00 46.01 ATOM 1610 O SER 1087 122.063 22.067 146.636 1.00 46.35 ATOM 1611 N VAL 1088 120.793 20.989 148.108 1.00 46.03 ATOM 1612 CA VAL 1088 119.792 22.038 148.112 1.00 46.71 ATOM 1613 CB VAL 1088 118.524 21.563 148.840 1.00 46.96 ATOM 1614 CG1 VAL 1088 117.427 22.596 148.709 1.00 47.19 ATOM 1615 CG2 VAL 1088 118.069 20.241 148.253 1.00 48.07 ATOM 1616 C VAL 1088 120.254 23.350 148.722 1.00 47.27 ATOM 1617 O VAL 1088 121.065 23.370 149.651 1.00 48.46 ATOM 1618 N THR 1089 119.730 24.444 148.178 1.00 47.34 ATOM 1619 CA THR 1089 120.035 25.792 148.650 1.00 48.06 ATOM 1620 CB THR 1089 121.104 26.468 147.793 1.00 49.46 ATOM 1621 OG1 THR 1089 120.468 27.273 146.790 1.00 50.85 ATOM 1622 CG2 THR 1089 121.990 25.417 147.122 1.00 49.79 ATOM 1623 C THR 1089 118.750 26.596 148.517 1.00 47.80 ATOM 1624 O THR 1089 117.827 26.181 147.820 1.00 47.73 ATOM 1625 N ASP 1090 118.693 27.753 149.163 1.00 48.02 ATOM 1626 CA ASP 1090 117.488 28.575 149.127 1.00 49.32 ATOM 1627 CB ASP 1090 117.664 29.796 150.035 1.00 51.84 ATOM 1628 CG ASP 1090 118.986 30.499 149.811 1.00 54.89 ATOM 1629 OD1 ASP 1090 119.108 31.227 148.801 1.00 56.63 ATOM 1630 OD2 ASP 1090 119.905 30.309 150.642 1.00 56.50 ATOM 1631 C ASP 1090 117.083 29.021 147.731 1.00 48.91 ATOM 1632 O ASP 1090 116.061 29.689 147.557 1.00 49.18 ATOM 1633 N GLU 1091 117.878 28.646 146.736 1.00 48.37 ATOM 1634 CA GLU 1091 117.596 29.023 145.350 1.00 47.47 ATOM 1635 CB GLU 1091 118.876 29.494 144.635 1.00 49.80 ATOM 1636 CG GLU 1091 119.301 30.935 144.886 1.00 50.93 ATOM 1637 CD GLU 1091 120.616 31.274 144.195 1.00 51.80 ATOM 1638 OE1 GLU 1091 121.626 30.605 144.502 1.00 52.38 ATOM 1639 OE2 GLU 1091 120.640 32.202 143.351 1.00 51.13 ATOM 1640 C GLU 1091 117.012 27.871 144.555 1.00 45.38 ATOM 1641 O GLU 1091 116.833 27.983 143.348 1.00 45.82 ATOM 1642 N CYS 1092 116.733 26.759 145.219 1.00 43.43 ATOM 1643 CA CYS 1092 116.182 25.607 144.525 1.00 41.85 ATOM 1644 CB CYS 1092 116.895 24.332 144.968 1.00 43.23 ATOM 1645 SG CYS 1092 118.677 24.412 144.713 1.00 49.74 ATOM 1646 C CYS 1092 114.698 25.479 144.777 1.00 39.04 ATOM 1647 O CYS 1092 114.115 24.426 144.546 1.00 39.56 ATOM 1648 N PHE 1093 114.085 26.559 145.235 1.00 36.22 ATOM 1649 CA PHE 1093 112.663 26.534 145.532 1.00 35.29 ATOM 1650 CB PHE 1093 112.437 26.872 147.012 1.00 35.35 ATOM 1651 CG PHE 1093 113.179 25.953 147.953 1.00 36.46 ATOM 1652 CD1 PHE 1093 113.031 24.570 147.858 1.00 36.94 ATOM 1653 CD2 PHE 1093 114.069 26.460 148.894 1.00 36.72 ATOM 1654 CE1 PHE 1093 113.763 23.708 148.680 1.00 36.12 ATOM 1655 CE2 PHE 1093 114.803 25.602 149.719 1.00 36.60 ATOM 1656 CZ PHE 1093 114.647 24.227 149.607 1.00 36.17 ATOM 1657 C PHE 1093 111.873 27.464 144.632 1.00 34.61 ATOM 1658 O PHE 1093 112.259 28.610 144.400 1.00 35.53 ATOM 1659 N PHE 1094 110.757 26.958 144.120 1.00 32.86 ATOM 1660 CA PHE 1094 109.937 27.740 143.218 1.00 31.49 ATOM 1661 CB PHE 1094 110.168 27.247 141.793 1.00 33.20 ATOM 1662 CG PHE 1094 111.613 27.080 141.432 1.00 32.78 ATOM 1663 CD1 PHE 1094 112.212 27.930 140.520 1.00 33.09 ATOM 1664 CD2 PHE 1094 112.365 26.057 141.987 1.00 33.53 ATOM 1665 CE1 PHE 1094 113.538 27.761 140.162 1.00 34.51 ATOM 1666 CE2 PHE 1094 113.695 25.875 141.640 1.00 34.65 ATOM 1667 CZ PHE 1094 114.286 26.726 140.724 1.00 34.52 ATOM 1668 C PHE 1094 108.456 27.645 143.551 1.00 30.07 ATOM 1669 O PHE 1094 108.011 26.683 144.165 1.00 30.00 ATOM 1670 N PHE 1095 107.697 28.656 143.150 1.00 29.18 ATOM 1671 CA PHE 1095 106.258 28.654 143.367 1.00 29.08 ATOM 1672 CB PHE 1095 105.678 30.075 143.330 1.00 30.70 ATOM 1673 CG PHE 1095 105.982 30.902 144.540 1.00 32.10 ATOM 1674 CD1 PHE 1095 106.302 32.251 144.405 1.00 32.20 ATOM 1675 CD2 PHE 1095 105.943 30.353 145.814 1.00 32.82 ATOM 1676 CE1 PHE 1095 106.581 33.039 145.521 1.00 31.63 ATOM 1677 CE2 PHE 1095 106.223 31.142 146.943 1.00 32.55 ATOM 1678 CZ PHE 1095 106.542 32.482 146.789 1.00 31.42 ATOM 1679 C PHE 1095 105.674 27.896 142.190 1.00 28.62 ATOM 1680 O PHE 1095 105.714 28.378 141.052 1.00 28.80 ATOM 1681 N GLU 1096 105.147 26.707 142.442 1.00 27.22 ATOM 1682 CA GLU 1096 104.543 25.963 141.361 1.00 25.98 ATOM 1683 CB GLU 1096 104.605 24.475 141.632 1.00 25.73 ATOM 1684 CG GLU 1096 104.008 23.669 140.521 1.00 23.45 ATOM 1685 CD GLU 1096 103.987 22.226 140.855 1.00 22.74 ATOM 1686 OE1 GLU 1096 103.359 21.875 141.877 1.00 23.44 ATOM 1687 OE2 GLU 1096 104.607 21.449 140.108 1.00 22.66 ATOM 1688 C GLU 1096 103.096 26.427 141.272 1.00 25.50 ATOM 1689 O GLU 1096 102.356 26.399 142.254 1.00 25.24 ATOM 1690 N ARG 1097 102.699 26.866 140.090 1.00 25.40 ATOM 1691 CA ARG 1097 101.358 27.364 139.908 1.00 26.28 ATOM 1692 CB ARG 1097 101.390 28.886 139.876 1.00 29.12 ATOM 1693 CG ARG 1097 100.057 29.523 139.621 1.00 32.88 ATOM 1694 CD ARG 1097 100.215 31.021 139.479 1.00 36.76 ATOM 1695 NE ARG 1097 98.950 31.673 139.134 1.00 40.51 ATOM 1696 CZ ARG 1097 97.952 31.895 139.989 1.00 40.70 ATOM 1697 NH1 ARG 1097 98.069 31.519 141.262 1.00 40.49 ATOM 1698 NH2 ARG 1097 96.835 32.482 139.565 1.00 38.85 ATOM 1699 C ARG 1097 100.684 26.845 138.656 1.00 25.40 ATOM 1700 O ARG 1097 101.218 26.930 137.557 1.00 25.12 ATOM 1701 N LEU 1098 99.501 26.291 138.847 1.00 24.84 ATOM 1702 CA LEU 1098 98.699 25.771 137.765 1.00 24.97 ATOM 1703 CB LEU 1098 97.751 24.707 138.332 1.00 23.50 ATOM 1704 CG LEU 1098 96.656 24.214 137.391 1.00 23.67 ATOM 1705 CD1 LEU 1098 97.270 23.896 136.041 1.00 23.41 ATOM 1706 CD2 LEU 1098 95.951 23.008 137.988 1.00 22.84 ATOM 1707 C LEU 1098 97.939 26.994 137.227 1.00 25.39 ATOM 1708 O LEU 1098 96.951 27.446 137.818 1.00 25.72 ATOM 1709 N GLU 1099 98.419 27.546 136.118 1.00 25.13 ATOM 1710 CA GLU 1099 97.805 28.732 135.530 1.00 24.71 ATOM 1711 CB GLU 1099 98.692 29.296 134.429 1.00 22.34 ATOM 1712 CG GLU 1099 100.048 29.735 134.924 1.00 21.66 ATOM 1713 CD GLU 1099 99.965 30.849 135.934 1.00 22.92 ATOM 1714 OE1 GLU 1099 101.012 31.195 136.520 1.00 22.60 ATOM 1715 OE2 GLU 1099 98.852 31.387 136.140 1.00 25.85 ATOM 1716 C GLU 1099 96.435 28.441 134.980 1.00 25.92 ATOM 1717 O GLU 1099 96.065 27.287 134.814 1.00 27.25 ATOM 1718 N SER 1100 95.681 29.495 134.689 1.00 27.31 ATOM 1719 CA SER 1100 94.330 29.326 134.169 1.00 27.39 ATOM 1720 CB SER 1100 93.592 30.670 134.125 1.00 28.14 ATOM 1721 OG SER 1100 94.405 31.699 133.591 1.00 31.03 ATOM 1722 C SER 1100 94.263 28.646 132.813 1.00 26.49 ATOM 1723 O SER 1100 93.225 28.116 132.450 1.00 28.60 ATOM 1724 N ASN 1101 95.365 28.643 132.075 1.00 25.73 ATOM 1725 CA ASN 1101 95.415 28.013 130.760 1.00 24.86 ATOM 1726 CB ASN 1101 96.489 28.684 129.938 1.00 23.07 ATOM 1727 CG ASN 1101 97.768 28.790 130.700 1.00 22.42 ATOM 1728 OD1 ASN 1101 97.889 28.230 131.790 1.00 20.74 ATOM 1729 ND2 ASN 1101 98.733 29.503 130.152 1.00 24.80 ATOM 1730 C ASN 1101 95.781 26.545 130.902 1.00 24.40 ATOM 1731 O ASN 1101 95.906 25.841 129.915 1.00 25.58 ATOM 1732 N ASN 1102 96.005 26.109 132.132 1.00 23.54 ATOM 1733 CA ASN 1102 96.354 24.731 132.411 1.00 23.40 ATOM 1734 CB ASN 1102 95.420 23.812 131.654 1.00 26.98 ATOM 1735 CG ASN 1102 93.998 23.998 132.080 1.00 30.54 ATOM 1736 OD1 ASN 1102 93.680 23.887 133.265 1.00 33.07 ATOM 1737 ND2 ASN 1102 93.124 24.297 131.125 1.00 32.71 ATOM 1738 C ASN 1102 97.803 24.331 132.180 1.00 22.35 ATOM 1739 O ASN 1102 98.130 23.152 132.074 1.00 22.20 ATOM 1740 N TYR 1103 98.676 25.321 132.109 1.00 21.25 ATOM 1741 CA TYR 1103 100.098 25.064 131.960 1.00 21.42 ATOM 1742 CB TYR 1103 100.707 25.993 130.904 1.00 21.03 ATOM 1743 CG TYR 1103 100.594 25.458 129.486 1.00 21.58 ATOM 1744 CD1 TYR 1103 101.568 24.605 128.961 1.00 22.58 ATOM 1745 CE1 TYR 1103 101.460 24.083 127.672 1.00 22.23 ATOM 1746 CD2 TYR 1103 99.501 25.775 128.683 1.00 20.55 ATOM 1747 CE2 TYR 1103 99.383 25.257 127.390 1.00 22.04 ATOM 1748 CZ TYR 1103 100.364 24.415 126.887 1.00 22.33 ATOM 1749 OH TYR 1103 100.263 23.922 125.596 1.00 21.39 ATOM 1750 C TYR 1103 100.627 25.424 133.326 1.00 21.79 ATOM 1751 O TYR 1103 99.947 26.096 134.076 1.00 23.68 ATOM 1752 N ASN 1104 101.819 24.971 133.669 1.00 22.54 ATOM 1753 CA ASN 1104 102.387 25.299 134.970 1.00 23.11 ATOM 1754 CB ASN 1104 102.982 24.061 135.641 1.00 21.78 ATOM 1755 CG ASN 1104 101.953 23.244 136.358 1.00 19.51 ATOM 1756 OD1 ASN 1104 100.761 23.516 136.271 1.00 18.29 ATOM 1757 ND2 ASN 1104 102.408 22.228 137.075 1.00 18.41 ATOM 1758 C ASN 1104 103.484 26.325 134.815 1.00 24.80 ATOM 1759 O ASN 1104 104.102 26.442 133.757 1.00 25.15 ATOM 1760 N THR 1105 103.729 27.067 135.883 1.00 25.84 ATOM 1761 CA THR 1105 104.776 28.060 135.863 1.00 26.64 ATOM 1762 CB THR 1105 104.186 29.483 135.731 1.00 25.73 ATOM 1763 OG1 THR 1105 103.226 29.720 136.765 1.00 27.01 ATOM 1764 CG2 THR 1105 103.513 29.634 134.389 1.00 25.56 ATOM 1765 C THR 1105 105.588 27.909 137.141 1.00 27.82 ATOM 1766 O THR 1105 105.038 27.824 138.242 1.00 27.80 ATOM 1767 N TYR 1106 106.902 27.849 136.981 1.00 28.80 ATOM 1768 CA TYR 1106 107.792 27.697 138.118 1.00 30.47 ATOM 1769 CB TYR 1106 108.760 26.553 137.832 1.00 29.61 ATOM 1770 CG TYR 1106 108.023 25.253 137.768 1.00 29.12 ATOM 1771 CD1 TYR 1106 107.828 24.493 138.914 1.00 30.78 ATOM 1772 CE1 TYR 1106 107.020 23.362 138.903 1.00 30.90 ATOM 1773 CD2 TYR 1106 107.397 24.846 136.597 1.00 29.58 ATOM 1774 CE2 TYR 1106 106.583 23.720 136.572 1.00 30.55 ATOM 1775 CZ TYR 1106 106.398 22.984 137.734 1.00 31.06 ATOM 1776 OH TYR 1106 105.583 21.881 137.740 1.00 31.17 ATOM 1777 C TYR 1106 108.525 29.000 138.393 1.00 32.52 ATOM 1778 O TYR 1106 109.573 29.273 137.806 1.00 33.70 ATOM 1779 N ARG 1107 107.954 29.805 139.286 1.00 33.59 ATOM 1780 CA ARG 1107 108.519 31.098 139.637 1.00 33.71 ATOM 1781 CB ARG 1107 107.395 32.094 139.922 1.00 34.16 ATOM 1782 CG ARG 1107 107.888 33.456 140.363 1.00 35.95 ATOM 1783 CD ARG 1107 106.743 34.421 140.627 1.00 37.06 ATOM 1784 NE ARG 1107 105.738 33.845 141.517 1.00 39.01 ATOM 1785 CZ ARG 1107 104.896 34.553 142.264 1.00 38.49 ATOM 1786 NH1 ARG 1107 104.929 35.878 142.238 1.00 38.07 ATOM 1787 NH2 ARG 1107 104.028 33.930 143.048 1.00 38.62 ATOM 1788 C ARG 1107 109.439 30.998 140.835 1.00 34.38 ATOM 1789 O ARG 1107 109.050 30.486 141.882 1.00 34.01 ATOM 1790 N SER 1108 110.662 31.498 140.678 1.00 35.71 ATOM 1791 CA SER 1108 111.642 31.450 141.759 1.00 38.01 ATOM 1792 CB SER 1108 112.977 32.060 141.337 1.00 39.41 ATOM 1793 OG SER 1108 113.881 32.099 142.438 1.00 40.69 ATOM 1794 C SER 1108 111.161 32.180 142.991 1.00 38.82 ATOM 1795 O SER 1108 110.839 33.369 142.932 1.00 38.18 ATOM 1796 N ARG 1109 111.129 31.460 144.110 1.00 39.76 ATOM 1797 CA ARG 1109 110.689 32.041 145.370 1.00 40.06 ATOM 1798 CB ARG 1109 110.539 30.951 146.430 1.00 39.42 ATOM 1799 CG ARG 1109 109.916 31.444 147.706 1.00 39.10 ATOM 1800 CD ARG 1109 109.331 30.300 148.500 1.00 38.91 ATOM 1801 NE ARG 1109 110.356 29.444 149.079 1.00 39.39 ATOM 1802 CZ ARG 1109 110.552 29.301 150.385 1.00 40.16 ATOM 1803 NH1 ARG 1109 109.788 29.966 151.251 1.00 40.03 ATOM 1804 NH2 ARG 1109 111.505 28.486 150.824 1.00 40.40 ATOM 1805 C ARG 1109 111.671 33.108 145.852 1.00 40.49 ATOM 1806 O ARG 1109 111.284 34.035 146.570 1.00 39.63 ATOM 1807 N LYS 1110 112.934 32.970 145.445 1.00 41.21 ATOM 1808 CA LYS 1110 113.987 33.914 145.813 1.00 41.55 ATOM 1809 CB LYS 1110 115.351 33.274 145.566 1.00 42.81 ATOM 1810 CG LYS 1110 116.498 33.927 146.296 1.00 44.18 ATOM 1811 CD LYS 1110 116.463 33.554 147.765 1.00 45.85 ATOM 1812 CE LYS 1110 117.705 34.044 148.494 1.00 45.51 ATOM 1813 NZ LYS 1110 117.731 33.606 149.913 1.00 44.54 ATOM 1814 C LYS 1110 113.847 35.177 144.955 1.00 41.30 ATOM 1815 O LYS 1110 113.522 36.250 145.450 1.00 41.19 ATOM 1816 N TYR 1111 114.080 35.047 143.659 1.00 40.34 ATOM 1817 CA TYR 1111 113.967 36.195 142.793 1.00 40.72 ATOM 1818 CB TYR 1111 115.054 36.105 141.731 1.00 42.65 ATOM 1819 CG TYR 1111 116.376 35.699 142.349 1.00 44.83 ATOM 1820 CD1 TYR 1111 116.894 36.390 143.441 1.00 46.11 ATOM 1821 CE1 TYR 1111 118.072 35.980 144.066 1.00 46.16 ATOM 1822 CD2 TYR 1111 117.078 34.586 141.890 1.00 45.77 ATOM 1823 CE2 TYR 1111 118.254 34.172 142.507 1.00 45.94 ATOM 1824 CZ TYR 1111 118.741 34.872 143.595 1.00 46.79 ATOM 1825 OH TYR 1111 119.891 34.454 144.223 1.00 48.18 ATOM 1826 C TYR 1111 112.556 36.205 142.222 1.00 40.96 ATOM 1827 O TYR 1111 112.338 36.113 141.009 1.00 40.93 ATOM 1828 N THR 1112 111.611 36.345 143.150 1.00 40.69 ATOM 1829 CA THR 1112 110.160 36.346 142.909 1.00 41.96 ATOM 1830 CB THR 1112 109.387 37.022 144.083 1.00 42.40 ATOM 1831 OC1 THR 1112 109.881 38.349 144.294 1.00 43.03 ATOM 1832 CG2 THR 1112 109.525 36.206 145.359 1.00 43.31 ATOM 1833 C THR 1112 109.516 36.878 141.630 1.00 41.46 ATOM 1834 O THR 1112 108.302 36.748 141.461 1.00 41.50 ATOM 1835 N SER 1113 110.279 37.476 140.729 1.00 41.45 ATOM 1836 CA SER 1113 109.652 37.967 139.510 1.00 41.57 ATOM 1837 CB SER 1113 109.912 39.459 139.332 1.00 40.56 ATOM 1838 OC SER 1113 109.240 40.186 140.339 1.00 40.01 ATOM 1839 C SER 1113 110.107 37.216 138.278 1.00 42.04 ATOM 1840 O SER 1113 109.700 37.546 137.170 1.00 42.45 ATOM 1841 N TRP 1114 110.943 36.199 138.472 1.00 42.64 ATOM 1842 CA TRP 1114 111.442 35.415 137.348 1.00 42.72 ATOM 1843 CB TRP 1114 112.966 35.412 137.327 1.00 44.69 ATOM 1844 CG TRP 1114 113.565 36.761 137.407 1.00 46.18 ATOM 1845 CD2 TRP 1114 114.924 37.068 137.724 1.00 46.92 ATOM 1846 CE2 TRP 1114 115.052 38.471 137.691 1.00 46.89 ATOM 1847 CE3 TRP 1114 116.050 36.291 138.033 1.00 46.48 ATOM 1848 CD1 TRP 1114 112.939 37.952 137.195 1.00 45.40 ATOM 1849 NE1 TRP 1114 113.824 38.985 137.365 1.00 46.95 ATOM 1850 CZ2 TRP 1114 116.256 39.117 137.959 1.00 46.46 ATOM 1851 CZ3 TRP 1114 117.245 36.929 138.298 1.00 46.25 ATOM 1852 CH2 TRP 1114 117.339 38.329 138.260 1.00 47.38 ATOM 1853 C TRP 1114 110.958 33.976 137.355 1.00 41.32 ATOM 1854 O TRP 1114 110.705 33.391 138.407 1.00 41.19 ATOM 1855 N TYR 1115 110.848 33.402 136.166 1.00 40.12 ATOM 1856 CA TYR 1115 110.392 32.033 136.042 1.00 39.14 ATOM 1857 CB TYR 1115 109.154 31.942 135.155 1.00 40.95 ATOM 1858 CG TYR 1115 107.946 32.713 135.625 1.00 42.57 ATOM 1859 CD1 TYR 1115 107.879 34.097 135.489 1.00 43.25 ATOM 1860 CE1 TYR 1115 106.737 34.801 135.860 1.00 43.70 ATOM 1861 CD2 TYR 1115 106.844 32.052 136.152 1.00 42.47 ATOM 1862 CE2 TYR 1115 105.705 32.741 136.525 1.00 43.45 ATOM 1863 CZ TYR 1115 105.651 34.114 136.377 1.00 43.67 ATOM 1864 OH TYR 1115 104.507 34.794 136.741 1.00 43.60 ATOM 1865 C TYR 1115 111.439 31.139 135.427 1.00 37.49 ATOM 1866 O TYR 1115 112.450 31.602 134.892 1.00 37.76 ATOM 1867 N VAL 1116 111.183 29.841 135.514 1.00 35.40 ATOM 1868 CA VAL 1116 112.061 28.861 134.909 1.00 33.52 ATOM 1869 CB VAL 1116 111.905 27.491 135.565 1.00 31.20 ATOM 1870 CG1 VAL 1116 112.733 26.472 134.837 1.00 30.76 ATOM 1871 CG2 VAL 1116 112.331 27.572 137.002 1.00 31.44 ATOM 1872 C VAL 1116 111.499 28.831 133.497 1.00 33.90 ATOM 1873 O VAL 1116 110.276 28.797 133.309 1.00 33.24 ATOM 1874 N ALA 1117 112.373 28.877 132.500 1.00 33.87 ATOM 1875 CA ALA 1117 111.889 28.885 131.135 1.00 33.71 ATOM 1876 CB ALA 1117 111.443 30.292 130.763 1.00 34.03 ATOM 1877 C ALA 1117 112.892 28.388 130.124 1.00 33.59 ATOM 1878 O ALA 1117 114.093 28.397 130.359 1.00 32.47 ATOM 1879 N LEU 1118 112.375 27.954 128.984 1.00 34.46 ATOM 1880 CA LEU 1118 113.218 27.471 127.912 1.00 36.34 ATOM 1881 CB LEU 1118 112.948 25.988 127.631 1.00 35.80 ATOM 1882 CG LEU 1118 113.447 24.981 128.665 1.00 35.65 ATOM 1883 CD1 LEU 1118 113.236 23.573 128.137 1.00 35.34 ATOM 1884 CD2 LEU 1118 114.919 25.224 128.955 1.00 35.14 ATOM 1885 C LEU 1118 112.944 28.279 126.657 1.00 37.87 ATOM 1886 O LEU 1118 111.819 28.718 126.418 1.00 37.12 ATOM 1887 N LYS 1119 113.989 28.483 125.868 1.00 40.57 ATOM 1888 CA LYS 1119 113.874 29.216 124.621 1.00 43.52 ATOM 1889 CB LYS 1119 115.246 29.756 124.202 1.00 46.49 ATOM 1890 CG LYS 1119 115.889 30.729 125.193 1.00 49.41 ATOM 1891 CD LYS 1119 117.235 31.252 124.667 1.00 51.97 ATOM 1892 CE LYS 1119 118.247 30.117 124.423 1.00 54.07 ATOM 1893 NZ LYS 1119 119.659 30.590 124.192 1.00 53.57 ATOM 1894 C LYS 1119 113.370 28.238 123.571 1.00 43.83 ATOM 1895 O LYS 1119 113.392 27.030 123.789 1.00 43.14 ATOM 1896 N ARG 1120 112.922 28.752 122.433 1.00 45.00 ATOM 1897 CA ARG 1120 112.433 27.891 121.354 1.00 46.36 ATOM 1898 CB ARG 1120 111.674 28.734 120.323 1.00 47.22 ATOM 1899 CG ARG 1120 112.434 29.992 119.949 1.00 47.48 ATOM 1900 CD ARG 1120 111.698 30.906 118.988 1.00 47.23 ATOM 1901 NE ARG 1120 112.375 32.199 118.949 1.00 47.79 ATOM 1902 CZ ARG 1120 112.119 33.166 118.079 1.00 48.69 ATOM 1903 NH1 ARG 1120 111.192 33.001 117.146 1.00 50.68 ATOM 1904 NH2 ARG 1120 112.786 34.307 118.151 1.00 49.30 ATOM 1905 C ARG 1120 113.626 27.224 120.678 1.00 46.59 ATOM 1906 O ARG 1120 113.477 26.494 119.700 1.00 47.90 ATOM 1907 N THR 1121 114.808 27.481 121.220 1.00 45.62 ATOM 1908 CA THR 1121 116.043 26.946 120.685 1.00 45.18 ATOM 1909 CB THR 1121 117.096 28.037 120.658 1.00 47.00 ATOM 1910 OG1 THR 1121 117.243 28.581 121.978 1.00 47.87 ATOM 1911 OG2 THR 1121 116.675 29.144 119.709 1.00 48.44 ATOM 1912 C THR 1121 116.588 25.785 121.505 1.00 44.47 ATOM 1913 O THR 1121 117.621 25.216 121.167 1.00 43.67 ATOM 1914 N GLY 1122 115.914 25.448 122.597 1.00 44.23 ATOM 1915 CA GLY 1122 116.378 24.345 123.420 1.00 44.06 ATOM 1916 C GLY 1122 117.257 24.718 124.603 1.00 44.26 ATOM 1917 O GLY 1122 117.724 23.845 125.336 1.00 43.92 ATOM 1918 N GLN 1123 117.496 26.009 124.792 1.00 44.58 ATOM 1919 CA GLN 1123 118.314 26.462 125.903 1.00 45.08 ATOM 1920 CB GLN 1123 119.447 27.352 125.391 1.00 46.52 ATOM 1921 CG GLN 1123 120.503 26.603 124.608 1.00 48.98 ATOM 1922 CD GLN 1123 121.063 25.421 125.393 1.00 52.53 ATOM 1923 OE1 GLN 1123 121.477 25.561 126.547 1.00 55.31 ATOM 1924 NE2 GLN 1123 121.075 24.250 124.768 1.00 53.43 ATOM 1925 C GLN 1123 117.406 27.237 126.828 1.00 44.24 ATOM 1926 O GLN 1123 116.265 27.733 126.393 1.00 43.79 ATOM 1927 N TYR 1124 117.781 27.351 128.095 1.00 43.32 ATOM 1928 CA TYR 1124 116.926 28.078 129.014 1.00 43.63 ATOM 1929 CB TYR 1124 117.378 27.845 130.444 1.00 43.93 ATOM 1930 CG TYR 1124 118.702 28.462 130.800 1.00 45.08 ATOM 1931 CD1 TYR 1124 118.810 29.834 131.055 1.00 45.15 ATOM 1932 CE1 TYR 1124 120.015 30.398 131.480 1.00 45.60 ATOM 1933 CD2 TYR 1124 119.839 27.664 130.965 1.00 45.30 ATOM 1934 CE2 TYR 1124 121.051 28.217 131.387 1.00 45.76 ATOM 1935 CZ TYR 1124 121.129 29.584 131.647 1.00 45.95 ATOM 1936 OH TYR 1124 122.313 30.125 132.091 1.00 46.50 ATOM 1937 C TYR 1124 116.924 29.561 128.694 1.00 44.09 ATOM 1938 O TYR 1124 117.623 30.007 127.791 1.00 43.93 ATOM 1939 N LYS 1125 116.120 30.318 129.431 1.00 45.08 ATOM 1940 CA LYS 1125 116.021 31.759 129.237 1.00 45.69 ATOM 1941 CB LYS 1125 114.638 32.138 128.757 1.00 47.45 ATOM 1942 CG LYS 1125 114.513 33.591 128.391 1.00 51.87 ATOM 1943 CD LYS 1125 113.087 33.908 127.989 1.00 55.02 ATOM 1944 CE LYS 1125 112.509 32.801 127.120 1.00 56.51 ATOM 1945 NZ LYS 1125 113.491 32.290 126.111 1.00 57.79 ATOM 1946 C LYS 1125 116.270 32.451 130.558 1.00 45.66 ATOM 1947 O LYS 1125 115.652 32.105 131.568 1.00 46.25 ATOM 1948 N LEU 1126 117.166 33.434 130.556 1.00 45.63 ATOM 1949 CA LEU 1126 117.483 34.154 131.779 1.00 44.89 ATOM 1950 CB LEU 1126 118.397 35.337 131.470 1.00 45.08 ATOM 1951 CG LEU 1126 119.805 34.879 131.076 1.00 45.49 ATOM 1952 CD1 LEU 1126 120.710 36.090 130.900 1.00 44.77 ATOM 1953 CD2 LEU 1126 120.363 33.944 132.155 1.00 44.32 ATOM 1954 C LEU 1126 116.223 34.622 132.492 1.00 44.51 ATOM 1955 O LEU 1126 115.379 35.292 131.899 1.00 43.78 ATOM 1956 N GLY 1127 116.092 34.246 133.762 1.00 44.39 ATOM 1957 CA GLY 1127 114.928 34.643 134.529 1.00 44.48 ATOM 1958 C GLY 1127 114.696 36.122 134.340 1.00 45.13 ATOM 1959 O GLY 1127 113.572 36.572 134.144 1.00 45.43 ATOM 1960 N SER 1128 115.783 36.878 134.394 1.00 46.06 ATOM 1961 CA SER 1128 115.741 38.321 134.212 1.00 47.14 ATOM 1962 CB SER 1128 117.170 38.865 134.190 1.00 48.37 ATOM 1963 OG SER 1128 117.981 38.083 133.323 1.00 50.04 ATOM 1964 C SER 1128 115.036 38.702 132.913 1.00 47.38 ATOM 1965 O SER 1128 114.670 39.864 132.717 1.00 48.31 ATOM 1966 N LYS 1129 114.862 37.723 132.027 1.00 47.45 ATOM 1967 CA LYS 1129 114.213 37.934 130.729 1.00 46.81 ATOM 1968 CB LYS 1129 115.068 37.362 129.584 1.00 47.07 ATOM 1969 CG LYS 1129 115.843 38.379 128.751 1.00 47.89 ATOM 1970 CD LYS 1129 115.787 38.062 127.237 1.00 48.45 ATOM 1971 CE LYS 1129 116.364 36.686 126.873 1.00 48.23 ATOM 1972 NZ LYS 1129 116.321 36.413 125.406 1.00 47.29 ATOM 1973 C LYS 1129 112.842 37.271 130.660 1.00 46.09 ATOM 1974 O LYS 1129 112.156 37.379 129.644 1.00 46.51 ATOM 1975 N THR 1130 112.450 36.576 131.725 1.00 44.67 ATOM 1976 CA THR 1130 111.161 35.881 131.754 1.00 43.50 ATOM 1977 CB THR 1130 111.166 34.743 132.768 1.00 44.14 ATOM 1978 OG1 THR 1130 111.272 35.291 134.087 1.00 45.49 ATOM 1979 CG2 THR 1130 112.344 33.816 132.514 1.00 44.12 ATOM 1980 C THR 1130 110.022 36.814 132.117 1.00 41.64 ATOM 1981 O THR 1130 110.242 37.845 132.730 1.00 41.80 ATOM 1982 N GLY 1131 108.804 36.444 131.740 1.00 40.73 ATOM 1983 CA GLY 1131 107.657 37.285 132.032 1.00 40.05 ATOM 1984 C GLY 1131 106.308 36.611 131.838 1.00 40.05 ATOM 1985 O GLY 1131 106.158 35.741 130.979 1.00 39.10 ATOM 1986 N PRO 1132 105.293 37.029 132.611 1.00 40.35 ATOM 1987 CD PRO 1132 105.371 38.307 133.333 1.00 40.07 ATOM 1988 CA PRO 1132 103.908 36.533 132.618 1.00 40.62 ATOM 1989 CB PRO 1132 103.148 37.621 133.373 1.00 39.90 ATOM 1990 CG PRO 1132 103.978 38.841 133.150 1.00 40.34 ATOM 1991 C PRO 1132 103.263 36.203 131.275 1.00 40.73 ATOM 1992 O PRO 1132 102.640 35.151 131.129 1.00 41.94 ATOM 1993 N GLY 1133 103.400 37.086 130.295 1.00 40.65 ATOM 1994 CA GLY 1133 102.800 36.813 129.001 1.00 40.72 ATOM 1995 C GLY 1133 103.587 35.877 128.091 1.00 40.28 ATOM 1996 O GLY 1133 103.111 35.536 127.007 1.00 40.90 ATOM 1997 N GLN 1134 104.771 35.443 128.523 1.00 39.26 ATOM 1998 CA GLN 1134 105.617 34.568 127.708 1.00 38.73 ATOM 1999 CB GLN 1134 107.073 34.670 128.167 1.00 39.96 ATOM 2000 CG GLN 1134 107.705 36.024 127.933 1.00 41.43 ATOM 2001 CD GLN 1134 109.218 35.975 128.005 1.00 42.47 ATOM 2002 OE1 GLN 1134 109.871 35.256 127.237 1.00 43.63 ATOM 2003 NE2 GLN 1134 109.787 36.743 128.924 1.00 42.75 ATOM 2004 C GLN 1134 105.239 33.090 127.630 1.00 38.46 ATOM 2005 O GLN 1134 104.686 32.513 128.576 1.00 38.92 ATOM 2006 N LYS 1135 105.570 32.491 126.487 1.00 37.04 ATOM 2007 CA LYS 1135 105.315 31.086 126.197 1.00 35.96 ATOM 2008 CB LYS 1135 105.212 30.899 124.679 1.00 36.41 ATOM 2009 CG LYS 1135 105.119 29.460 124.192 1.00 38.29 ATOM 2010 CD LYS 1135 105.087 29.400 122.659 1.00 39.86 ATOM 2011 CE LYS 1135 105.142 27.959 122.134 1.00 39.82 ATOM 2012 NZ LYS 1135 105.459 27.863 120.671 1.00 39.42 ATOM 2013 C LYS 1135 106.443 30.226 126.761 1.00 35.48 ATOM 2014 O LYS 1135 106.263 29.034 126.997 1.00 35.40 ATOM 2015 N ALA 1136 107.602 30.834 126.992 1.00 34.91 ATOM 2016 CA ALA 1136 108.746 30.091 127.518 1.00 34.69 ATOM 2017 CB ALA 1136 110.020 30.921 127.415 1.00 34.51 ATOM 2018 C ALA 1136 108.558 29.619 128.953 1.00 33.97 ATOM 2019 O ALA 1136 109.147 28.619 129.357 1.00 33.77 ATOM 2020 N ILE 1137 107.733 30.334 129.710 1.00 32.70 ATOM 2021 CA ILE 1137 107.476 30.010 131.113 1.00 32.21 ATOM 2022 CB ILE 1137 106.915 31.254 131.857 1.00 31.38 ATOM 2023 CG2 ILE 1137 107.975 32.348 131.928 1.00 30.84 ATOM 2024 CG1 ILE 1137 105.645 31.745 131.146 1.00 30.94 ATOM 2025 CD1 ILE 1137 104.820 32.734 131.927 1.00 29.44 ATOM 2026 C ILE 1137 106.491 28.857 131.361 1.00 31.36 ATOM 2027 O ILE 1137 106.534 28.202 132.403 1.00 32.48 ATOM 2028 N LEU 1138 105.609 28.616 130.404 1.00 29.32 ATOM 2029 CA LEU 1138 104.588 27.597 130.554 1.00 28.65 ATOM 2030 CB LEU 1138 103.480 27.870 129.540 1.00 29.90 ATOM 2031 CG LEU 1138 103.086 29.350 129.460 1.00 29.89 ATOM 2032 CD1 LEU 1138 102.268 29.600 128.209 1.00 28.56 ATOM 2033 CD2 LEU 1138 102.333 29.759 130.730 1.00 29.29 ATOM 2034 C LEU 1138 105.090 26.172 130.414 1.00 28.55 ATOM 2035 O LEU 1138 105.711 25.822 129.413 1.00 30.20 ATOM 2036 N PHE 1139 104.822 25.344 131.420 1.00 27.45 ATOM 2037 CA PHE 1139 105.247 23.948 131.368 1.00 26.67 ATOM 2038 CB PHE 1139 106.353 23.650 132.377 1.00 27.49 ATOM 2039 CG PHE 1139 107.670 24.280 132.044 1.00 27.20 ATOM 2040 CD1 PHE 1139 107.893 25.630 132.299 1.00 25.89 ATOM 2041 CD2 PHE 1139 108.690 23.518 131.483 1.00 27.89 ATOM 2042 CE1 PHE 1139 109.101 26.212 132.011 1.00 26.60 ATOM 2043 CE2 PHE 1139 109.913 24.088 131.184 1.00 28.43 ATOM 2044 CZ PHE 1139 110.123 25.443 131.450 1.00 28.31 ATOM 2045 C PHE 1139 104.094 23.003 131.624 1.00 25.43 ATOM 2046 O PHE 1139 103.171 23.315 132.368 1.00 24.30 ATOM 2047 N LEU 1140 104.166 21.832 131.009 1.00 24.47 ATOM 2048 CA LEU 1140 103.123 20.840 131.156 1.00 23.19 ATOM 2049 CB LEU 1140 102.554 20.497 129.783 1.00 22.43 ATOM 2050 CG LEU 1140 101.042 20.378 129.638 1.00 22.70 ATOM 2051 CD1 LEU 1140 100.347 21.532 130.323 1.00 22.43 ATOM 2052 CD2 LEU 1140 100.702 20.368 128.155 1.00 23.99 ATOM 2053 C LEU 1140 103.708 19.609 131.810 1.00 23.00 ATOM 2054 O LEU 1140 104.572 18.943 131.252 1.00 24.30 ATOM 2055 N PRO 1141 103.263 19.302 133.027 1.00 22.81 ATOM 2056 CD PRO 1141 102.349 20.065 133.894 1.00 22.88 ATOM 2057 CA PRO 1141 103.777 18.126 133.721 1.00 22.66 ATOM 2058 CB PRO 1141 103.290 18.344 135.151 1.00 22.42 ATOM 2059 CG PRO 1141 102.003 19.050 134.960 1.00 22.65 ATOM 2060 C PRO 1141 103.237 16.840 133.103 1.00 23.04 ATOM 2061 O PRO 1141 102.044 16.719 132.832 1.00 21.39 ATOM 2062 N MET 1142 104.125 15.881 132.896 1.00 24.58 ATOM 2063 CA MET 1142 103.757 14.606 132.310 1.00 26.08 ATOM 2064 CB MET 1142 104.282 14.537 130.889 1.00 24.74 ATOM 2065 CG MET 1142 103.748 15.661 130.039 1.00 23.66 ATOM 2066 SD MET 1142 104.337 15.545 128.375 1.00 25.16 ATOM 2067 CE MET 1142 103.295 14.240 127.721 1.00 24.74 ATOM 2068 C MET 1142 104.311 13.457 133.129 1.00 27.87 ATOM 2069 O MET 1142 105.429 13.518 133.635 1.00 28.66 ATOM 2070 N SER 1143 103.520 12.401 133.246 1.00 30.37 ATOM 2071 CA SER 1143 103.892 11.233 134.025 1.00 31.39 ATOM 2072 CB SER 1143 102.731 10.252 134.044 1.00 32.34 ATOM 2073 OG SER 1143 102.373 9.911 132.717 1.00 32.97 ATOM 2074 C SER 1143 105.138 10.521 133.522 1.00 32.02 ATOM 2075 O SER 1143 105.568 10.697 132.379 1.00 30.87 ATOM 2076 N ALA 1144 105.704 9.700 134.402 1.00 32.96 ATOM 2077 CA ALA 1144 106.893 8.925 134.089 1.00 33.67 ATOM 2078 CB ALA 1144 108.129 9.807 134.174 1.00 33.96 ATOM 2079 C ALA 1144 107.007 7.748 135.057 1.00 34.12 ATOM 2080 O ALA 1144 106.518 6.656 134.683 1.00 32.94 ATOM 2081 CB MET 2149 101.053 53.171 93.062 1.00 57.58 ATOM 2082 CG MET 2149 99.622 52.593 93.151 1.00 59.75 ATOM 2083 SD MET 2149 98.295 53.481 92.279 1.00 60.90 ATOM 2084 CE MET 2149 98.247 52.549 90.723 1.00 59.28 ATOM 2085 C MET 2149 100.602 54.176 95.322 1.00 55.07 ATOM 2086 O MET 2149 100.145 53.082 95.647 1.00 55.37 ATOM 2087 N MET 2149 102.837 54.415 94.242 1.00 56.18 ATOM 2088 CA MET 2149 101.360 54.347 94.000 1.00 56.33 ATOM 2089 N PRO 2150 100.451 55.262 96.097 1.00 53.63 ATOM 2090 CD PRO 2150 100.990 56.605 95.830 1.00 53.80 ATOM 2091 CA PRO 2150 99.753 55.236 97.389 1.00 52.35 ATOM 2092 CB PRO 2150 99.719 56.709 97.792 1.00 52.99 ATOM 2093 CG PRO 2150 100.984 57.228 97.216 1.00 53.82 ATOM 2094 C PRO 2150 98.359 54.618 97.391 1.00 50.70 ATOM 2095 O PRO 2150 97.569 54.821 96.467 1.00 50.65 ATOM 2096 N VAL 2151 98.073 53.870 98.453 1.00 49.03 ATOM 2097 CA VAL 2151 96.785 53.209 98.643 1.00 47.15 ATOM 2098 CB VAL 2151 96.776 51.794 98.067 1.00 47.39 ATOM 2099 CG1 VAL 2151 95.359 51.234 98.121 1.00 47.16 ATOM 2100 CG2 VAL 2151 97.330 51.800 96.653 1.00 48.15 ATOM 2101 C VAL 2151 96.506 53.065 100.125 1.00 45.27 ATOM 2102 O VAL 2151 97.367 52.602 100.875 1.00 44.84 ATOM 2103 N ALA 2152 95.306 53.448 100.546 1.00 43.54 ATOM 2104 CA ALA 2152 94.938 53.336 101.953 1.00 43.04 ATOM 2105 CB ALA 2152 93.699 54.174 102.247 1.00 42.03 ATOM 2106 C ALA 2152 94.684 51.872 102.315 1.00 42.13 ATOM 2107 O ALA 2152 94.254 51.077 101.481 1.00 42.41 ATOM 2108 N PRO 2153 94.960 51.490 103.564 1.00 41.04 ATOM 2109 CD PRO 2153 95.360 52.284 104.734 1.00 41.11 ATOM 2110 CA PRO 2153 94.726 50.099 103.936 1.00 40.71 ATOM 2111 CB PRO 2153 95.118 50.066 105.408 1.00 40.77 ATOM 2112 CG PRO 2153 94.820 51.449 105.862 1.00 41.38 ATOM 2113 C PRO 2153 93.280 49.704 103.691 1.00 40.37 ATOM 2114 O PRO 2153 92.366 50.478 103.947 1.00 40.64 ATOM 2115 N TYR 2154 93.080 48.497 103.180 1.00 39.94 ATOM 2116 CA TYR 2154 91.740 48.016 102.894 1.00 40.42 ATOM 2117 CB TYR 2154 91.394 48.289 101.428 1.00 42.56 ATOM 2118 CG TYR 2154 92.311 47.597 100.447 1.00 45.15 ATOM 2119 CD1 TYR 2154 93.656 47.944 100.357 1.00 46.86 ATOM 2120 CE1 TYR 2154 94.518 47.266 99.494 1.00 48.33 ATOM 2121 CD2 TYR 2154 91.845 46.559 99.642 1.00 45.83 ATOM 2122 CE2 TYR 2154 92.697 45.876 98.775 1.00 46.76 ATOM 2123 CZ TYR 2154 94.030 46.230 98.711 1.00 47.85 ATOM 2124 OH TYR 2154 94.884 45.524 97.898 1.00 49.09 ATOM 2125 C TYR 2154 91.593 46.523 103.195 1.00 39.88 ATOM 2126 O TYR 2154 92.564 45.766 103.153 1.00 38.80 ATOM 2127 N TRP 2155 90.367 46.110 103.499 1.00 38.54 ATOM 2128 CA TRP 2155 90.070 44.724 103.809 1.00 37.07 ATOM 2129 CB TRP 2155 88.639 44.624 104.319 1.00 35.60 ATOM 2130 CG TRP 2155 88.409 45.458 105.518 1.00 34.08 ATOM 2131 CD2 TRP 2155 89.249 45.540 106.672 1.00 33.12 ATOM 2132 CE2 TRP 2155 88.632 46.434 107.574 1.00 33.83 ATOM 2133 CE3 TRP 2155 90.462 44.945 107.035 1.00 32.00 ATOM 2134 CD1 TRP 2155 87.348 46.282 105.753 1.00 33.78 ATOM 2135 NE1 TRP 2155 87.473 46.872 106.986 1.00 33.15 ATOM 2136 CZ2 TRP 2155 89.191 46.745 108.823 1.00 33.85 ATOM 2137 CZ3 TRP 2155 91.017 45.256 108.272 1.00 32.16 ATOM 2138 CH2 TRP 2155 90.381 46.148 109.151 1.00 32.30 ATOM 2139 C TRP 2155 90.219 43.879 102.557 1.00 37.57 ATOM 2140 O TRP 2155 89.580 44.161 101.544 1.00 37.17 ATOM 2141 N THR 2156 91.053 42.845 102.623 1.00 37.89 ATOM 2142 CA THR 2156 91.263 41.963 101.479 1.00 38.70 ATOM 2143 CB THR 2156 92.707 41.387 101.449 1.00 38.01 ATOM 2144 OG1 THR 2156 92.982 40.682 102.665 1.00 36.69 ATOM 2145 CG2 THR 2156 93.720 42.496 101.295 1.00 38.03 ATOM 2146 C THR 2156 90.272 40.806 101.485 1.00 40.73 ATOM 2147 O THR 2156 89.873 40.329 100.434 1.00 40.95 ATOM 2148 N SER 2157 89.875 40.359 102.673 1.00 43.95 ATOM 2149 CA SER 2157 88.920 39.254 102.812 1.00 47.06 ATOM 2150 CB SER 2157 89.622 38.009 103.352 1.00 46.16 ATOM 2151 OG SER 2157 90.642 37.586 102.471 1.00 46.00 ATOM 2152 C SER 2157 87.819 39.678 103.774 1.00 49.00 ATOM 2153 O SER 2157 87.689 39.143 104.869 1.00 49.66 ATOM 2154 N PRO 2158 86.992 40.631 103.353 1.00 50.85 ATOM 2155 CD PRO 2158 86.797 40.916 101.923 1.00 51.12 ATOM 2156 CA PRO 2158 85.883 41.179 104.131 1.00 52.38 ATOM 2157 CB PRO 2158 85.188 42.080 103.130 1.00 52.28 ATOM 2158 CG PRO 2158 85.334 41.288 101.877 1.00 52.37 ATOM 2159 C PRO 2158 84.922 40.154 104.692 1.00 53.86 ATOM 2160 O PRO 2158 84.401 40.326 105.796 1.00 53.93 ATOM 2161 N GLU 2159 84.682 39.095 103.921 1.00 55.27 ATOM 2162 CA GLU 2159 83.731 38.062 104.322 1.00 56.66 ATOM 2163 CB GLU 2159 83.480 37.080 103.172 1.00 58.65 ATOM 2164 CG GLU 2159 82.250 36.186 103.394 1.00 62.88 ATOM 2165 CD GLU 2159 81.955 35.237 102.220 1.00 65.39 ATOM 2166 OE1 GLU 2159 81.698 35.732 101.095 1.00 65.81 ATOM 2167 OE2 GLU 2159 81.977 33.995 102.422 1.00 66.67 ATOM 2168 C GLU 2159 84.132 37.296 105.567 1.00 56.11 ATOM 2169 O GLU 2159 83.274 36.950 106.384 1.00 56.78 ATOM 2170 N LYS 2160 85.423 37.025 105.721 1.00 54.57 ATOM 2171 CA LYS 2160 85.854 36.311 106.908 1.00 53.84 ATOM 2172 CB LYS 2160 87.172 35.567 106.657 1.00 55.32 ATOM 2173 CG LYS 2160 88.375 36.432 106.353 1.00 57.32 ATOM 2174 CD LYS 2160 89.645 35.584 106.283 1.00 57.82 ATOM 2175 CE LYS 2160 89.594 34.570 105.150 1.00 59.01 ATOM 2176 NZ LYS 2160 90.778 33.672 105.173 1.00 62.14 ATOM 2177 C LYS 2160 85.966 37.257 108.113 1.00 52.94 ATOM 2178 O LYS 2160 86.763 37.041 109.029 1.00 52.74 ATOM 2179 N MET 2161 85.144 38.304 108.104 1.00 51.47 ATOM 2180 CA MET 2161 85.104 39.283 109.187 1.00 49.13 ATOM 2181 CB MET 2161 85.700 40.610 108.736 1.00 49.15 ATOM 2182 CG MET 2161 87.121 40.500 108.241 1.00 49.16 ATOM 2183 SD MET 2161 87.834 42.120 107.942 1.00 49.46 ATOM 2184 CE MET 2161 88.397 42.506 109.578 1.00 50.63 ATOM 2185 C MET 2161 83.650 39.484 109.569 1.00 47.71 ATOM 2186 O MET 2161 83.321 40.305 110.422 1.00 46.77 ATOM 2187 N GLU 2162 82.789 38.707 108.928 1.00 46.49 ATOM 2188 CA GLU 2162 81.362 38.763 109.154 1.00 46.30 ATOM 2189 CB GLU 2162 80.680 37.832 108.164 1.00 48.00 ATOM 2190 CG GLU 2162 79.214 38.119 107.992 1.00 51.96 ATOM 2191 CD GLU 2162 78.966 39.454 107.321 1.00 54.10 ATOM 2192 OE1 GLU 2162 79.457 40.479 107.846 1.00 55.94 ATOM 2193 OE2 GLU 2162 78.284 39.475 106.268 1.00 56.14 ATOM 2194 C GLU 2162 80.944 38.398 110.582 1.00 45.40 ATOM 2195 O GLU 2162 80.121 39.081 111.190 1.00 45.60 ATOM 2196 N LYS 2163 81.506 37.319 111.118 1.00 44.38 ATOM 2197 CA LYS 2163 81.153 36.896 112.468 1.00 42.97 ATOM 2198 CB LYS 2163 81.607 35.459 112.747 1.00 43.63 ATOM 2199 CG LYS 2163 81.071 34.923 114.078 1.00 43.85 ATOM 2200 CD LYS 2163 81.675 33.576 114.468 1.00 44.67 ATOM 2201 CE LYS 2163 83.171 33.672 114.728 1.00 44.08 ATOM 2202 NZ LYS 2163 83.546 34.722 115.741 1.00 45.08 ATOM 2203 C LYS 2163 81.759 37.817 113.511 1.00 42.14 ATOM 2204 O LYS 2163 82.889 37.607 113.956 1.00 41.65 ATOM 2205 N LYS 2164 80.993 38.830 113.911 1.00 41.38 ATOM 2206 CA LYS 2164 81.459 39.791 114.907 1.00 40.83 ATOM 2207 CB LYS 2164 80.715 41.121 114.766 1.00 42.68 ATOM 2208 CG LYS 2164 81.076 41.904 113.502 1.00 45.26 ATOM 2209 CD LYS 2164 81.126 43.406 113.792 1.00 47.67 ATOM 2210 CE LYS 2164 81.036 44.253 112.519 1.00 47.25 ATOM 2211 NZ LYS 2164 79.682 44.252 111.886 1.00 48.33 ATOM 2212 C LYS 2164 81.372 39.314 116.354 1.00 39.23 ATOM 2213 O LYS 2164 82.065 39.846 117.222 1.00 39.43 ATOM 2214 N LEU 2165 80.522 38.324 116.619 1.00 36.91 ATOM 2215 CA LEU 2165 80.391 37.790 117.969 1.00 33.81 ATOM 2216 CB LEU 2165 78.939 37.752 118.420 1.00 32.68 ATOM 2217 CG LEU 2165 78.777 36.988 119.740 1.00 30.79 ATOM 2218 CD1 LEU 2165 79.495 37.744 120.834 1.00 29.86 ATOM 2219 CD2 LEU 2165 77.310 36.829 120.098 1.00 29.83 ATOM 2220 C LEU 2165 80.925 36.382 118.059 1.00 32.95 ATOM 2221 O LEU 2165 80.433 35.485 117.381 1.00 31.95 ATOM 2222 N HIS 2166 81.929 36.184 118.902 1.00 32.94 ATOM 2223 CA HIS 2166 82.482 34.863 119.074 1.00 33.18 ATOM 2224 CB HIS 2166 83.967 34.837 118.748 1.00 38.15 ATOM 2225 CG HIS 2166 84.471 33.461 118.447 1.00 44.40 ATOM 2226 CD2 HIS 2166 83.813 32.337 118.067 1.00 45.92 ATOM 2227 ND1 HIS 2166 85.801 33.110 118.548 1.00 47.16 ATOM 2228 CE1 HIS 2166 85.940 31.829 118.249 1.00 48.42 ATOM 2229 NE2 HIS 2166 84.748 31.337 117.953 1.00 47.24 ATOM 2230 C HIS 2166 82.249 34.367 120.487 1.00 30.67 ATOM 2231 O HIS 2166 82.909 34.791 121.428 1.00 29.79 ATOM 2232 N ALA 2167 81.281 33.469 120.625 1.00 29.14 ATOM 2233 CA ALA 2167 80.946 32.898 121.914 1.00 27.52 ATOM 2234 CB ALA 2167 79.423 32.832 122.095 1.00 26.36 ATOM 2235 C ALA 2167 81.553 31.511 121.912 1.00 26.95 ATOM 2236 O ALA 2167 81.368 30.742 120.965 1.00 26.26 ATOM 2237 N VAL 2168 82.294 31.206 122.971 1.00 25.92 ATOM 2238 CA VAL 2168 82.954 29.921 123.100 1.00 24.85 ATOM 2239 CB VAL 2168 84.389 30.007 122.556 1.00 25.27 ATOM 2240 CG1 VAL 2168 84.377 30.434 121.101 1.00 25.08 ATOM 2241 CG2 VAL 2168 85.198 30.996 123.390 1.00 24.21 ATOM 2242 C VAL 2168 83.058 29.492 124.559 1.00 24.37 ATOM 2243 O VAL 2168 82.950 30.312 125.465 1.00 24.58 ATOM 2244 N PRO 2169 83.241 28.186 124.805 1.00 23.79 ATOM 2245 CD PRO 2169 83.022 27.050 123.895 1.00 22.95 ATOM 2246 CA PRO 2169 83.371 27.732 126.193 1.00 23.24 ATOM 2247 CB PRO 2169 83.049 26.241 126.097 1.00 21.71 ATOM 2248 CG PRO 2169 83.503 25.889 124.721 1.00 22.73 ATOM 2249 C PRO 2169 84.826 28.019 126.581 1.00 23.62 ATOM 2250 O PRO 2169 85.687 28.147 125.709 1.00 22.49 ATOM 2251 N ALA 2170 85.110 28.121 127.873 1.00 24.54 ATOM 2252 CA ALA 2170 86.466 28.446 128.309 1.00 25.37 ATOM 2253 CB ALA 2170 86.532 28.488 129.830 1.00 25.45 ATOM 2254 C ALA 2170 87.523 27.504 127.781 1.00 25.81 ATOM 2255 O ALA 2170 87.228 26.370 127.423 1.00 26.77 ATOM 2256 N ALA 2171 88.756 28.001 127.749 1.00 26.06 ATOM 2257 CA ALA 2171 89.933 27.266 127.302 1.00 26.68 ATOM 2258 CB ALA 2171 89.954 25.877 127.885 1.00 26.19 ATOM 2259 C ALA 2171 90.058 27.185 125.806 1.00 28.23 ATOM 2260 O ALA 2171 91.168 27.056 125.275 1.00 29.90 ATOM 2261 N LYS 2172 88.937 27.256 125.108 1.00 28.87 ATOM 2262 CA LYS 2172 89.016 27.164 123.664 1.00 29.95 ATOM 2263 CB LYS 2172 87.632 27.295 123.034 1.00 31.07 ATOM 2264 CG LYS 2172 87.607 26.846 121.584 1.00 32.86 ATOM 2265 CD LYS 2172 86.196 26.624 121.097 1.00 33.53 ATOM 2266 CE LYS 2172 86.242 26.136 119.681 1.00 34.62 ATOM 2267 NZ LYS 2172 87.076 27.064 118.858 1.00 37.40 ATOM 2268 C LYS 2172 89.950 28.256 123.159 1.00 29.64 ATOM 2269 O LYS 2172 90.022 29.327 123.749 1.00 29.37 ATOM 2270 N THR 2173 90.693 27.960 122.096 1.00 29.36 ATOM 2271 CA THR 2173 91.616 28.929 121.503 1.00 28.42 ATOM 2272 CB THR 2173 92.679 28.248 120.603 1.00 28.14 ATOM 2273 OG1 THR 2173 93.569 27.471 121.407 1.00 29.92 ATOM 2274 CG2 THR 2173 93.474 29.277 119.831 1.00 26.11 ATOM 2275 C THR 2173 90.814 29.856 120.610 1.00 28.51 ATOM 2276 O THR 2173 89.989 29.402 119.815 1.00 27.97 ATOM 2277 N VAL 2174 91.054 31.154 120.737 1.00 29.34 ATOM 2278 CA VAL 2174 90.340 32.124 119.921 1.00 30.30 ATOM 2279 CB VAL 2174 89.595 33.149 120.781 1.00 30.41 ATOM 2280 CG1 VAL 2174 88.985 34.203 119.892 1.00 31.26 ATOM 2281 CG2 VAL 2174 88.512 32.463 121.584 1.00 30.49 ATOM 2282 C VAL 2174 91.312 32.875 119.037 1.00 30.86 ATOM 2283 O VAL 2174 92.387 33.259 119.476 1.00 31.22 ATOM 2284 N LYS 2175 90.911 33.086 117.792 1.00 31.57 ATOM 2285 CA LYS 2175 91.727 33.785 116.816 1.00 33.31 ATOM 2286 CB LYS 2175 92.308 32.771 115.823 1.00 35.27 ATOM 2287 CG LYS 2175 92.892 33.378 114.550 1.00 38.22 ATOM 2288 CD LYS 2175 93.420 32.294 113.610 1.00 41.78 ATOM 2289 CE LYS 2175 94.239 32.888 112.452 1.00 44.24 ATOM 2290 NZ LYS 2175 94.879 31.850 111.566 1.00 45.00 ATOM 2291 C LYS 2175 90.878 34.807 116.061 1.00 34.00 ATOM 2292 O LYS 2175 89.881 34.445 115.437 1.00 33.89 ATOM 2293 N PHE 2176 91.272 36.078 116.128 1.00 34.33 ATOM 2294 CA PHE 2176 90.570 37.154 115.428 1.00 34.12 ATOM 2295 CB PHE 2176 90.262 38.304 116.389 1.00 32.91 ATOM 2296 CG PHE 2176 89.290 37.946 117.466 1.00 31.94 ATOM 2297 CD1 PHE 2176 87.994 37.574 117.152 1.00 30.90 ATOM 2298 CD2 PHE 2176 89.671 37.971 118.797 1.00 31.99 ATOM 2299 CE1 PHE 2176 87.091 37.231 118.148 1.00 31.11 ATOM 2300 CE2 PHE 2176 88.770 37.626 119.806 1.00 31.88 ATOM 2301 CZ PHE 2176 87.479 37.255 119.478 1.00 30.39 ATOM 2302 C PHE 2176 91.485 37.652 114.318 1.00 34.66 ATOM 2303 O PHE 2176 92.662 37.941 114.570 1.00 34.60 ATOM 2304 N LYS 2177 90.956 37.753 113.099 1.00 34.79 ATOM 2305 CA LYS 2177 91.759 38.212 111.967 1.00 35.78 ATOM 2306 CB LYS 2177 91.971 37.064 110.980 1.00 36.77 ATOM 2307 CG LYS 2177 90.722 36.268 110.696 1.00 39.23 ATOM 2308 CD LYS 2177 91.062 34.929 110.073 1.00 41.52 ATOM 2309 CE LYS 2177 89.818 34.068 109.929 1.00 44.06 ATOM 2310 NZ LYS 2177 90.138 32.776 109.261 1.00 45.50 ATOM 2311 C LYS 2177 91.181 39.408 111.231 1.00 35.77 ATOM 2312 O LYS 2177 89.969 39.596 111.179 1.00 35.34 ATOM 2313 N CYS 2178 92.070 40.219 110.668 1.00 35.64 ATOM 2314 CA CYS 2178 91.669 41.396 109.915 1.00 35.78 ATOM 2315 C CYS 2178 92.463 41.503 108.623 1.00 37.33 ATOM 2316 O CYS 2178 93.258 42.428 108.432 1.00 37.67 ATOM 2317 CB CYS 2178 91.852 42.656 110.752 1.00 34.60 ATOM 2318 SG CYS 2178 90.535 42.925 111.984 1.00 35.18 ATOM 2319 N PRO 2179 92.247 40.548 107.711 1.00 38.50 ATOM 2320 CD PRO 2179 91.225 39.495 107.822 1.00 39.46 ATOM 2321 CA PRO 2179 92.911 40.480 106.410 1.00 39.04 ATOM 2322 CB PRO 2179 92.131 39.394 105.680 1.00 39.14 ATOM 2323 CG PRO 2179 91.673 38.511 106.779 1.00 39.46 ATOM 2324 C PRO 2179 92.763 41.801 105.706 1.00 39.02 ATOM 2325 O PRO 2179 91.650 42.181 105.358 1.00 39.25 ATOM 2326 N SER 2180 93.878 42.491 105.498 1.00 39.35 ATOM 2327 CA SER 2180 93.862 43.775 104.815 1.00 40.27 ATOM 2328 CB SER 2180 93.639 44.898 105.826 1.00 38.75 ATOM 2329 OG SER 2180 94.704 44.963 106.746 1.00 37.59 ATOM 2330 C SER 2180 95.163 44.019 104.054 1.00 41.09 ATOM 2331 O SER 2180 96.146 43.309 104.248 1.00 41.62 ATOM 2332 N SER 2181 95.153 45.025 103.184 1.00 41.78 ATOM 2333 CA SER 2181 96.323 45.391 102.390 1.00 42.47 ATOM 2334 CB SER 2181 96.303 44.688 101.032 1.00 41.93 ATOM 2335 OG SER 2181 96.561 43.307 101.165 1.00 43.05 ATOM 2336 C SER 2181 96.353 46.891 102.153 1.00 43.03 ATOM 2337 O SER 2181 95.466 47.622 102.589 1.00 43.52 ATOM 2338 N GLY 2182 97.371 47.344 101.435 1.00 43.41 ATOM 2339 CA GLY 2182 97.487 48.759 101.152 1.00 44.12 ATOM 2340 C GLY 2182 98.941 49.155 101.091 1.00 44.00 ATOM 2341 O GLY 2182 99.760 48.631 101.837 1.00 44.97 ATOM 2342 N THR 2183 99.268 50.089 100.210 1.00 43.66 ATOM 2343 CA THR 2183 100.646 50.514 100.058 1.00 42.77 ATOM 2344 CB THR 2183 101.111 50.256 98.634 1.00 41.91 ATOM 2345 OG1 THR 2183 100.517 51.224 97.769 1.00 41.95 ATOM 2346 CG2 THR 2183 100.673 48.865 98.183 1.00 41.42 ATOM 2347 C THR 2183 100.835 51.989 100.391 1.00 42.68 ATOM 2348 O THR 2183 100.083 52.841 99.928 1.00 43.54 ATOM 2349 N PRO 2184 101.841 52.305 101.217 1.00 41.92 ATOM 2350 CD PRO 2184 102.188 53.676 101.616 1.00 41.42 ATOM 2351 CA PRO 2184 102.767 51.343 101.820 1.00 41.86 ATOM 2352 CB PRO 2184 103.800 52.240 102.494 1.00 41.71 ATOM 2353 CG PRO 2184 103.000 53.442 102.863 1.00 41.80 ATOM 2354 C PRO 2184 102.083 50.402 102.811 1.00 41.92 ATOM 2355 O PRO 2184 101.066 50.753 103.414 1.00 42.43 ATOM 2356 N GLN 2185 102.651 49.210 102.962 1.00 40.80 ATOM 2357 CA GLN 2185 102.132 48.191 103.867 1.00 40.57 ATOM 2358 CB GLN 2185 103.230 47.171 104.158 1.00 40.77 ATOM 2359 CG GLN 2185 102.746 45.902 104.792 1.00 40.48 ATOM 2360 CD GLN 2185 101.819 45.131 103.878 1.00 41.61 ATOM 2361 OE1 GLN 2185 101.392 44.028 104.212 1.00 43.14 ATOM 2362 NE2 GLN 2185 101.497 45.705 102.720 1.00 40.31 ATOM 2363 C GLN 2185 101.643 48.784 105.187 1.00 40.32 ATOM 2364 O GLN 2185 102.407 49.433 105.902 1.00 41.24 ATOM 2365 N PRO 2186 100.360 48.569 105.529 1.00 39.44 ATOM 2366 CD PRO 2186 99.262 48.067 104.684 1.00 39.20 ATOM 2367 CA PRO 2186 99.851 49.121 106.790 1.00 38.75 ATOM 2368 CB PRO 2186 98.334 49.118 106.586 1.00 38.97 ATOM 2369 CG PRO 2186 98.123 47.966 105.662 1.00 39.83 ATOM 2370 C PRO 2186 100.293 48.343 108.024 1.00 37.46 ATOM 2371 O PRO 2186 100.662 47.172 107.939 1.00 38.41 ATOM 2372 N THR 2187 100.283 49.017 109.165 1.00 36.11 ATOM 2373 CA THR 2187 100.667 48.407 110.432 1.00 35.86 ATOM 2374 CB THR 2187 101.258 49.448 111.378 1.00 36.05 ATOM 2375 OG1 THR 2187 100.284 50.475 111.622 1.00 35.43 ATOM 2376 CG2 THR 2187 102.499 50.062 110.771 1.00 35.70 ATOM 2377 C THR 2187 99.419 47.825 111.097 1.00 35.74 ATOM 2378 O THR 2187 98.309 48.332 110.902 1.00 36.38 ATOM 2379 N LEU 2188 99.606 46.779 111.898 1.00 34.42 ATOM 2380 CA LEU 2188 98.490 46.120 112.574 1.00 33.53 ATOM 2381 CB LEU 2188 98.435 44.643 112.171 1.00 32.39 ATOM 2382 CG LEU 2188 97.143 43.839 112.361 1.00 32.55 ATOM 2383 CD1 LEU 2188 97.476 42.351 112.346 1.00 31.88 ATOM 2384 CD2 LEU 2188 96.459 44.208 113.655 1.00 32.73 ATOM 2385 C LEU 2188 98.615 46.193 114.094 1.00 33.67 ATOM 2386 O LEU 2188 99.650 45.836 114.656 1.00 34.52 ATOM 2387 N ARG 2189 97.566 46.652 114.764 1.00 32.45 ATOM 2388 CA ARG 2189 97.601 46.705 116.213 1.00 31.36 ATOM 2389 CB ARG 2189 98.046 48.098 116.694 1.00 30.49 ATOM 2390 CG ARG 2189 97.078 49.248 116.499 1.00 31.19 ATOM 2391 CD ARG 2189 97.797 50.576 116.766 1.00 32.99 ATOM 2392 NE ARG 2189 96.896 51.703 117.021 1.00 34.94 ATOM 2393 CZ ARG 2189 96.462 52.050 118.232 1.00 36.42 ATOM 2394 NH1 ARG 2189 96.857 51.349 119.289 1.00 37.29 ATOM 2395 NH2 ARG 2189 95.639 53.090 118.397 1.00 35.50 ATOM 2396 C ARG 2189 96.226 46.303 116.751 1.00 31.00 ATOM 2397 O ARG 2189 95.225 46.406 116.037 1.00 31.19 ATOM 2398 N TRP 2190 96.173 45.813 117.988 1.00 29.63 ATOM 2399 CA TRP 2190 94.905 45.382 118.571 1.00 28.95 ATOM 2400 CB TRP 2190 94.941 43.885 118.851 1.00 27.63 ATOM 2401 CG TRP 2190 94.984 43.058 117.625 1.00 27.16 ATOM 2402 CD2 TRP 2190 93.861 42.498 116.935 1.00 27.28 ATOM 2403 CE2 TRP 2190 94.366 41.822 115.797 1.00 28.20 ATOM 2404 CE3 TRP 2190 92.476 42.502 117.165 1.00 25.80 ATOM 2405 CD1 TRP 2190 96.086 42.713 116.907 1.00 27.06 ATOM 2406 NE1 TRP 2190 95.728 41.969 115.807 1.00 27.55 ATOM 2407 CZ2 TRP 2190 93.531 41.151 114.883 1.00 28.99 ATOM 2408 CZ3 TRP 2190 91.644 41.835 116.258 1.00 26.84 ATOM 2409 CH2 TRP 2190 92.177 41.168 115.129 1.00 27.57 ATOM 2410 C TRP 2190 94.509 46.108 119.841 1.00 29.55 ATOM 2411 O TRP 2190 95.359 46.620 120.567 1.00 30.93 ATOM 2412 N LEU 2191 93.210 46.131 120.116 1.00 29.19 ATOM 2413 CA LEU 2191 92.697 46.803 121.304 1.00 30.59 ATOM 2414 CB LEU 2191 92.063 48.138 120.935 1.00 29.16 ATOM 2415 CG LEU 2191 92.931 49.249 120.379 1.00 27.44 ATOM 2416 CD1 LEU 2191 92.052 50.472 120.222 1.00 25.74 ATOM 2417 CD2 LEU 2191 94.104 49.521 121.308 1.00 27.11 ATOM 2418 C LEU 2191 91.646 46.001 122.049 1.00 32.08 ATOM 2419 O LEU 2191 90.678 45.521 121.453 1.00 31.85 ATOM 2420 N LYS 2192 91.824 45.876 123.358 1.00 32.21 ATOM 2421 CA LYS 2192 90.856 45.159 124.160 1.00 32.88 ATOM 2422 CB LYS 2192 91.567 44.330 125.225 1.00 32.95 ATOM 2423 CG LYS 2192 90.653 43.486 126.089 1.00 32.27 ATOM 2424 CD LYS 2192 91.452 42.389 126.781 1.00 33.72 ATOM 2425 CE LYS 2192 90.622 41.595 127.794 1.00 34.06 ATOM 2426 NZ LYS 2192 91.298 40.309 128.159 1.00 34.85 ATOM 2427 C LYS 2192 90.006 46.240 124.788 1.00 34.32 ATOM 2428 O LYS 2192 90.506 47.043 125.564 1.00 35.63 ATOM 2429 N ASN 2193 88.728 46.278 124.424 1.00 36.52 ATOM 2430 CA ASN 2193 87.795 47.284 124.931 1.00 38.57 ATOM 2431 CB ASN 2193 87.482 47.020 126.400 1.00 38.98 ATOM 2432 CG ASN 2193 86.819 45.683 126.613 1.00 39.97 ATOM 2433 OD1 ASN 2193 85.844 45.353 125.934 1.00 40.22 ATOM 2434 ND2 ASN 2193 87.336 44.903 127.558 1.00 40.04 ATOM 2435 C ASN 2193 88.326 48.707 124.765 1.00 39.79 ATOM 2436 O ASN 2193 88.290 49.504 125.696 1.00 39.94 ATOM 2437 N GLY 2194 88.823 49.019 123.573 1.00 40.67 ATOM 2438 CA GLY 2194 89.351 50.349 123.325 1.00 40.52 ATOM 2439 C GLY 2194 90.767 50.590 123.820 1.00 40.79 ATOM 2440 O GLY 2194 91.576 51.183 123.117 1.00 41.69 ATOM 2441 N LYS 2195 91.074 50.136 125.027 1.00 40.12 ATOM 2442 CA LYS 2195 92.402 50.330 125.589 1.00 40.52 ATOM 2443 CB LYS 2195 92.387 50.012 127.087 1.00 39.82 ATOM 2444 C LYS 2195 93.464 49.483 124.889 1.00 41.22 ATOM 2445 O LYS 2195 93.146 48.483 124.243 1.00 41.36 ATOM 2446 N GLU 2196 94.725 49.893 125.024 1.00 41.29 ATOM 2447 CA GLU 2196 95.851 49.189 124.422 1.00 41.22 ATOM 2448 CB GLU 2196 97.128 50.014 124.548 1.00 42.15 ATOM 2449 CG GLU 2196 98.403 49.191 124.357 1.00 42.05 ATOM 2450 CD GLU 2196 99.644 49.865 124.928 1.00 42.46 ATOM 2451 OE1 GLE 2196 99.608 50.302 126.101 1.00 42.02 ATOM 2452 OE2 GLU 2196 100.663 49.946 124.210 1.00 43.16 ATOM 2453 C GLU 2196 96.098 47.838 125.069 1.00 41.45 ATOM 2454 O GLU 2196 96.266 47.740 126.277 1.00 40.77 ATOM 2455 N PHE 2197 96.157 46.808 124.237 1.00 41.80 ATOM 2456 CA PHE 2197 96.378 45.433 124.664 1.00 42.48 ATOM 2457 CB PHE 2197 95.756 44.540 123.578 1.00 41.27 ATOM 2458 CG PHE 2197 95.269 43.195 124.054 1.00 39.86 ATOM 2459 CD1 PHE 2197 94.888 42.230 123.128 1.00 38.62 ATOM 2460 CD2 PHE 2197 95.197 42.881 125.400 1.00 40.20 ATOM 2461 CE1 PHE 2197 94.449 40.974 123.528 1.00 38.94 ATOM 2462 CE2 PHE 2197 94.756 41.618 125.812 1.00 39.99 ATOM 2463 CZ PHE 2197 94.383 40.666 124.872 1.00 39.73 ATOM 2464 C PHE 2197 97.901 45.207 124.766 1.00 43.80 ATOM 2465 O PHE 2197 98.668 45.900 124.108 1.00 45.77 ATOM 2466 N LYS 2198 98.337 44.253 125.586 1.00 44.13 ATOM 2467 CA LYS 2198 99.768 43.928 125.739 1.00 44.71 ATOM 2468 CB LYS 2198 100.454 44.829 126.777 1.00 45.08 ATOM 2469 CG LYS 2198 100.915 46.175 126.239 1.00 46.46 ATOM 2470 CD LYS 2198 101.578 47.027 127.319 1.00 48.52 ATOM 2471 CE LYS 2198 101.944 48.421 126.776 1.00 49.18 ATOM 2472 NZ LYS 2198 102.534 49.339 127.804 1.00 48.52 ATOM 2473 C LYS 2198 99.898 42.477 126.183 1.00 44.72 ATOM 2474 O LYS 2198 99.252 42.060 127.141 1.00 45.40 ATOM 2475 N PRO 2199 100.739 41.686 125.497 1.00 43.97 ATOM 2476 CD PRO 2199 101.524 42.007 124.298 1.00 43.28 ATOM 2477 CA PRO 2199 100.918 40.276 125.850 1.00 43.87 ATOM 2478 CB PRO 2199 102.173 39.901 125.084 1.00 42.82 ATOM 2479 CG PRO 2199 101.948 40.624 123.817 1.00 42.83 ATOM 2480 C PRO 2199 100.951 39.908 127.340 1.00 44.42 ATOM 2481 O PRO 2199 100.379 38.888 127.728 1.00 45.33 ATOM 2482 N ASP 2200 101.587 40.712 128.184 1.00 43.91 ATOM 2483 CA ASP 2200 101.586 40.379 129.601 1.00 44.12 ATOM 2484 CB ASP 2200 102.720 41.121 130.330 1.00 47.94 ATOM 2485 CG ASP 2200 102.936 42.544 129.815 1.00 52.10 ATOM 2486 OD1 ASP 2200 101.955 43.321 129.716 1.00 54.71 ATOM 2487 OD2 ASP 2200 104.101 42.890 129.518 1.00 52.51 ATOM 2488 C ASP 2200 100.217 40.657 130.268 1.00 42.28 ATOM 2489 O ASP 2200 100.046 40.441 131.466 1.00 41.60 ATOM 2490 N HIS 2201 99.243 41.113 129.484 1.00 39.83 ATOM 2491 CA HIS 2201 97.902 41.408 129.994 1.00 38.18 ATOM 2492 CB HIS 2201 97.095 42.252 129.000 1.00 36.78 ATOM 2493 CG HIS 2201 97.474 43.699 128.956 1.00 35.18 ATOM 2494 CD2 HIS 2201 97.140 44.675 128.078 1.00 33.45 ATOM 2495 ND1 HIS 2201 98.255 44.300 129.920 1.00 33.71 ATOM 2496 CE1 HIS 2201 98.386 45.584 129.636 1.00 33.15 ATOM 2497 NE2 HIS 2201 97.719 45.837 128.524 1.00 33.26 ATOM 2498 C HIS 2201 97.050 40.178 130.293 1.00 37.71 ATOM 2499 O HIS 2201 95.958 40.307 130.842 1.00 37.87 ATOM 2500 N ARG 2202 97.510 38.998 129.895 1.00 36.98 ATOM 2501 CA ARG 2202 96.757 37.774 130.152 1.00 36.37 ATOM 2502 CB ARG 2202 95.773 37.490 129.014 1.00 35.42 ATOM 2503 CG ARG 2202 96.408 36.963 127.733 1.00 32.75 ATOM 2504 CD ARG 2202 95.375 36.864 126.619 1.00 30.71 ATOM 2505 NE ARG 2202 94.316 35.902 126.909 1.00 29.13 ATOM 2506 CZ ARG 2202 94.454 34.584 126.808 1.00 30.20 ATOM 2507 NH1 ARG 2202 95.608 34.058 126.424 1.00 31.83 ATOM 2508 NH2 ARG 2202 93.435 33.784 127.070 1.00 30.13 ATOM 2509 C ARG 2202 97.740 36.623 130.266 1.00 37.00 ATOM 2510 O ARG 2202 98.799 36.652 129.640 1.00 35.95 ATOM 2511 N ILE 2203 97.407 35.609 131.058 1.00 38.08 ATOM 2512 CA ILE 2203 98.330 34.493 131.181 1.00 39.00 ATOM 2513 CB ILE 2203 97.884 33.446 132.213 1.00 39.18 ATOM 2514 CC2 ILE 2203 96.685 32.657 131.694 1.00 38.82 ATOM 2515 CG1 ILE 2203 99.053 32.499 132.495 1.00 39.82 ATOM 2516 CD1 ILE 2203 100.275 33.187 133.083 1.00 37.47 ATOM 2517 C ILE 2203 98.508 33.817 129.830 1.00 39.98 ATOM 2518 O ILE 2203 97.544 33.559 129.100 1.00 40.24 ATOM 2519 N GLY 2204 99.759 33.538 129.499 1.00 40.59 ATOM 2520 CA GLY 2204 100.051 32.927 128.219 1.00 41.35 ATOM 2521 C GLY 2204 100.042 34.010 127.157 1.00 41.56 ATOM 2522 O GLY 2204 100.469 33.789 126.025 1.00 41.20 ATOM 2523 N GLY 2205 99.548 35.187 127.537 1.00 41.55 ATOM 2524 CA GLY 2205 99.469 36.316 126.626 1.00 40.71 ATOM 2525 C GLY 2205 98.821 36.028 125.281 1.00 40.50 ATOM 2526 O GLY 2205 98.122 35.027 125.113 1.00 39.66 ATOM 2527 N TYR 2206 99.021 36.932 124.325 1.00 40.49 ATOM 2528 CA TYR 2206 98.482 36.723 122.993 1.00 40.63 ATOM 2529 CB TYR 2206 97.446 37.775 122.580 1.00 39.91 ATOM 2530 CG TYR 2206 97.850 39.221 122.748 1.00 40.02 ATOM 2531 CD1 TYR 2206 97.755 39.850 123.994 1.00 40.48 ATOM 2532 CE1 TYR 2206 98.058 41.199 124.151 1.00 39.15 ATOM 2533 CD2 TYR 2206 98.268 39.980 121.660 1.00 38.56 ATOM 2534 CE2 TYR 2206 98.576 41.332 121.805 1.00 38.64 ATOM 2535 CZ TYR 2206 98.468 41.940 123.056 1.00 39.43 ATOM 2536 OH TYR 2206 98.762 43.285 123.211 1.00 38.19 ATOM 2537 C TYR 2206 99.605 36.681 121.988 1.00 41.31 ATOM 2538 O TYR 2206 100.753 37.004 122.298 1.00 41.16 ATOM 2539 N LYS 2207 99.264 36.247 120.784 1.00 42.04 ATOM 2540 CA LYS 2207 100.223 36.121 119.703 1.00 43.21 ATOM 2541 CB LYS 2207 100.465 34.647 119.398 1.00 44.52 ATOM 2542 CG LYS 2207 101.339 34.407 118.187 1.00 47.14 ATOM 2543 CD LYS 2207 101.051 33.041 117.596 1.00 49.53 ATOM 2544 CE LYS 2207 101.862 32.797 116.344 1.00 50.27 ATOM 2545 NZ LYS 2207 101.553 31.473 115.742 1.00 51.00 ATOM 2546 C LYS 2207 99.659 36.802 118.469 1.00 43.19 ATOM 2547 O LYS 2207 98.533 36.518 118.057 1.00 43.68 ATOM 2548 N VAL 2208 100.432 37.704 117.877 1.00 42.85 ATOM 2549 CA VAL 2208 99.959 38.396 116.687 1.00 42.83 ATOM 2550 CB VAL 2208 100.080 39.937 116.819 1.00 42.12 ATOM 2551 CG1 VAL 2208 99.676 40.608 115.516 1.00 41.15 ATOM 2552 CG2 VAL 2208 99.182 40.433 117.932 1.00 41.53 ATOM 2553 C VAL 2208 100.722 37.946 115.455 1.00 42.80 ATOM 2554 O VAL 2208 101.942 38.056 115.396 1.00 42.90 ATOM 2555 N ARG 2209 99.987 37.422 114.481 1.00 43.49 ATOM 2556 CA ARG 2209 100.565 36.953 113.222 1.00 43.88 ATOM 2557 CB ARG 2209 100.000 35.584 112.835 1.00 44.05 ATOM 2558 CG ARG 2209 100.652 34.440 113.565 1.00 45.90 ATOM 2559 CD ARG 2209 102.020 34.172 112.999 1.00 48.17 ATOM 2560 NE ARG 2209 102.967 33.768 114.030 1.00 51.06 ATOM 2561 CZ ARG 2209 104.083 33.079 113.801 1.00 53.29 ATOM 2562 NH1 ARG 2209 104.397 32.705 112.565 1.00 53.46 ATOM 2563 NH2 ARG 2209 104.891 32.765 114.807 1.00 55.10 ATOM 2564 C ARG 2209 100.263 37.945 112.112 1.00 44.04 ATOM 2565 O ARG 2209 99.323 37.755 111.340 1.00 43.78 ATOM 2566 N TYR 2210 101.061 39.008 112.035 1.00 43.71 ATOM 2567 CA TYR 2210 100.850 40.019 111.011 1.00 42.27 ATOM 2568 CB TYR 2210 101.966 41.056 110.993 1.00 43.20 ATOM 2569 CG TYR 2210 102.161 41.743 112.316 1.00 45.09 ATOM 2570 CD1 TYR 2210 102.831 41.103 113.358 1.00 46.50 ATOM 2571 CE1 TYR 2210 102.994 41.723 114.604 1.00 47.53 ATOM 2572 CD2 TYR 2210 101.655 43.023 112.543 1.00 45.57 ATOM 2573 CE2 TYR 2210 101.811 43.655 113.786 1.00 46.60 ATOM 2574 CZ TYR 2210 102.482 42.997 114.811 1.00 47.26 ATOM 2575 OH TYR 2210 102.646 43.593 116.039 1.00 47.71 ATOM 2576 C TYR 2210 100.799 39.321 109.685 1.00 40.96 ATOM 2577 O TYR 2210 100.130 39.775 108.772 1.00 41.30 ATOM 2578 N ALA 2211 101.502 38.203 109.588 1.00 40.54 ATOM 2579 CA ALA 2211 101.521 37.428 108.357 1.00 40.16 ATOM 2580 CB ALA 2211 102.254 36.112 108.595 1.00 40.83 ATOM 2581 C ALA 2211 100.089 37.168 107.873 1.00 39.20 ATOM 2582 O ALA 2211 99.832 37.054 106.678 1.00 37.66 ATOM 2583 N THR 2212 99.158 37.073 108.814 1.00 39.40 ATOM 2584 CA THR 2212 97.765 36.846 108.462 1.00 39.47 ATOM 2585 CB THR 2212 97.312 35.401 108.767 1.00 40.20 ATOM 2586 OG1 THR 2212 97.752 35.004 110.077 1.00 41.45 ATOM 2587 CG2 THR 2212 97.872 34.462 107.722 1.00 40.38 ATOM 2588 C THR 2212 96.834 37.837 109.148 1.00 38.95 ATOM 2589 O THR 2212 95.623 37.620 109.218 1.00 38.42 ATOM 2590 N TRP 2213 97.415 38.931 109.637 1.00 38.83 ATOM 2591 CA TRP 2213 96.662 39.999 110.290 1.00 38.61 ATOM 2592 CB TRP 2213 95.779 40.736 109.276 1.00 40.70 ATOM 2593 CG TRP 2213 96.537 41.323 108.162 1.00 42.61 ATOM 2594 CD2 TRP 2213 97.098 42.634 108.118 1.00 43.58 ATOM 2595 CE2 TRP 2213 97.789 42.749 106.896 1.00 44.29 ATOM 2596 CE3 TRP 2213 97.084 43.726 108.994 1.00 43.52 ATOM 2597 CD1 TRP 2213 96.895 40.710 107.002 1.00 43.01 ATOM 2598 NE1 TRP 2213 97.650 41.558 106.233 1.00 44.09 ATOM 2599 CZ2 TRP 2213 98.461 43.916 106.526 1.00 44.49 ATOM 2600 CZ3 TRP 2213 97.750 44.883 108.627 1.00 43.51 ATOM 2601 CH2 TRP 2213 98.429 44.969 107.403 1.00 44.41 ATOM 2602 C TRP 2213 95.774 39.442 111.371 1.00 37.32 ATOM 2603 O TRP 2213 94.617 39.846 111.507 1.00 37.76 ATOM 2604 N SER 2214 96.308 38.512 112.143 1.00 35.32 ATOM 2605 CA SER 2214 95.516 37.892 113.190 1.00 33.63 ATOM 2606 CB SER 2214 95.370 36.392 112.924 1.00 33.71 ATOM 2607 OG SER 2214 94.681 36.144 111.720 1.00 34.61 ATOM 2608 C SER 2214 96.104 38.058 114.572 1.00 31.52 ATOM 2609 O SER 2214 97.281 38.396 114.736 1.00 31.05 ATOM 2610 N ILE 2215 95.259 37.810 115.565 1.00 28.95 ATOM 2611 CA ILE 2215 95.664 37.854 116.960 1.00 26.54 ATOM 2612 CB ILE 2215 94.951 38.965 117.733 1.00 23.98 ATOM 2613 CG2 ILE 2215 93.471 38.938 117.434 1.00 22.03 ATOM 2614 CG1 ILE 2215 95.239 38.798 119.220 1.00 22.66 ATOM 2615 CD1 ILE 2215 94.372 39.645 120.105 1.00 23.72 ATOM 2616 C ILE 2215 95.195 36.509 117.486 1.00 25.62 ATOM 2617 O ILE 2215 94.132 36.024 117.090 1.00 26.30 ATOM 2618 N ILE 2216 95.967 35.890 118.361 1.00 23.36 ATOM 2619 CA ILE 2216 95.546 34.600 118.866 1.00 23.42 ATOM 2620 CB ILE 2216 96.436 33.461 118.341 1.00 24.04 ATOM 2621 CG2 ILE 2216 95.658 32.164 118.362 1.00 22.84 ATOM 2622 CG1 ILE 2216 96.924 33.763 116.918 1.00 26.50 ATOM 2623 CD1 ILE 2216 96.007 33.275 115.788 1.00 27.77 ATOM 2624 C ILE 2216 95.571 34.522 120.380 1.00 24.32 ATOM 2625 O ILE 2216 96.529 34.949 121.037 1.00 24.53 ATOM 2626 N MET 2217 94.503 33.971 120.935 1.00 24.28 ATOM 2627 CA MET 2217 94.415 33.803 122.360 1.00 24.21 ATOM 2628 CB MET 2217 93.352 34.715 122.959 1.00 24.38 ATOM 2629 CG MET 2217 93.798 36.155 123.093 1.00 22.92 ATOM 2630 SD MET 2217 92.463 37.174 123.666 1.00 21.81 ATOM 2631 CE MET 2217 91.382 37.054 122.235 1.00 20.91 ATOM 2632 C MET 2217 94.109 32.354 122.639 1.00 24.86 ATOM 2633 O MET 2217 93.064 31.820 122.250 1.00 24.66 ATOM 2634 N ASP 2218 95.076 31.727 123.294 1.00 25.10 ATOM 2635 CA ASP 2218 94.993 30.344 123.687 1.00 24.19 ATOM 2636 CB ASP 2218 96.385 29.741 123.795 1.00 24.55 ATOM 2637 CG ASP 2218 96.751 28.908 122.600 1.00 25.12 ATOM 2638 OD1 ASP 2218 95.908 28.741 121.693 1.00 25.15 ATOM 2639 OD2 ASP 2218 97.895 28.411 122.575 1.00 25.43 ATOM 2640 C ASP 2218 94.309 30.273 125.041 1.00 25.23 ATOM 2641 O ASP 2218 94.398 31.203 125.847 1.00 24.60 ATOM 2642 N SER 2219 93.613 29.162 125.268 1.00 25.53 ATOM 2643 CA SER 2219 92.913 28.901 126.520 1.00 24.58 ATOM 2644 CB SER 2219 93.900 28.304 127.536 1.00 26.55 ATOM 2645 OG SER 2219 93.242 27.559 128.559 1.00 30.52 ATOM 2646 C SER 2219 92.258 30.145 127.104 1.00 22.73 ATOM 2647 O SER 2219 92.674 30.645 128.140 1.00 21.07 ATOM 2648 N VAL 2220 91.215 30.637 126.450 1.00 22.94 ATOM 2649 CA VAL 2220 90.548 31.835 126.935 1.00 23.29 ATOM 2650 CB VAL 2220 89.682 32.470 125.839 1.00 21.85 ATOM 2651 CG1 VAL 2220 90.564 32.792 124.638 1.00 21.42 ATOM 2652 CG2 VAL 2220 88.544 31.549 125.455 1.00 19.27 ATOM 2653 C VAL 2220 89.713 31.601 128.184 1.00 24.09 ATOM 2654 O VAL 2220 89.290 30.485 128.466 1.00 25.16 ATOM 2655 N VAL 2221 89.496 32.664 128.946 1.00 24.97 ATOM 2656 CA VAL 2221 88.712 32.585 130.177 1.00 25.49 ATOM 2657 CB VAL 2221 89.608 32.400 131.424 1.00 24.80 ATOM 2658 CG1 VAL 2221 90.294 31.048 131.374 1.00 24.92 ATOM 2659 CG2 VAL 2221 90.626 33.526 131.511 1.00 25.00 ATOM 2660 C VAL 2221 87.870 33.840 130.374 1.00 25.44 ATOM 2661 O VAL 2221 88.061 34.837 129.687 1.00 25.70 ATOM 2662 N PRO 2222 86.922 33.807 131.323 1.00 26.28 ATOM 2663 CD PRO 2222 86.620 32.728 132.281 1.00 26.63 ATOM 2664 CA PRO 2222 86.063 34.969 131.579 1.00 27.30 ATOM 2665 CB PRO 2222 85.534 34.698 132.981 1.00 25.99 ATOM 2666 CG PRO 2222 85.346 33.230 132.951 1.00 26.68 ATOM 2667 C PRO 2222 86.760 36.321 131.489 1.00 27.54 ATOM 2668 O PRO 2222 86.225 37.268 130.908 1.00 27.07 ATOM 2669 N SER 2223 87.951 36.412 132.069 1.00 28.28 ATOM 2670 CA SER 2223 88.699 37.667 132.053 1.00 29.16 ATOM 2671 CB SER 2223 90.073 37.486 132.721 1.00 30.38 ATOM 2672 OG SER 2223 91.045 36.980 131.812 1.00 31.85 ATOM 2673 C SER 2223 88.894 38.215 130.638 1.00 28.77 ATOM 2674 O SER 2223 89.073 39.417 130.447 1.00 29.12 ATOM 2675 N ASP 2224 88.847 37.334 129.649 1.00 28.24 ATOM 2676 CA ASP 2224 89.045 37.747 128.279 1.00 27.95 ATOM 2677 CB ASP 2224 89.609 36.577 127.476 1.00 29.00 ATOM 2678 CG ASP 2224 90.940 36.103 128.022 1.00 29.75 ATOM 2679 OD1 ASP 2224 91.806 36.968 128.293 1.00 30.18 ATOM 2680 OD2 ASP 2224 91.119 34.876 128.183 1.00 29.10 ATOM 2681 C ASP 2224 87.792 38.300 127.629 1.00 27.30 ATOM 2682 O ASP 2224 87.866 38.939 126.585 1.00 27.89 ATOM 2683 N LYS 2225 86.641 38.073 128.243 1.00 27.44 ATOM 2684 CA LYS 2225 85.403 38.582 127.669 1.00 29.05 ATOM 2685 CB LYS 2225 84.240 38.398 128.640 1.00 30.40 ATOM 2686 CG LYS 2225 84.042 36.969 129.081 1.00 31.45 ATOM 2687 CD LYS 2225 82.580 36.664 129.267 1.00 34.02 ATOM 2688 CE LYS 2225 81.939 37.559 130.300 1.00 35.70 ATOM 2689 NZ LYS 2225 80.492 37.226 130.416 1.00 38.06 ATOM 2690 C LYS 2225 85.589 40.056 127.370 1.00 29.01 ATOM 2691 O LYS 2225 86.169 40.779 128.178 1.00 29.46 ATOM 2692 N GLY 2226 85.115 40.499 126.210 1.00 28.77 ATOM 2693 CA GLY 2226 85.257 41.899 125.860 1.00 29.00 ATOM 2694 C GLY 2226 85.247 42.191 124.372 1.00 29.03 ATOM 2695 O GLY 2226 84.906 41.336 123.562 1.00 29.33 ATOM 2696 N ASN 2227 85.605 43.421 124.016 1.00 29.41 ATOM 2697 CA ASN 2227 85.654 43.832 122.623 1.00 29.45 ATOM 2698 CB ASN 2227 85.078 45.229 122.453 1.00 30.02 ATOM 2699 CG ASN 2227 83.646 45.307 122.876 1.00 31.29 ATOM 2700 OD1 ASN 2227 82.765 44.769 122.207 1.00 32.09 ATOM 2701 ND2 ASN 2227 83.397 45.967 124.006 1.00 31.20 ATOM 2702 C ASN 2227 87.099 43.858 122.205 1.00 29.08 ATOM 2703 O ASN 2227 87.959 44.302 122.955 1.00 30.38 ATOM 2704 N TYR 2228 87.369 43.385 121.005 1.00 27.71 ATOM 2705 CA TYR 2228 88.721 43.374 120.514 1.00 28.06 ATOM 2706 CB TYR 2228 89.195 41.921 120.363 1.00 28.22 ATOM 2707 CG TYR 2228 89.471 41.237 121.692 1.00 27.12 ATOM 2708 CD1 TYR 2228 88.432 40.824 122.531 1.00 25.93 ATOM 2709 CE1 TYR 2228 88.698 40.271 123.793 1.00 26.56 ATOM 2710 CD2 TYR 2228 90.779 41.074 122.143 1.00 27.73 ATOM 2711 CE2 TYR 2228 91.053 40.526 123.399 1.00 27.06 ATOM 2712 CZ TYR 2228 90.016 40.129 124.215 1.00 26.74 ATOM 2713 OH TYR 2228 90.326 39.598 125.442 1.00 27.37 ATOM 2714 C TYR 2228 88.719 44.119 119.188 1.00 29.09 ATOM 2715 O TYR 2228 87.966 43.769 118.278 1.00 29.31 ATOM 2716 N THR 2229 89.544 45.159 119.087 1.00 29.61 ATOM 2717 CA THR 2229 89.608 45.959 117.872 1.00 29.63 ATOM 2718 CB THR 2229 89.333 47.437 118.158 1.00 28.68 ATOM 2719 OG1 THR 2229 88.084 47.574 118.831 1.00 27.17 ATOM 2720 CG2 THR 2229 89.300 48.223 116.858 1.00 28.49 ATOM 2721 C THR 2229 90.952 45.913 117.175 1.00 30.97 ATOM 2722 O THR 2229 92.004 46.149 117.784 1.00 30.73 ATOM 2723 N CYS 2230 90.913 45.639 115.882 1.00 32.04 ATOM 2724 CA CYS 2230 92.136 45.615 115.110 1.00 33.92 ATOM 2725 C CYS 2230 92.179 46.950 114.387 1.00 34.62 ATOM 2726 O CYS 2230 91.147 47.457 113.961 1.00 34.44 ATOM 2727 CB CYS 2230 92.110 44.483 114.084 1.00 33.63 ATOM 2728 SG CYS 2230 90.959 44.779 112.710 1.00 32.18 ATOM 2729 N ILE 2231 93.372 47.518 114.261 1.00 35.98 ATOM 2730 CA ILE 2231 93.545 48.786 113.577 1.00 36.56 ATOM 2731 CB ILE 2231 93.892 49.900 114.556 1.00 35.25 ATOM 2732 CG2 ILE 2231 94.255 51.160 113.805 1.00 36.52 ATOM 2733 CG1 ILE 2231 92.699 50.170 115.457 1.00 35.13 ATOM 2734 CD1 ILE 2231 92.949 51.257 116.448 1.00 35.38 ATOM 2735 C ILE 2231 94.653 48.694 112.547 1.00 38.34 ATOM 2736 O ILE 2231 95.840 48.685 112.891 1.00 38.80 ATOM 2737 N VAL 2232 94.258 48.617 111.283 1.00 39.59 ATOM 2738 CA VAL 2232 95.213 48.546 110.193 1.00 41.70 ATOM 2739 CB VAL 2232 94.705 47.653 109.084 1.00 42.55 ATOM 2740 CG1 VAL 2232 95.767 47.522 108.005 1.00 43.06 ATOM 2741 CG2 VAL 2232 94.340 46.304 109.658 1.00 43.42 ATOM 2742 C VAL 2232 95.353 49.958 109.667 1.00 42.90 ATOM 2743 O VAL 2232 94.356 50.625 109.405 1.00 42.57 ATOM 2744 N GLU 2233 96.589 50.408 109.488 1.00 44.86 ATOM 2745 CA GLU 2233 96.802 51.775 109.050 1.00 46.62 ATOM 2746 CB GLU 2233 96.569 52.671 110.253 1.00 48.43 ATOM 2747 CG GLU 2233 97.511 52.278 111.386 1.00 52.28 ATOM 2748 CD GLU 2233 97.188 52.948 112.701 1.00 54.75 ATOM 2749 OE1 GLU 2233 96.683 54.092 112.668 1.00 56.35 ATOM 2750 OE2 GLU 2233 97.457 52.338 113.764 1.00 55.00 ATOM 2751 C GLU 2233 98.181 52.096 108.466 1.00 46.69 ATOM 2752 O GLU 2233 99.210 51.595 108.924 1.00 45.42 ATOM 2753 N ASN 2234 98.181 52.940 107.442 1.00 47.28 ATOM 2754 CA ASN 2234 99.415 53.408 106.837 1.00 48.02 ATOM 2755 CB ASN 2234 99.665 52.807 105.440 1.00 48.62 ATOM 2756 CG ASN 2234 98.596 53.170 104.434 1.00 49.97 ATOM 2757 OD1 ASN 2234 97.922 54.196 104.563 1.00 50.42 ATOM 2758 ND2 ASN 2234 98.448 52.336 103.404 1.00 50.09 ATOM 2759 C ASN 2234 99.253 54.925 106.782 1.00 48.23 ATOM 2760 O ASN 2234 98.372 55.473 107.439 1.00 47.22 ATOM 2761 N GLU 2235 100.083 55.598 106.000 1.00 48.98 ATOM 2762 CA GLU 2235 100.051 57.052 105.905 1.00 49.40 ATOM 2763 CB GLU 2235 101.323 57.527 105.210 1.00 51.16 ATOM 2764 CC GLU 2235 102.574 56.796 105.669 1.00 55.19 ATOM 2765 CD GLU 2235 103.767 57.050 104.756 1.00 58.69 ATOM 2766 OE1 GLU 2235 103.660 56.759 103.539 1.00 60.15 ATOM 2767 OE2 GLU 2235 104.811 57.539 105.257 1.00 58.99 ATOM 2768 C GLU 2235 98.845 57.662 105.191 1.00 48.61 ATOM 2769 O GLU 2235 98.562 58.845 105.357 1.00 47.90 ATOM 2770 N TYR 2236 98.128 56.869 104.408 1.00 48.32 ATOM 2771 CA TYR 2236 96.997 57.413 103.662 1.00 48.33 ATOM 2772 CB TYR 2236 97.152 57.090 102.178 1.00 50.15 ATOM 2773 CG TYR 2236 98.554 57.340 101.694 1.00 53.62 ATOM 2774 CD1 TYR 2236 99.607 56.542 102.137 1.00 55.10 ATOM 2775 CE1 TYR 2236 100.917 56.815 101.784 1.00 57.18 ATOM 2776 CD2 TYR 2236 98.850 58.420 100.868 1.00 55.01 ATOM 2777 CE2 TYR 2236 100.167 58.704 100.504 1.00 57.17 ATOM 2778 CZ TYR 2236 101.196 57.895 100.972 1.00 57.54 ATOM 2779 OH TYR 2236 102.507 58.170 100.655 1.00 59.18 ATOM 2780 C TYR 2236 95.638 56.958 104.141 1.00 47.36 ATOM 2781 O TYR 2236 94.657 57.050 103.408 1.00 47.35 ATOM 2782 N GLY 2237 95.573 56.476 105.375 1.00 46.08 ATOM 2783 CA GLY 2237 94.302 56.026 105.903 1.00 43.02 ATOM 2784 C GLY 2237 94.425 54.969 106.980 1.00 41.26 ATOM 2785 O GLY 2237 95.512 54.455 107.270 1.00 40.98 ATOM 2786 N SER 2238 93.286 54.654 107.585 1.00 38.81 ATOM 2787 CA SER 2238 93.214 53.654 108.635 1.00 35.42 ATOM 2788 CB SER 2238 93.350 54.294 110.007 1.00 34.17 ATOM 2789 OG SER 2238 92.170 54.064 110.755 1.00 30.78 ATOM 2790 C SER 2238 91.860 52.996 108.556 1.00 34.05 ATOM 2791 O SER 2238 90.883 53.624 108.170 1.00 34.61 ATOM 2792 N ILE 2239 91.813 51.728 108.926 1.00 32.36 ATOM 2793 CA ILE 2239 90.580 50.968 108.929 1.00 30.84 ATOM 2794 CB ILE 2239 90.540 49.998 107.745 1.00 30.29 ATOM 2795 CG2 ILE 2239 90.206 50.742 106.481 1.00 30.27 ATOM 2796 CG1 ILE 2239 91.891 49.299 107.611 1.00 29.92 ATOM 2797 CD1 ILE 2239 92.028 48.517 106.356 1.00 30.31 ATOM 2798 C ILE 2239 90.582 50.185 110.230 1.00 30.38 ATOM 2799 O ILE 2239 91.627 50.039 110.872 1.00 30.66 ATOM 2800 N ASN 2240 89.424 49.678 110.624 1.00 29.34 ATOM 2801 CA ASN 2240 89.356 48.924 111.859 1.00 28.33 ATOM 2802 CB ASN 2240 89.456 49.875 113.032 1.00 27.41 ATOM 2803 CG ASN 2240 88.246 50.745 113.143 1.00 27.47 ATOM 2804 OD1 ASN 2240 87.304 50.428 113.858 1.00 30.26 ATOM 2805 ND2 ASN 2240 88.244 51.839 112.405 1.00 28.28 ATOM 2806 C ASN 2240 88.062 48.142 111.972 1.00 28.33 ATOM 2807 O ASN 2240 87.001 48.607 111.568 1.00 29.54 ATOM 2808 N HIS 2241 88.165 46.943 112.524 1.00 27.96 ATOM 2809 CA HIS 2241 87.010 46.106 112.727 1.00 26.95 ATOM 2810 CB HIS 2241 87.081 44.867 111.848 1.00 27.14 ATOM 2811 CG HIS 2241 85.795 44.109 111.785 1.00 25.98 ATOM 2812 CD2 HIS 2241 85.365 43.023 112.468 1.00 26.60 ATOM 2813 ND1 HIS 2241 84.757 44.482 110.962 1.00 25.66 ATOM 2814 CE1 HIS 2241 83.743 43.656 111.138 1.00 27.38 ATOM 2815 NE2 HIS 2241 84.085 42.761 112.047 1.00 28.32 ATOM 2816 C HIS 2241 87.042 45.727 114.195 1.00 26.83 ATOM 2817 O HIS 2241 88.097 45.791 114.840 1.00 27.26 ATOM 2818 N THR 2242 85.895 45.334 114.726 1.00 26.44 ATOM 2819 CA THR 2242 85.827 44.978 116.129 1.00 26.55 ATOM 2820 CB THR 2242 85.252 46.153 116.937 1.00 24.58 ATOM 2821 OG1 THR 2242 86.180 47.241 116.898 1.00 22.77 ATOM 2822 CG2 THR 2242 84.995 45.756 118.375 1.00 22.55 ATOM 2823 C THR 2242 85.004 43.728 116.374 1.00 27.83 ATOM 2824 O THR 2242 83.844 43.650 115.970 1.00 29.08 ATOM 2825 N TYR 2243 85.619 42.754 117.037 1.00 28.35 ATOM 2826 CA TYR 2243 84.949 41.504 117.347 1.00 29.79 ATOM 2827 CB TYR 2243 85.867 40.329 117.040 1.00 30.18 ATOM 2828 CG TYR 2243 86.383 40.323 115.618 1.00 30.20 ATOM 2829 CD1 TYR 2243 87.669 40.761 115.324 1.00 29.45 ATOM 2830 CE1 TYR 2243 88.161 40.716 114.027 1.00 31.01 ATOM 2831 CD2 TYR 2243 85.595 39.847 114.573 1.00 29.56 ATOM 2832 CE2 TYR 2243 86.076 39.800 113.271 1.00 30.63 ATOM 2833 CZ TYR 2243 87.362 40.231 113.001 1.00 31.28 ATOM 2834 OH TYR 2243 87.856 40.162 111.715 1.00 31.89 ATOM 2835 C TYR 2243 84.552 41.478 118.810 1.00 30.90 ATOM 2836 O TYR 2243 85.180 42.131 119.641 1.00 32.19 ATOM 2837 N GLN 2244 83.507 40.725 119.127 1.00 31.55 ATOM 2838 CA GLN 2244 83.040 40.629 120.501 1.00 32.33 ATOM 2839 CB GLN 2244 81.541 40.895 120.579 1.00 34.66 ATOM 2840 CG GLN 2244 81.114 42.118 119.818 1.00 41.95 ATOM 2841 CD GLN 2244 79.612 42.191 119.631 1.00 46.48 ATOM 2842 OE1 GLN 2244 78.980 41.210 119.228 1.00 50.88 ATOM 2843 NE2 GLN 2244 79.029 43.360 119.911 1.00 47.45 ATOM 2844 C GLN 2244 83.299 39.225 120.971 1.00 30.93 ATOM 2845 O CLN 2244 82.847 38.281 120.342 1.00 32.32 ATOM 2846 N LEU 2245 84.031 39.081 122.066 1.00 29.70 ATOM 2847 CA LEU 2245 84.314 37.764 122.595 1.00 28.82 ATOM 2848 CB LEU 2245 85.803 37.613 122.932 1.00 29.07 ATOM 2849 CG LEU 2245 86.203 36.301 123.622 1.00 28.66 ATOM 2850 CD1 LEU 2245 85.712 35.124 122.828 1.00 28.15 ATOM 2851 CD2 LEU 2245 87.707 36.236 123.769 1.00 29.54 ATOM 2852 C LEU 2245 83.495 37.542 123.839 1.00 27.92 ATOM 2853 O LEU 2245 83.411 38.416 124.694 1.00 28.60 ATOM 2854 N ASP 2246 82.872 36.376 123.923 1.00 27.25 ATOM 2855 CA ASP 2246 82.086 36.015 125.086 1.00 27.26 ATOM 2856 CB ASP 2246 80.593 36.149 124.805 1.00 28.12 ATOM 2857 CG ASP 2246 79.757 36.109 126.076 1.00 30.44 ATOM 2858 OD1 ASP 2246 78.511 36.132 125.976 1.00 33.16 ATOM 2859 OD2 ASP 2246 80.343 36.061 127.180 1.00 29.88 ATOM 2860 C ASP 2246 82.441 34.578 125.426 1.06 27.63 ATOM 2861 O ASP 2246 82.342 33.682 124.585 1.00 27.86 ATOM 2862 N VAL 2247 82.881 34.370 126.661 1.00 27.19 ATOM 2863 CA VAL 2247 83.275 33.049 127.116 1.00 26.28 ATOM 2864 CB VAL 2247 84.661 33.111 127.724 1.00 26.83 ATOM 2865 CG1 VAL 2247 85.186 31.704 127.951 1.00 26.77 ATOM 2866 CG2 VAL 2247 85.573 33.926 126.799 1.00 26.27 ATOM 2867 C VAL 2247 82.270 32.478 128.117 1.00 25.49 ATOM 2868 O VAL 2247 81.866 33.135 129.070 1.00 25.04 ATOM 2869 N VAL 2248 81.861 31.241 127.883 1.00 25.33 ATOM 2870 CA VAL 2248 80.875 30.577 128.728 1.00 24.03 ATOM 2871 CB VAL 2248 79.725 29.997 127.854 1.00 22.77 ATOM 2872 CG1 VAL 2248 78.704 29.305 128.707 1.00 21.53 ATOM 2873 CG2 VAL 2248 79.080 31.093 127.056 1.00 21.73 ATOM 2874 C VAL 2248 81.525 29.432 129.501 1.00 24.15 ATOM 2875 O VAL 2248 82.047 28.504 128.891 1.00 24.08 ATOM 2876 N GLU 2249 81.538 29.492 130.833 1.00 24.50 ATOM 2877 CA GLU 2249 82.133 28.392 131.605 1.00 25.67 ATOM 2878 CB GLU 2249 82.573 28.855 133.002 1.00 25.92 ATOM 2879 CG GLU 2249 83.681 29.907 133.001 1.00 27.35 ATOM 2880 CD GLU 2249 84.096 30.356 134.400 1.00 28.29 ATOM 2881 OE1 GLU 2249 83.223 30.792 135.169 1.00 29.15 ATOM 2882 OE2 GLU 2249 85.298 30.287 134.729 1.00 28.96 ATOM 2883 C GLU 2249 81.089 27.287 131.731 1.00 25.94 ATOM 2884 O GLU 2249 79.934 27.550 132.090 1.00 27.27 ATOM 2885 N ARG 2250 81.488 26.055 131.434 1.00 24.48 ATOM 2886 CA ARG 2250 80.564 24.931 131.494 1.00 24.34 ATOM 2887 CB ARG 2250 80.731 24.071 130.239 1.00 22.86 ATOM 2888 CG ARG 2250 80.671 24.831 128.918 1.00 21.47 ATOM 2889 CD ARG 2250 79.364 25.574 128.775 1.00 20.47 ATOM 2890 NE ARG 2250 78.209 24.684 128.907 1.00 18.58 ATOM 2891 CZ ARG 2250 77.726 23.919 127.934 1.00 16.19 ATOM 2892 NH1 ARG 2250 78.277 23.928 226.732 1.00 15.47 ATOM 2893 NH2 ARG 2250 76.681 23.150 128.172 1.00 14.35 ATOM 2894 C ARG 2250 80.734 24.048 132.737 1.00 25.57 ATOM 2895 O ARG 2250 81.855 23.784 133.154 1.00 26.62 ATOM 2896 N SER 2251 79.622 23.588 133.318 1.00 27.67 ATOM 2897 CA SER 2251 79.648 22.705 134.498 1.00 29.59 ATOM 2898 CB SER 2251 78.802 23.289 135.645 1.00 29.49 ATOM 2899 OG SER 2251 79.417 24.407 136.271 1.00 29.28 ATOM 2900 C SER 2251 79.094 21.322 134.138 1.00 30.92 ATOM 2901 O SER 2251 77.887 21.103 134.227 1.00 30.80 ATOM 2902 N PRO 2252 79.972 20.372 133.747 1.00 32.52 ATOM 2903 CD PRO 2252 81.428 20.579 133.660 1.00 33.32 ATOM 2904 CA PRO 2252 79.641 18.996 133.357 1.00 33.64 ATOM 2905 CB PRO 2252 80.797 18.638 132.462 1.00 32.97 ATOM 2906 CG PRO 2252 81.936 19.192 133.257 1.00 33.41 ATOM 2907 C PRO 2252 79.557 18.052 134.554 1.00 35.26 ATOM 2908 O PRO 2252 80.393 17.162 134.709 1.00 35.60 ATOM 2909 N HIS 2253 78.547 18.245 135.390 1.00 36.75 ATOM 2910 CA HIS 2253 78.380 17.423 136.577 1.00 39.62 ATOM 2911 CB HIS 2253 78.988 18.135 137.782 1.00 43.57 ATOM 2912 CG HIS 2253 80.472 18.278 137.709 1.00 48.09 ATOM 2913 CD2 HIS 2253 81.447 17.888 138.563 1.00 49.70 ATOM 2914 ND1 HIS 2253 81.110 18.861 136.636 1.00 50.53 ATOM 2915 CE1 HIS 2253 82.416 18.821 136.831 1.00 52.26 ATOM 2916 NE2 HIS 2253 82.647 18.236 137.994 1.00 51.65 ATOM 2917 C HIS 2253 76.918 17.175 136.860 1.00 38.87 ATOM 2918 O HIS 2253 76.053 17.848 136.305 1.00 39.07 ATOM 2919 N ARG 2254 76.634 16.213 137.731 1.00 37.62 ATOM 2920 CA ARG 2254 75.249 15.958 138.065 1.00 36.58 ATOM 2921 CB ARG 2254 75.111 14.724 138.963 1.00 37.86 ATOM 2922 CG ARG 2254 75.908 14.745 140.243 1.00 39.87 ATOM 2923 CD ARG 2254 75.703 13.437 141.000 1.00 41.72 ATOM 2924 NE ARG 2254 75.427 13.677 142.414 1.00 44.34 ATOM 2925 CZ ARG 2254 76.355 13.791 143.358 1.00 44.80 ATOM 2926 NH1 ARG 2254 77.643 13.672 143.050 1.00 46.11 ATOM 2927 NH2 ARG 2254 75.989 14.058 144.607 1.00 45.02 ATOM 2928 C ARG 2254 74.757 17.219 138.756 1.00 34.56 ATOM 2929 O ARG 2254 75.548 18.025 139.229 1.00 34.81 ATOM 2930 N PRO 2255 73.443 17.428 138.792 1.00 33.17 ATOM 2931 CD PRO 2255 72.344 16.608 138.261 1.00 32.67 ATOM 2932 CA PRO 2255 72.937 18.638 139.445 1.00 31.64 ATOM 2933 CB PRO 2255 71.422 18.512 139.288 1.00 31.80 ATOM 2934 CG PRO 2255 71.219 17.022 139.152 1.00 33.31 ATOM 2935 C PRO 2255 73.382 18.777 140.887 1.00 30.09 ATOM 2936 O PRO 2255 73.759 17.807 141.520 1.00 29.82 ATOM 2937 N ILE 2256 73.351 20.001 141.391 1.00 29.29 ATOM 2938 CA ILE 2256 73.742 20.275 142.763 1.00 29.70 ATOM 2939 CB ILE 2256 74.964 21.191 142.795 1.00 30.13 ATOM 2940 CG2 ILE 2256 75.252 21.633 144.218 1.00 30.25 ATOM 2941 CG1 ILE 2256 76.149 20.472 142.163 1.00 29.49 ATOM 2942 CD1 ILE 2256 77.398 21.292 142.128 1.00 32.07 ATOM 2943 C ILE 2256 72.593 20.953 143.511 1.00 30.42 ATOM 2944 O ILE 2256 72.040 21.950 143.036 1.00 30.59 ATOM 2945 N LEU 2257 72.234 20.414 144.677 1.00 29.49 ATOM 2946 CA LEU 2257 71.140 20.986 145.453 1.00 29.81 ATOM 2947 CB LEU 2257 70.230 19.888 146.023 1.00 30.16 ATOM 2948 CG LEU 2257 69.651 18.754 145.166 1.00 30.57 ATOM 2949 CD1 LEU 2257 68.237 18.428 145.650 1.00 28.49 ATOM 2950 CD2 LEU 2257 69.619 19.160 143.703 1.00 30.97 ATOM 2951 C LEU 2257 71.681 21.813 146.606 1.00 30.20 ATOM 2952 O LEU 2257 72.579 21.370 147.311 1.00 31.09 ATOM 2953 N GLN 2258 71.137 23.013 146.804 1.00 29.96 ATOM 2954 CA GLN 2258 71.585 23.869 147.902 1.00 28.96 ATOM 2955 CB GLN 2258 70.717 25.122 148.021 1.00 28.83 ATOM 2956 C GLN 2258 71.485 23.092 149.201 1.00 28.90 ATOM 2957 O GLN 2258 70.412 22.631 149.584 1.00 29.36 ATOM 2958 N ALA 2259 72.614 22.935 149.874 1.00 28.31 ATOM 2959 CA ALA 2259 72.637 22.232 151.141 1.00 26.85 ATOM 2960 CB ALA 2259 74.014 22.353 151.773 1.00 26.17 ATOM 2961 C ALA 2259 71.596 22.859 152.057 1.00 26.35 ATOM 2962 O ALA 2259 71.340 24.057 151.989 1.00 26.69 ATOM 2963 N GLY 2260 70.987 22.048 152.908 1.00 26.17 ATOM 2964 CA GLY 2260 70.010 22.580 153.831 1.00 26.69 ATOM 2965 C GLY 2260 68.583 22.528 153.332 1.00 27.47 ATOM 2966 O GLY 2260 67.647 22.592 154.135 1.00 27.56 ATOM 2967 N LEU 2261 68.405 22.433 152.017 1.00 27.03 ATOM 2968 CA LEU 2261 67.066 22.364 151.454 1.00 26.14 ATOM 2969 CB LEU 2261 66.824 23.561 150.548 1.00 23.68 ATOM 2970 CG LEU 2261 67.108 24.907 151.206 1.00 21.44 ATOM 2971 CD1 LEU 2261 66.415 26.001 150.409 1.00 19.96 ATOM 2972 CD2 LEU 2261 66.606 24.901 152.631 1.00 20.06 ATOM 2973 C LEU 2261 66.844 21.055 150.694 1.00 27.99 ATOM 2974 O LEU 2261 67.742 20.569 149.995 1.00 29.22 ATOM 2975 N PRO 2262 65.641 20.461 150.824 1.00 28.27 ATOM 2976 CD PRO 2262 65.334 19.148 150.228 1.00 27.52 ATOM 2977 CA PRO 2262 64.507 20.941 151.626 1.00 27.27 ATOM 2978 CB PRO 2262 63.380 19.991 151.232 1.00 26.90 ATOM 2979 CG PRO 2262 64.107 18.717 151.000 1.00 27.49 ATOM 2980 C PRO 2262 64.822 20.899 153.110 1.00 26.77 ATOM 2981 O PRO 2262 65.772 20.243 153.526 1.00 25.45 ATOM 2982 N ALA 2263 64.025 21.590 153.911 1.00 27.41 ATOM 2983 CA ALA 2263 64.293 21.629 155.342 1.00 28.52 ATOM 2984 CB ALA 2263 64.411 23.068 155.794 1.00 29.22 ATOM 2985 C ALA 2263 63.261 20.915 156.183 1.00 29.21 ATOM 2986 O ALA 2263 62.068 21.002 155.909 1.00 29.99 ATOM 2987 N ASN 2264 63.716 20.213 157.213 1.00 29.48 ATOM 2988 CA ASN 2264 62.782 19.522 158.075 1.00 30.81 ATOM 2989 CB ASN 2264 63.511 18.779 159.183 1.00 31.19 ATOM 2990 CG ASN 2264 64.414 17.697 158.653 1.00 33.95 ATOM 2991 OD1 ASN 2264 64.021 16.915 157.791 1.00 35.19 ATOM 2992 ND2 ASN 2264 65.635 17.635 159.173 1.00 36.12 ATOM 2993 C ASN 2264 61.870 20.562 158.688 1.00 32.46 ATOM 2994 O ASN 2264 62.313 21.654 159.049 1.00 33.58 ATOM 2995 N LYS 2265 60.589 20.242 158.788 1.00 33.38 ATOM 2996 CA LYS 2265 59.651 21.169 159.387 1.00 34.69 ATOM 2997 CB LYS 2265 58.895 21.962 158.325 1.00 33.92 ATOM 2998 CG LYS 2265 59.765 22.767 157.408 1.00 35.31 ATOM 2999 CD LYS 2265 58.923 23.796 156.699 1.00 38.59 ATOM 3000 CE LYS 2265 59.563 24.252 155.406 1.00 40.99 ATOM 3001 NZ LYS 2265 59.557 23.168 154.382 1.00 42.54 ATOM 3002 C LYS 2265 58.660 20.408 160.241 1.00 36.45 ATOM 3003 O LYS 2265 58.172 19.345 159.857 1.00 38.01 ATOM 3004 N THR 2266 58.384 20.950 161.417 1.00 37.19 ATOM 3005 CA THR 2266 57.421 20.365 162.331 1.00 37.14 ATOM 3006 CB THR 2266 58.019 20.261 163.744 1.00 37.39 ATOM 3007 OG1 THR 2266 59.134 19.361 163.715 1.00 37.04 ATOM 3008 CG2 THR 2266 56.994 19.753 164.729 1.00 37.38 ATOM 3009 C THR 2266 56.255 21.343 162.293 1.00 37.21 ATOM 3010 O THR 2266 56.450 22.548 162.427 1.00 36.61 ATOM 3011 N VAL 2267 55.048 20.840 162.069 1.00 38.23 ATOM 3012 CA VAL 2267 53.889 21.723 161.988 1.00 39.46 ATOM 3013 CB VAL 2267 53.548 22.067 160.534 1.00 39.17 ATOM 3014 CG1 VAL 2267 54.768 22.625 159.824 1.00 39.01 ATOM 3015 CG2 VAL 2267 53.027 20.829 159.831 1.00 39.27 ATOM 3016 C VAL 2267 52.635 21.138 162.608 1.00 40.66 ATOM 3017 O VAL 2267 52.543 19.932 162.848 1.00 42.01 ATOM 3018 N ALA 2268 51.664 22.012 162.843 1.00 41.22 ATOM 3019 CA ALA 2268 50.400 21.627 163.439 1.00 41.45 ATOM 3020 CB ALA 2268 49.697 22.853 163.965 1.00 41.09 ATOM 3021 C ALA 2268 49.512 20.910 162.435 1.00 41.95 ATOM 3022 O ALA 2268 49.542 21.197 161.238 1.00 42.09 ATOM 3023 N LEU 2269 48.730 19.962 162.927 1.00 42.41 ATOM 3024 CA LEU 2269 47.826 19.221 162.069 1.00 43.71 ATOM 3025 CB LEU 2269 46.992 18.259 162.922 1.00 44.16 ATOM 3026 CG LEU 2269 45.907 17.412 162.257 1.00 44.43 ATOM 3027 CD1 LEU 2269 45.865 16.040 162.909 1.00 44.37 ATOM 3028 CD2 LEU 2269 44.559 18.122 162.361 1.00 44.90 ATOM 3029 C LEU 2269 46.933 20.226 161.342 1.00 44.37 ATOM 3030 O LEU 2269 46.468 21.193 161.940 1.00 44.68 ATOM 3031 N GLY 2270 46.718 20.016 160.047 1.00 44.77 ATOM 3032 CA GLY 2270 45.873 20.920 159.286 1.00 44.86 ATOM 3033 C GLY 2270 46.569 22.151 158.725 1.00 45.21 ATOM 3034 O GLY 2270 45.978 22.898 157.938 1.00 46.08 ATOM 3035 N SER 2271 47.821 22.368 159.120 1.00 44.66 ATOM 3036 CA SER 2271 48.599 23.514 158.643 1.00 44.47 ATOM 3037 CB SER 2271 49.962 23.551 159.337 1.00 43.11 ATOM 3038 OG SER 2271 49.839 23.441 160.737 1.00 43.71 ATOM 3039 C SER 2271 48.870 23.488 157.134 1.00 44.57 ATOM 3040 O SER 2271 48.425 22.592 156.406 1.00 45.14 ATOM 3041 N ASN 2272 49.622 24.487 156.685 1.00 43.89 ATOM 3042 CA ASN 2272 50.040 24.605 155.290 1.00 43.78 ATOM 3043 CB ASN 2272 49.604 25.931 154.672 1.00 45.49 ATOM 3044 CG ASN 2272 48.121 26.029 154.494 1.00 47.22 ATOM 3045 OD1 ASN 2272 47.515 25.236 153.769 1.00 48.34 ATOM 3046 ND2 ASN 2272 47.514 27.010 155.155 1.00 49.19 ATOM 3047 C ASN 2272 51.553 24.603 155.341 1.00 42.43 ATOM 3048 O ASN 2272 52.146 25.277 156.176 1.00 42.15 ATOM 3049 N VAL 2273 52.185 23.858 154.451 1.00 41.35 ATOM 3050 CA VAL 2273 53.636 23.811 154.445 1.00 40.09 ATOM 3051 CB VAL 2273 54.156 22.581 155.213 1.00 39.83 ATOM 3052 CG1 VAL 2273 53.383 21.362 154.797 1.00 40.44 ATOM 3053 CG2 VAL 2273 55.640 22.369 154.931 1.00 39.62 ATOM 3054 C VAL 2273 54.164 23.747 153.035 1.00 39.30 ATOM 3055 O VAL 2273 53.531 23.169 152.156 1.00 39.51 ATOM 3056 N GLU 2274 55.317 24.360 152.818 1.00 38.06 ATOM 3057 CA GLU 2274 55.926 24.320 151.512 1.00 38.64 ATOM 3058 CB GLU 2274 55.685 25.638 150.763 1.00 40.66 ATOM 3059 CG GLU 2274 56.370 26.881 151.318 1.00 43.80 ATOM 3060 CD GLU 2274 55.780 28.173 150.741 1.00 45.03 ATOM 3061 OE1 GLU 2274 54.604 28.468 151.045 1.00 46.22 ATOM 3062 OE2 GLU 2274 56.479 28.887 149.985 1.00 44.78 ATOM 3063 C GLU 2274 57.410 23.997 151.637 1.00 37.72 ATOM 3064 O GLU 2274 58.132 24.605 152.428 1.00 38.00 ATOM 3065 N PHE 2275 57.843 22.995 150.880 1.00 36.09 ATOM 3066 CA PHE 2275 59.234 22.567 150.882 1.00 34.28 ATOM 3067 CB PHE 2275 59.320 21.059 150.722 1.00 32.50 ATOM 3068 CG PHE 2275 59.230 20.314 152.011 1.00 31.28 ATOM 3069 CD1 PHE 2275 60.273 20.366 152.928 1.00 30.79 ATOM 3070 CD2 PHE 2275 58.113 19.552 152.310 1.00 30.84 ATOM 3071 CE1 PHE 2275 60.206 19.672 154.116 1.00 29.97 ATOM 3072 CE2 PHE 2275 58.035 18.850 153.500 1.00 29.96 ATOM 3073 CZ PHE 2275 59.084 18.910 154.405 1.00 30.45 ATOM 3074 C PHE 2275 59.966 23.238 149.745 1.00 33.99 ATOM 3075 O PHE 2275 59.389 23.511 148.701 1.00 33.87 ATOM 3076 N MET 2276 61.246 23.497 149.933 1.00 33.77 ATOM 3077 CA MET 2276 61.983 24.162 148.890 1.00 34.52 ATOM 3078 CB MET 2276 62.365 25.544 149.387 1.00 37.58 ATOM 3079 CG MET 2276 62.775 26.494 148.306 1.00 43.79 ATOM 3080 SD MET 2276 62.744 28.176 148.933 1.00 52.43 ATOM 3081 CE MET 2276 63.765 28.004 150.468 1.00 49.38 ATOM 3082 C MET 2276 63.207 23.385 148.416 1.00 33.46 ATOM 3083 O MET 2276 63.807 22.615 149.165 1.00 32.44 ATOM 3084 N CYS 2277 63.563 23.586 147.152 1.00 32.65 ATOM 3085 CA CYS 2277 64.700 22.898 146.572 1.00 32.07 ATOM 3086 C CYS 2277 65.361 23.762 145.510 1.00 31.59 ATOM 3087 O CYS 2277 64.772 24.050 144.473 1.00 32.69 ATOM 3088 CB CYS 2277 64.234 21.579 145.967 1.00 31.67 ATOM 3089 SG CYS 2277 65.563 20.403 145.571 1.00 33.74 ATOM 3090 N LYS 2278 66.590 24.179 145.785 1.00 31.20 ATOM 3091 CA LYS 2278 67.360 25.024 144.876 1.00 30.18 ATOM 3092 CB LYS 2278 68.083 26.122 145.672 1.00 28.01 ATOM 3093 C LYS 2278 68.371 24.164 144.119 1.00 29.96 ATOM 3094 O LYS 2278 69.321 23.637 144.707 1.00 30.70 ATOM 3095 N VAL 2279 68.170 24.033 142.811 1.00 28.81 ATOM 3096 CA VAL 2279 69.036 23.201 141.979 1.00 27.68 ATOM 3097 CB VAL 2279 68.186 22.212 141.121 1.00 25.96 ATOM 3098 CG1 VAL 2279 69.068 21.351 140.274 1.00 24.56 ATOM 3099 CG2 VAL 2279 67.352 21.345 142.010 1.00 26.30 ATOM 3100 C VAL 2279 69.950 23.976 141.034 1.00 27.72 ATOM 3101 O VAL 2279 69.568 25.006 140.479 1.00 27.19 ATOM 3102 N TYR 2280 71.171 23.473 140.869 1.00 28.17 ATOM 3103 CA TYR 2280 72.135 24.064 139.947 1.00 27.42 ATOM 3104 CB TYR 2280 73.405 24.525 140.652 1.00 27.41 ATOM 3105 CG TYR 2280 74.394 25.059 139.655 1.00 27.18 ATOM 3106 CD1 TYR 2280 74.222 26.321 139.097 1.00 28.01 ATOM 3107 CE1 TYR 2280 75.029 26.771 138.067 1.00 26.71 ATOM 3108 CD2 TYR 2280 75.417 24.258 139.159 1.00 26.24 ATOM 3109 CE2 TYR 2280 76.231 24.701 138.124 1.00 25.96 ATOM 3110 CZ TYR 2280 76.023 25.959 137.582 1.00 26.31 ATOM 3111 OH TYR 2280 76.780 26.400 136.529 1.00 28.45 ATOM 3112 C TYR 2280 72.520 22.975 138.956 1.00 27.11 ATOM 3113 O TYR 2280 72.691 21.820 139.341 1.00 28.12 ATOM 3114 N SER 2281 72.674 23.337 137.689 1.00 25.08 ATOM 3115 CA SER 2281 73.028 22.359 136.676 1.00 23.95 ATOM 3116 CB SER 2281 71.908 21.324 136.533 1.00 24.09 ATOM 3117 OG SER 2281 72.181 20.398 135.489 1.00 22.96 ATOM 3118 C SER 2281 73.238 23.031 135.345 1.00 23.28 ATOM 3119 O SER 2281 72.375 23.764 134.878 1.00 22.83 ATOM 3120 N ASP 2282 74.380 22.784 134.715 1.00 23.54 ATOM 3121 CA ASP 2282 74.604 23.389 133.422 1.00 22.96 ATOM 3122 CB ASP 2282 76.019 23.128 132.924 1.00 24.67 ATOM 3123 CG ASP 2282 76.314 23.850 131.637 1.00 27.89 ATOM 3124 OG1 ASP 2282 77.502 23.973 131.293 1.00 29.40 ATOM 3125 OD2 ASP 2282 75.358 24.291 130.960 1.00 30.16 ATOM 3126 C ASP 2282 73.563 22.754 132.524 1.00 21.66 ATOM 3127 O ASP 2282 72.618 23.409 132.125 1.00 21.72 ATOM 3128 N PRO 2283 73.695 21.456 132.228 1.00 21.91 ATOM 3129 CD PRO 2283 74.691 20.479 132.692 1.00 22.08 ATOM 3130 CA PRO 2283 72.701 20.802 131.371 1.00 22.90 ATOM 3131 CB PRO 2283 73.166 19.354 131.342 1.00 22.53 ATOM 3132 CG PRO 2283 74.626 19.447 131.616 1.00 21.93 ATOM 3133 C PRO 2283 71.323 20.916 132.019 1.00 23.26 ATOM 3134 O PRO 2283 71.191 20.844 133.240 1.00 22.90 ATOM 3135 N GLN 2284 70.298 21.077 131.203 1.00 23.49 ATOM 3136 CA GLN 2284 68.946 21.192 131.714 1.00 24.43 ATOM 3137 CB GLN 2284 67.964 21.127 130.542 1.00 25.05 ATOM 3138 CG GLN 2284 66.814 22.065 130.681 1.00 25.12 ATOM 3139 CD GLN 2284 67.292 23.440 131.000 1.00 25.68 ATOM 3140 OE1 GLN 2284 67.992 24.077 130.202 1.00 27.13 ATOM 3141 NE2 GLN 2284 66.941 23.914 132.181 1.00 26.58 ATOM 3142 C GLN 2284 68.646 20.052 132.695 1.00 24.85 ATOM 3143 O GLN 2284 68.624 18.881 132.303 1.00 25.65 ATOM 3144 N PRO 2285 68.417 20.373 133.978 1.00 24.45 ATOM 3145 CD PRO 2285 68.537 21.685 134.637 1.00 24.26 ATOM 3146 CA PRO 2285 68.119 19.336 134.969 1.00 24.12 ATOM 3147 CB PRO 2285 68.541 19.980 136.271 1.00 23.75 ATOM 3148 CG PRO 2285 68.097 21.378 136.070 1.00 22.99 ATOM 3149 C PRO 2285 66.637 18.990 134.988 1.00 24.46 ATOM 3150 O PRO 2285 65.787 19.759 134.533 1.00 25.13 ATOM 3151 N HIS 2286 66.327 17.823 135.519 1.00 24.23 ATOM 3152 CA HIS 2286 64.946 17.408 135.620 1.00 24.03 ATOM 3153 CB HIS 2286 64.712 16.157 134.784 1.00 24.57 ATOM 3154 CG HIS 2286 63.319 15.629 134.894 1.00 25.55 ATOM 3155 CD2 HIS 2286 62.275 15.690 134.040 1.00 25.90 ATOM 3156 ND1 HIS 2286 62.853 14.997 136.026 1.00 26.20 ATOM 3157 CE1 HIS 2286 61.580 14.689 135.863 1.00 26.25 ATOM 3158 NE2 HIS 2286 61.205 15.098 134.664 1.00 26.27 ATOM 3159 C HIS 2286 64.615 17.158 137.090 1.00 23.84 ATOM 3160 O HIS 2286 65.011 16.154 137.673 1.00 22.43 ATOM 3161 N ILE 2287 63.896 18.097 137.689 1.00 24.72 ATOM 3162 CA ILE 2287 63.541 18.003 139.095 1.00 25.15 ATOM 3163 CB ILE 2287 63.338 19.400 139.682 1.00 24.12 ATOM 3164 CG2 ILE 2287 63.106 19.311 141.166 1.00 26.07 ATOM 3165 CG1 ILE 2287 64.572 20.248 139.411 1.00 22.78 ATOM 3166 CD1 ILE 2287 64.445 21.660 139.880 1.00 23.38 ATOM 3167 C ILE 2287 62.279 17.188 139.289 1.00 26.72 ATOM 3168 O ILE 2287 61.423 17.134 138.404 1.00 28.94 ATOM 3169 N GLN 2288 62.159 16.560 140.453 1.00 25.98 ATOM 3170 CA GLN 2288 60.998 15.742 140.749 1.00 25.93 ATOM 3171 CB GLN 2288 61.194 14.364 140.128 1.00 26.69 ATOM 3172 CG GLN 2288 59.997 13.458 140.215 1.00 27.14 ATOM 3173 CD GLN 2288 60.212 12.198 139.411 1.00 27.36 ATOM 3174 OE1 GLN 2288 59.344 11.777 138.636 1.00 26.74 ATOM 3175 NE2 GLN 2288 61.376 11.587 139.583 1.00 23.82 ATOM 3176 C GLN 2288 60.834 15.627 142.252 1.00 25.36 ATOM 3177 O GLN 2288 61.803 15.376 142.955 1.00 25.09 ATOM 3178 N TRP 2289 59.615 15.820 142.750 1.00 25.01 ATOM 3179 CA TRP 2289 59.378 15.724 144.188 1.00 24.43 ATOM 3180 CB TRP 2289 58.474 16.848 144.687 1.00 25.01 ATOM 3181 CG TRP 2289 59.160 18.185 144.825 1.00 26.96 ATOM 3182 CD2 TRP 2289 59.838 18.695 145.983 1.00 26.71 ATOM 3183 CE2 TRP 2289 60.271 20.005 145.673 1.00 27.05 ATOM 3184 CE3 TRP 2289 60.118 18.173 147.251 1.00 28.37 ATOM 3185 CD1 TRP 2289 59.218 19.174 143.888 1.00 28.38 ATOM 3186 NE1 TRP 2289 59.880 20.273 144.389 1.00 27.75 ATOM 3187 CZ2 TRP 2289 60.965 20.807 146.586 1.00 28.09 ATOM 3188 CZ3 TRP 2289 60.815 18.975 148.169 1.00 29.60 ATOM 3189 CH2 TRP 2289 61.228 20.278 147.828 1.00 29.72 ATOM 3190 C TRP 2289 58.772 14.389 144.567 1.00 24.28 ATOM 3191 O TRP 2289 57.858 13.915 143.921 1.00 25.11 ATOM 3192 N LEU 2290 59.299 13.784 145.623 1.00 24.33 ATOM 3193 CA LEU 2290 58.830 12.490 146.086 1.00 25.05 ATOM 3194 CB LEU 2290 59.894 11.423 145.890 1.00 24.75 ATOM 3195 CG LEU 2290 60.013 10.744 144.543 1.00 25.63 ATOM 3196 CD1 LEU 2290 60.314 11.755 143.453 1.00 26.85 ATOM 3197 CD2 LEU 2290 61.120 9.737 144.636 1.00 27.55 ATOM 3198 C LEU 2290 58.455 12.456 147.543 1.00 26.65 ATOM 3199 O LEU 2290 58.983 13.210 148.359 1.00 28.27 ATOM 3200 N LYS 2291 57.549 11.544 147.867 1.00 26.88 ATOM 3201 CA LYS 2291 57.109 11.338 149.234 1.00 27.14 ATOM 3202 CB LYS 2291 55.609 11.607 149.350 1.00 26.47 ATOM 3203 CG LYS 2291 54.919 11.054 150.589 1.00 25.04 ATOM 3204 CD LYS 2291 55.424 11.645 151.865 1.00 24.51 ATOM 3205 CE LYS 2291 54.493 11.304 153.015 1.00 24.39 ATOM 3206 NZ LYS 2291 54.334 9.840 153.244 1.00 26.35 ATOM 3207 C LYS 2291 57.430 9.874 149.469 1.00 28.21 ATOM 3208 O LYS 2291 57.182 9.043 148.602 1.00 27.88 ATOM 3209 N HIS 2292 58.018 9.570 150.620 1.00 29.84 ATOM 3210 CA HIS 2292 58.390 8.204 150.954 1.00 31.43 ATOM 3211 CB HIS 2292 59.652 8.193 151.792 1.00 31.88 ATOM 3212 CG HIS 2292 60.871 8.573 151.027 1.00 34.89 ATOM 3213 CD2 HIS 2292 61.500 9.764 150.883 1.00 36.36 ATOM 3214 ND1 HIS 2292 61.561 7.677 150.240 1.00 35.92 ATOM 3215 CE1 HIS 2292 62.563 8.299 149.644 1.00 35.84 ATOM 3216 NE2 HIS 2292 62.548 9.566 150.016 1.00 36.34 ATOM 3217 C HIS 2292 57.282 7.549 151.717 1.00 32.87 ATOM 3218 O HIS 2292 56.847 8.053 152.743 1.00 33.04 ATOM 3219 N ILE 2293 56.841 6.412 151.208 1.00 35.01 ATOM 3220 CA ILE 2293 55.761 5.668 151.812 1.00 37.06 ATOM 3221 CB ILE 2293 54.772 5.220 150.740 1.00 35.63 ATOM 3222 CG2 ILE 2293 53.512 4.692 151.384 1.00 35.81 ATOM 3223 CG1 ILE 2293 54.441 6.399 149.837 1.00 35.30 ATOM 3224 CD1 ILE 2293 53.900 7.592 150.575 1.00 38.63 ATOM 3225 C ILE 2293 56.243 4.438 152.565 1.00 39.27 ATOM 3226 O ILE 2293 57.374 3.979 152.395 1.00 39.33 ATOM 3227 N GLU 2294 55.362 3.926 153.413 1.00 41.94 ATOM 3228 CA GLU 2294 55.619 2.731 154.192 1.00 45.71 ATOM 3229 CB GLU 2294 55.745 3.080 155.680 1.00 44.67 ATOM 3230 C GLU 2294 54.378 1.878 153.936 1.00 48.77 ATOM 3231 O GLU 2294 53.269 2.292 154.270 1.00 49.30 ATOM 3232 N VAL 2295 54.550 0.711 153.316 1.00 52.41 ATOM 3233 CA VAL 2295 53.409 −0.166 153.033 1.00 55.38 ATOM 3234 CB VAL 2295 53.689 −1.086 151.812 1.00 55.33 ATOM 3235 CG1 VAL 2295 52.454 −1.913 151.468 1.00 55.99 ATOM 3236 CG2 VAL 2295 54.073 −0.247 150.618 1.00 55.54 ATOM 3237 C VAL 2295 53.081 −1.003 154.276 1.00 57.06 ATOM 3238 O VAL 2295 52.143 −1.806 154.282 1.00 57.53 ATOM 3239 N ASN 2296 53.871 −0.774 155.324 1.00 58.69 ATOM 3240 CA ASN 2296 53.754 −1.401 156.643 1.00 59.89 ATOM 3241 CB ASN 2296 54.078 −2.893 156.586 1.00 60.71 ATOM 3242 CG ASN 2296 53.175 −3.645 155.646 1.00 63.08 ATOM 3243 OD1 ASN 2296 51.976 −3.787 155.901 1.00 63.11 ATOM 3244 ND2 ASN 2296 53.736 −4.117 154.534 1.00 64.26 ATOM 3245 C ASN 2296 54.845 −0.689 157.427 1.00 60.02 ATOM 3246 O ASN 2296 55.143 0.477 157.164 1.00 59.99 ATOM 3247 N GLY 2297 55.445 −1.380 158.387 1.00 60.38 ATOM 3248 CA GLY 2297 56.538 −0.774 159.122 1.00 59.68 ATOM 3249 C GLY 2297 57.721 −0.845 158.168 1.00 59.19 ATOM 3250 O GLY 2297 58.866 −0.575 158.538 1.00 60.10 ATOM 3251 N SER 2298 57.420 −1.216 156.923 1.00 57.45 ATOM 3252 CA SER 2298 58.413 −1.360 155.868 1.00 55.47 ATOM 3253 CB SER 2298 58.111 −2.601 155.031 1.00 55.58 ATOM 3254 OG SER 2298 56.830 −2.494 154.431 1.00 56.51 ATOM 3255 C SER 2298 58.413 −0.149 154.960 1.00 54.17 ATOM 3256 O SER 2298 57.396 0.183 154.351 1.00 53.71 ATOM 3257 N LYS 2299 59.565 0.503 154.872 1.00 52.79 ATOM 3258 CA LYS 2299 59.717 1.673 154.027 1.00 51.38 ATOM 3259 CB LYS 2299 60.450 2.779 154.795 1.00 51.47 ATOM 3260 CG LYS 2299 59.620 3.315 155.958 1.00 52.71 ATOM 3261 CD LYS 2299 60.371 4.258 156.888 1.00 53.68 ATOM 3262 CE LYS 2299 59.521 4.555 158.132 1.00 54.50 ATOM 3263 NZ LYS 2299 60.194 5.439 159.126 1.00 53.51 ATOM 3264 C LYS 2299 60.490 1.242 152.794 1.00 50.17 ATOM 3265 O LYS 2299 60.744 2.034 151.885 1.00 49.68 ATOM 3266 N ILE 2300 60.841 −0.040 152.770 1.00 48.86 ATOM 3267 CA ILE 2300 61.578 −0.619 151.657 1.00 47.52 ATOM 3268 CB ILE 2300 62.953 −1.145 152.116 1.00 45.85 ATOM 3269 CG2 ILE 2300 63.751 −1.628 150.920 1.00 44.48 ATOM 3270 CG1 ILE 2300 63.726 −0.028 152.810 1.00 44.67 ATOM 3271 CD1 ILE 2300 63.996 1.184 151.917 1.00 43.92 ATOM 3272 C ILE 2300 60.790 −1.763 151.030 1.00 47.39 ATOM 3273 O ILE 2300 60.215 −2.592 151.727 1.00 47.74 ATOM 3274 N GLY 2301 60.767 −1.793 149.704 1.00 47.56 ATOM 3275 CA GLY 2301 60.055 −2.838 148.995 1.00 47.21 ATOM 3276 C GLY 2301 60.917 −4.057 148.717 1.00 47.10 ATOM 3277 O GLY 2301 62.140 −4.031 148.908 1.00 46.68 ATOM 3278 N PRO 2302 60.298 −5.155 148.259 1.00 46.75 ATOM 3279 CD PRO 2302 58.848 −5.306 148.038 1.00 46.14 ATOM 3280 CA PRO 2302 60.998 −6.403 147.949 1.00 45.69 ATOM 3281 CB PRO 2302 59.943 −7.193 147.187 1.00 45.56 ATOM 3282 CG PRO 2302 58.695 −6.813 147.918 1.00 45.16 ATOM 3283 C PRO 2302 62.285 −6.211 147.155 1.00 44.61 ATOM 3284 O PRO 2302 63.273 −6.889 147.411 1.00 44.15 ATOM 3285 N ASP 2303 62.270 −5.285 146.200 1.00 44.35 ATOM 3286 CA ASP 2303 63.447 −5.014 145.377 1.00 43.97 ATOM 3287 CB ASP 2303 63.034 −4.353 144.058 1.00 44.64 ATOM 3288 CG ASP 2303 62.144 −3.146 144.259 1.00 45.77 ATOM 3289 OD1 ASP 2303 61.861 −2.450 143.262 1.00 46.62 ATOM 3290 OD2 ASP 2303 61.719 −2.893 145.407 1.00 46.99 ATOM 3291 C ASP 2303 64.497 −4.144 146.067 1.00 43.64 ATOM 3292 O ASP 2303 65.417 −3.656 145.426 1.00 43.58 ATOM 3293 N ASN 2304 64.356 −3.957 147.373 1.00 43.36 ATOM 3294 CA ASN 2304 65.294 −3.154 148.145 1.00 43.46 ATOM 3295 CB ASN 2304 66.703 −3.767 148.086 1.00 43.04 ATOM 3296 CG ASN 2304 67.536 −3.457 149.334 1.00 42.69 ATOM 3297 OD1 ASN 2304 67.156 −3.807 150.454 1.00 43.07 ATOM 3298 ND2 ASN 2304 68.674 −2.801 149.142 1.00 42.29 ATOM 3299 C ASN 2304 65.330 −1.694 147.685 1.00 43.63 ATOM 3300 O ASN 2304 66.373 −1.032 147.732 1.00 44.41 ATOM 3301 N LEU 2305 64.189 −1.199 147.217 1.00 43.10 ATOM 3302 CA LEU 2305 64.072 0.198 146.806 1.00 42.32 ATOM 3303 CB LEU 2305 63.580 0.335 145.359 1.00 43.10 ATOM 3304 CG LEU 2305 64.518 0.106 144.166 1.00 43.78 ATOM 3305 CD1 LEU 2305 65.804 0.884 144.359 1.00 43.80 ATOM 3306 CD2 LEU 2305 64.821 −1.368 144.028 1.00 44.83 ATOM 3307 C LEU 2305 63.028 0.773 147.748 1.00 41.36 ATOM 3308 O LEU 2305 62.285 0.026 148.377 1.00 41.91 ATOM 3309 N PRO 2306 62.959 2.102 147.866 1.00 39.92 ATOM 3310 CD PRO 2306 63.946 3.081 147.384 1.00 39.37 ATOM 3311 CA PRO 2306 61.980 2.739 148.754 1.00 38.59 ATOM 3312 CB PRO 2306 62.674 4.038 149.126 1.00 38.32 ATOM 3313 CG PRO 2306 63.337 4.402 147.837 1.00 38.73 ATOM 3314 C PRO 2306 60.608 2.989 148.114 1.00 37.71 ATOM 3315 O PRO 2306 60.527 3.486 146.987 1.00 37.51 ATOM 3316 N TYR 2307 59.535 2.643 148.833 1.00 36.33 ATOM 3317 CA TYR 2307 58.180 2.862 148.334 1.00 34.33 ATOM 3318 CB TYR 2307 57.125 2.304 149.286 1.00 34.31 ATOM 3319 CG TYR 2307 57.182 0.824 149.564 1.00 34.95 ATOM 3320 CD1 TYR 2307 57.601 0.353 150.809 1.00 36.33 ATOM 3321 CE1 TYR 2307 57.585 −1.004 151.117 1.00 36.54 ATOM 3322 CD2 TYR 2307 56.753 −0.107 148.620 1.00 35.00 ATOM 3323 CE2 TYR 2307 56.733 −1.476 148.917 1.00 36.35 ATOM 3324 CZ TYR 2307 57.150 −1.914 150.172 1.00 36.96 ATOM 3325 OH TYR 2307 57.129 −3.255 150.495 1.00 36.36 ATOM 3326 C TYR 2307 57.994 4.364 148.276 1.00 33.55 ATOM 3327 O TYR 2307 58.064 5.036 149.292 1.00 33.97 ATOM 3328 N VAL 2308 57.744 4.901 147.098 1.00 32.60 ATOM 3329 CA VAL 2308 57.574 6.337 146.980 1.00 32.06 ATOM 3330 CB VAL 2308 58.792 6.988 146.319 1.00 32.31 ATOM 3331 CG1 VAL 2308 59.938 7.053 147.309 1.00 33.39 ATOM 3332 CG2 VAL 2308 59.193 6.194 145.085 1.00 30.33 ATOM 3333 C VAL 2308 56.356 6.749 146.194 1.00 31.70 ATOM 3334 O VAL 2308 55.769 5.970 145.462 1.00 32.93 ATOM 3335 N GLN 2309 55.992 8.007 146.348 1.00 31.09 ATOM 3336 CA GLN 2309 54.852 8.561 145.656 1.00 30.56 ATOM 3337 CB GLN 2309 53.779 8.899 146.680 1.00 31.43 ATOM 3338 CG GLN 2309 52.448 9.284 146.111 1.00 34.85 ATOM 3339 CD GLN 2309 51.490 9.728 147.202 1.00 37.78 ATOM 3340 OE1 GLN 2309 51.412 9.112 148.273 1.00 39.39 ATOM 3341 NE2 GLN 2309 50.751 10.799 146.936 1.00 39.29 ATOM 3342 C GLN 2309 55.317 9.822 144.914 1.00 29.60 ATOM 3343 O GLN 2309 55.737 10.805 145.530 1.00 30.26 ATOM 3344 N ILE 2310 55.285 9.784 143.589 1.00 27.79 ATOM 3345 CA ILE 2310 55.688 10.948 142.822 1.00 26.22 ATOM 3346 CB ILE 2310 55.675 10.656 141.314 1.00 24.98 ATOM 3347 CG2 ILE 2310 56.189 11.847 140.533 1.00 23.09 ATOM 3348 CG1 ILE 2310 56.533 9.429 141.037 1.00 24.99 ATOM 3349 CD1 ILE 2310 57.879 9.459 141.724 1.00 23.91 ATOM 3350 C ILE 2310 54.658 12.016 143.133 1.00 26.61 ATOM 3351 O ILE 2310 53.460 11.752 143.093 1.00 27.09 ATOM 3352 N LEU 2311 55.117 13.218 143.458 1.00 26.14 ATOM 3353 CA LEU 2311 54.202 14.301 143.785 1.00 25.19 ATOM 3354 CB LEU 2311 54.504 14.839 145.183 1.00 24.23 ATOM 3355 CG LEU 2311 54.577 13.816 146.316 1.00 23.86 ATOM 3356 CD1 LEU 2311 55.022 14.515 147.555 1.00 25.05 ATOM 3357 CD2 LEU 2311 53.242 13.158 146.551 1.00 22.35 ATOM 3358 C LEU 2311 54.261 15.448 142.790 1.00 25.59 ATOM 3359 O LEU 2311 53.276 16.156 142.600 1.00 26.28 ATOM 3360 N LYS 2312 55.405 15.620 142.142 1.00 25.78 ATOM 3361 CA LYS 2312 55.592 16.714 141.197 1.00 25.94 ATOM 3362 CB LYS 2312 55.973 17.969 141.988 1.00 26.21 ATOM 3363 CG LYS 2312 55.700 19.283 141.305 1.00 27.55 ATOM 3364 CD LYS 2312 55.687 20.408 142.335 1.00 27.49 ATOM 3365 CE LYS 2312 55.331 21.753 141.713 1.00 26.53 ATOM 3366 NZ LYS 2312 55.102 22.769 142.780 1.00 26.35 ATOM 3367 C LYS 2312 56.701 16.320 140.220 1.00 26.55 ATOM 3368 O LYS 2312 57.722 15.756 140.625 1.00 27.08 ATOM 3369 N THR 2313 56.509 16.610 138.937 1.00 26.65 ATOM 3370 CA THR 2313 57.507 16.237 137.937 1.00 27.27 ATOM 3371 CB THR 2313 57.049 15.020 137.142 1.00 25.47 ATOM 3372 OG1 THR 2313 55.968 14.397 137.834 1.00 26.44 ATOM 3373 CG2 THR 2313 58.172 14.024 136.977 1.00 24.30 ATOM 3374 C THR 2313 57.726 17.347 136.938 1.00 28.50 ATOM 3375 O THR 2313 56.771 17.827 136.333 1.00 29.05 ATOM 3376 N ALA 2314 58.981 17.737 136.744 1.00 29.23 ATOM 3377 CA ALA 2314 59.301 18.800 135.806 1.00 30.80 ATOM 3378 CB ALA 2314 60.802 19.052 135.807 1.00 31.98 ATOM 3379 C ALA 2314 58.836 18.425 134.409 1.00 31.39 ATOM 3380 O ALA 2314 58.810 17.249 134.051 1.00 32.01 ATOM 3381 N GLY 2315 58.470 19.426 133.617 1.00 31.57 ATOM 3382 CA GLY 2315 58.026 19.151 132.265 1.00 31.47 ATOM 3383 C GLY 2315 57.150 20.257 131.726 1.00 32.10 ATOM 3384 O GLY 2315 56.911 21.264 132.394 1.00 32.59 ATOM 3385 N VAL 2316 56.656 20.065 130.514 1.00 32.49 ATOM 3386 CA VAL 2316 55.811 21.055 129.881 1.00 33.21 ATOM 3387 CB VAL 2316 55.371 20.559 128.509 1.00 32.94 ATOM 3388 CG1 VAL 2316 54.382 21.522 127.913 1.00 36.27 ATOM 3389 CG2 VAL 2316 56.581 20.426 127.602 1.00 31.90 ATOM 3390 C VAL 2316 54.582 21.416 130.710 1.00 34.17 ATOM 3391 O VAL 2316 54.135 22.554 130.704 1.00 34.38 ATOM 3392 N ASN 2317 54.040 20.452 131.433 1.00 36.03 ATOM 3393 CA ASN 2317 52.853 20.715 132.233 1.00 37.90 ATOM 3394 CB ASN 2317 52.062 19.416 132.430 1.00 41.91 ATOM 3395 CG ASN 2317 51.529 18.844 131.115 1.00 44.25 ATOM 3396 OD1 ASN 2317 51.106 17.688 131.060 1.00 46.64 ATOM 3397 ND2 ASN 2317 51.539 19.656 130.058 1.00 44.82 ATOM 3398 C ASN 2317 53.196 21.336 133.578 1.00 37.48 ATOM 3399 O ASN 2317 52.357 21.998 134.204 1.00 38.61 ATOM 3400 N THR 2318 54.436 21.127 134.003 1.00 35.92 ATOM 3401 CA THR 2318 54.920 21.636 135.268 1.00 34.27 ATOM 3402 CB THR 2318 55.033 20.511 136.263 1.00 34.40 ATOM 3403 OG1 THR 2318 53.888 19.665 136.140 1.00 34.31 ATOM 3404 CG2 THR 2318 55.112 21.061 137.669 1.00 36.18 ATOM 3405 C THR 2318 56.302 22.168 135.001 1.00 33.31 ATOM 3406 O THR 2318 57.287 21.446 135.144 1.00 33.84 ATOM 3407 N THR 2319 56.372 23.429 134.608 1.00 31.80 ATOM 3408 CA THR 2319 57.637 24.061 134.288 1.00 30.00 ATOM 3409 CB THR 2319 57.360 25.345 133.542 1.00 29.99 ATOM 3410 OG1 THR 2319 56.618 25.018 132.363 1.00 26.20 ATOM 3411 CG2 THR 2319 58.658 26.054 133.166 1.00 31.40 ATOM 3412 C THR 2319 58.546 24.312 135.485 1.00 29.12 ATOM 3413 O THR 2319 58.094 24.386 136.624 1.00 29.08 ATOM 3414 N ASP 2320 59.836 24.441 135.212 1.00 28.31 ATOM 3415 CA ASP 2320 60.807 24.655 136.260 1.00 28.93 ATOM 3416 CB ASP 2320 62.215 24.767 135.625 1.00 25.80 ATOM 3417 CG ASP 2320 62.652 23.462 134.890 1.00 24.47 ATOM 3418 OD1 ASP 2320 62.224 22.354 135.281 1.00 22.80 ATOM 3419 OD2 ASP 2320 63.447 23.527 133.925 1.00 22.27 ATOM 3420 C ASP 2320 60.451 25.857 137.164 1.00 31.01 ATOM 3421 O ASP 2320 60.950 25.977 138.281 1.00 32.39 ATOM 3422 N LYS 2321 59.558 26.723 136.697 1.00 33.47 ATOM 3423 CA LYS 2321 59.140 27.884 137.476 1.00 35.16 ATOM 3424 CB LYS 2321 58.009 28.623 136.758 1.00 36.60 ATOM 3425 CG LYS 2321 58.167 28.692 135.255 1.00 40.39 ATOM 3426 CD LYS 2321 56.971 29.396 134.595 1.00 43.03 ATOM 3427 CE LYS 2321 56.860 29.066 133.076 1.00 43.90 ATOM 3428 NZ LYS 2321 58.066 29.382 132.239 1.00 40.93 ATOM 3429 C LYS 2321 58.635 27.442 138.846 1.00 36.16 ATOM 3430 O LYS 2321 59.090 27.923 139.882 1.00 37.35 ATOM 3431 N GLU 2322 57.687 26.516 138.843 1.00 36.64 ATOM 3432 CA GLU 2322 57.104 26.038 140.082 1.00 38.06 ATOM 3433 CB GLU 2322 55.611 25.818 139.876 1.00 40.30 ATOM 3434 CG GLU 2322 55.279 25.252 138.516 1.00 42.80 ATOM 3435 CD GLU 2322 53.782 25.177 138.265 1.00 45.28 ATOM 3436 OE1 GLU 2322 53.099 24.367 138.938 1.00 46.14 ATOM 3437 OE2 GLU 2322 53.291 25.932 137.393 1.00 45.44 ATOM 3438 C GLU 2322 57.727 24.785 140.674 1.00 37.57 ATOM 3439 O GLU 2322 57.266 24.299 141.703 1.00 37.88 ATOM 3440 N MET 2323 58.782 24.274 140.051 1.00 37.12 ATOM 3441 CA MET 2323 59.422 23.054 140.533 1.00 36.36 ATOM 3442 CB MET 2323 60.233 22.387 139.413 1.00 35.76 ATOM 3443 CG MET 2323 59.388 21.689 138.343 1.00 34.71 ATOM 3444 SD MET 2323 58.178 20.516 139.009 1.00 33.46 ATOM 3445 CE MET 2323 59.263 19.280 139.761 1.00 34.08 ATOM 3446 C MET 2323 60.308 23.200 141.755 1.00 36.28 ATOM 3447 O MET 2323 60.597 22.213 142.426 1.00 35.30 ATOM 3448 N GLU 2324 60.744 24.411 142.063 1.00 37.11 ATOM 3449 CA GLU 2324 61.601 24.563 143.227 1.00 38.55 ATOM 3450 CB GLU 2324 62.547 25.750 143.028 1.00 40.58 ATOM 3451 CG GLU 2324 63.556 25.485 141.907 1.00 42.57 ATOM 3452 CD GLU 2324 64.704 26.486 141.850 1.00 43.05 ATOM 3453 OE1 GLU 2324 64.438 27.689 141.632 1.00 44.25 ATOM 3454 OE2 GLU 2324 65.873 26.063 142.014 1.00 41.59 ATOM 3455 C GLU 2324 60.855 24.653 144.565 1.00 38.27 ATOM 3456 O GLU 2324 61.471 24.819 145.616 1.00 37.49 ATOM 3457 N VAL 2325 59.533 24.503 144.532 1.00 37.66 ATOM 3458 CA VAL 2325 58.750 24.565 145.754 1.00 37.45 ATOM 3459 CB VAL 2325 58.252 25.987 146.008 1.00 37.38 ATOM 3460 CG1 VAL 2325 57.319 26.409 144.893 1.00 38.00 ATOM 3461 CG2 VAL 2325 57.548 26.056 147.342 1.00 38.48 ATOM 3462 C VAL 2325 57.550 23.620 145.747 1.00 37.40 ATOM 3463 O VAL 2325 56.720 23.649 144.841 1.00 38.13 ATOM 3464 N LEU 2326 57.469 22.788 146.781 1.00 37.18 ATOM 3465 CA LEU 2326 56.392 21.815 146.936 1.00 36.35 ATOM 3466 CB LEU 2326 56.961 20.471 147.396 1.00 34.79 ATOM 3467 CG LEU 2326 55.955 19.339 147.516 1.00 33.40 ATOM 3468 CD1 LEU 2326 55.279 19.158 146.182 1.00 33.58 ATOM 3469 CD2 LEU 2326 56.657 18.064 147.931 1.00 31.96 ATOM 3470 C LEU 2326 55.403 22.321 147.974 1.00 37.00 ATOM 3471 O LEU 2326 55.769 22.553 149.125 1.00 36.12 ATOM 3472 N HIS 2327 54.149 22.489 147.564 1.00 38.27 ATOM 3473 CA HIS 2327 53.112 22.975 148.466 1.00 38.34 ATOM 3474 CB HIS 2327 52.195 23.963 147.741 1.00 40.16 ATOM 3475 CG HIS 2327 52.866 25.242 147.342 1.00 43.09 ATOM 3476 CD2 HIS 2327 53.264 25.701 146.130 1.00 42.98 ATOM 3477 ND1 HIS 2327 53.198 26.226 148.252 1.00 43.74 ATOM 3478 CE1 HIS 2327 53.768 27.236 147.617 1.00 43.62 ATOM 3479 NE2 HIS 2327 53.821 26.943 146.329 1.00 44.01 ATOM 3480 C HIS 2327 52.269 21.835 149.018 1.00 38.16 ATOM 3481 O HIS 2327 51.658 21.074 148.267 1.00 38.38 ATOM 3482 N LEU 2328 52.244 21.720 150.340 1.00 37.91 ATOM 3483 CA LEU 2328 51.461 20.696 151.012 1.00 37.84 ATOM 3484 CB LEU 2328 52.318 19.939 152.034 1.00 36.72 ATOM 3485 CG LEU 2328 53.402 18.969 151.535 1.00 36.31 ATOM 3486 CD1 LEU 2328 54.295 18.550 152.683 1.00 35.20 ATOM 3487 CD2 LEU 2328 52.757 17.751 150.909 1.00 36.53 ATOM 3488 C LEU 2328 50.362 21.449 151.725 1.00 39.07 ATOM 3489 O LEU 2328 50.593 22.023 152.789 1.00 39.32 ATOM 3490 N ARG 2329 49.169 21.459 151.137 1.00 40.36 ATOM 3491 CA ARG 2329 48.052 22.175 151.738 1.00 41.25 ATOM 3492 CB ARG 2329 47.116 22.703 150.650 1.00 41.14 ATOM 3493 C ARG 2329 47.273 21.355 152.769 1.00 42.07 ATOM 3494 O ARG 2329 47.039 20.154 152.601 1.00 41.21 ATOM 3495 N ASN 2330 46.897 22.039 153.847 1.00 43.83 ATOM 3496 CA ASN 2330 46.151 21.463 154.962 1.00 45.93 ATOM 3497 CB ASN 2330 44.652 21.498 154.676 1.00 49.05 ATOM 3498 CG ASN 2330 43.834 21.086 155.877 1.00 52.00 ATOM 3499 OD1 ASN 2330 43.787 19.907 156.235 1.00 53.82 ATOM 3500 ND2 ASN 2330 43.201 22.063 156.527 1.00 53.24 ATOM 3501 C ASN 2330 46.576 20.043 155.276 1.00 45.58 ATOM 3502 O ASN 2330 45.868 19.085 154.973 1.00 45.29 ATOM 3503 N VAL 2331 47.733 19.928 155.914 1.00 45.27 ATOM 3504 CA VAL 2331 48.328 18.647 156.266 1.00 44.77 ATOM 3505 CB VAL 2331 49.705 18.893 156.864 1.00 43.57 ATOM 3506 CG1 VAL 2331 50.467 19.858 155.978 1.00 42.63 ATOM 3507 CG2 VAL 2331 49.566 19.469 158.248 1.00 42.71 ATOM 3508 C VAL 2331 47.520 17.772 157.218 1.00 44.99 ATOM 3509 O VAL 2331 46.598 18.235 157.878 1.00 46.10 ATOM 3510 N SER 2332 47.891 16.499 157.278 1.00 45.10 ATOM 3511 CA SER 2332 47.237 15.517 158.131 1.00 45.49 ATOM 3512 CB SER 2332 46.184 14.756 157.334 1.00 44.55 ATOM 3513 OG SER 2332 46.716 14.303 156.100 1.00 42.28 ATOM 3514 C SER 2332 48.304 14.555 158.612 1.00 46.64 ATOM 3515 O SER 2332 49.397 14.523 158.056 1.00 47.33 ATOM 3516 N PHE 2333 47.994 13.770 159.639 1.00 47.66 ATOM 3517 CA PHE 2333 48.956 12.812 160.168 1.00 48.81 ATOM 3518 CB PHE 2333 48.298 11.942 161.235 1.00 50.74 ATOM 3519 CG PHE 2333 48.494 12.451 162.627 1.00 53.07 ATOM 3520 CD1 PHE 2333 48.721 11.561 163.679 1.00 54.72 ATOM 3521 CD2 PHE 2333 48.475 13.817 162.890 1.00 53.83 ATOM 3522 CE1 PHE 2333 48.932 12.026 164.984 1.00 56.27 ATOM 3523 CE2 PHE 2333 48.684 14.298 164.184 1.00 56.09 ATOM 3524 CZ PHE 2333 48.914 13.397 165.238 1.00 56.78 ATOM 3525 C PHE 2333 49.532 11.927 159.065 1.00 48.00 ATOM 3526 O PHE 2333 50.653 11.419 159.167 1.00 47.65 ATOM 3527 N GLU 2334 48.749 11.756 158.009 1.00 47.38 ATOM 3528 CA GLU 2334 49.150 10.937 156.882 1.00 46.61 ATOM 3529 CB GLU 2334 47.984 10.764 155.897 1.00 48.93 ATOM 3530 CG GLU 2334 46.775 9.973 156.415 1.00 53.50 ATOM 3531 CD GLU 2334 45.860 10.760 157.379 1.00 57.12 ATOM 3532 OE1 GLU 2334 46.224 10.929 158.572 1.00 58.37 ATOM 3533 OE2 GLU 2334 44.768 11.208 156.941 1.00 57.75 ATOM 3534 C GLU 2334 50.318 11.595 156.170 1.00 44.79 ATOM 3535 O GLU 2334 51.326 10.955 155.895 1.00 44.39 ATOM 3536 N ASP 2335 50.181 12.882 155.879 1.00 42.84 ATOM 3537 CA ASP 2335 51.230 13.618 155.181 1.00 41.47 ATOM 3538 CB ASP 2335 50.817 15.073 154.958 1.00 42.11 ATOM 3539 CG ASP 2335 49.568 15.199 154.119 1.00 42.52 ATOM 3540 OD1 ASP 2335 49.399 14.405 153.163 1.00 40.64 ATOM 3541 OD2 ASP 2335 48.763 16.110 154.414 1.00 43.61 ATOM 3542 C ASP 2335 52.559 13.594 155.920 1.00 39.66 ATOM 3543 O ASP 2335 53.599 13.957 155.370 1.00 38.79 ATOM 3544 N ALA 2336 52.523 13.178 157.176 1.00 37.90 ATOM 3545 CA ALA 2336 53.732 13.110 157.972 1.00 35.84 ATOM 3546 CB ALA 2336 53.402 12.565 159.357 1.00 35.87 ATOM 3547 C ALA 2336 54.711 12.193 157.257 1.00 34.69 ATOM 3548 O ALA 2336 54.307 11.198 156.646 1.00 34.69 ATOM 3549 N GLY 2337 55.994 12.523 157.318 1.00 32.66 ATOM 3550 CA GLY 2337 56.966 11.679 156.659 1.00 31.48 ATOM 3551 C GLY 2337 58.111 12.389 155.972 1.00 30.67 ATOM 3552 O GLY 2337 58.294 13.590 156.108 1.00 30.86 ATOM 3553 N GLU 2338 58.879 11.624 155.211 1.00 29.73 ATOM 3554 CA GLU 2338 60.037 12.137 154.515 1.00 29.01 ATOM 3555 CB GLU 2338 61.181 11.145 154.647 1.00 29.00 ATOM 3556 CG GLU 2338 62.364 11.401 153.752 1.00 29.50 ATOM 3557 CD GLU 2338 63.415 10.343 153.957 1.00 30.76 ATOM 3558 OE1 GLU 2338 63.021 9.169 154.106 1.00 31.01 ATOM 3559 OE2 GLU 2338 64.622 10.668 153.974 1.00 31.61 ATOM 3560 C GLU 2338 59.799 12.436 153.052 1.00 28.96 ATOM 3561 O GLU 2338 59.389 11.573 152.284 1.00 30.22 ATOM 3562 N TYR 2339 60.071 13.672 152.668 1.00 27.97 ATOM 3563 CA TYR 2339 59.906 14.075 151.291 1.00 27.40 ATOM 3564 CB TYR 2339 59.145 15.395 151.216 1.00 27.47 ATOM 3565 CG TYR 2339 57.696 15.266 151.646 1.00 28.45 ATOM 3566 CD1 TYR 2339 57.359 14.954 152.970 1.00 27.51 ATOM 3567 CE1 TYR 2339 56.035 14.821 153.361 1.00 26.85 ATOM 3568 CD2 TYR 2339 56.658 15.441 150.724 1.00 27.65 ATOM 3569 CE2 TYR 2339 55.338 15.310 151.106 1.00 26.77 ATOM 3570 CZ TYR 2339 55.031 15.001 152.422 1.00 27.88 ATOM 3571 OH TYR 2339 53.710 14.862 152.783 1.00 30.57 ATOM 3572 C TYR 2339 61.286 14.200 150.670 1.00 27.30 ATOM 3573 O TYR 2339 62.271 14.467 151.360 1.00 27.32 ATOM 3574 N THR 2340 61.354 14.004 149.360 1.00 26.14 ATOM 3575 CA THR 2340 62.623 14.057 148.677 1.00 25.92 ATOM 3576 CB THR 2340 63.077 12.645 148.289 1.00 25.98 ATOM 3577 OG1 THR 2340 63.349 11.894 149.477 1.00 26.37 ATOM 3578 CG2 THR 2340 64.316 12.700 147.426 1.00 24.86 ATOM 3579 C THR 2340 62.582 14.891 147.424 1.00 26.30 ATOM 3580 O THR 2340 61.628 14.830 146.662 1.00 26.81 ATOM 3581 N CYS 2341 63.627 15.679 147.224 1.00 26.04 ATOM 3582 CA CYS 2341 63.723 16.482 146.035 1.00 26.62 ATOM 3583 C CYS 2341 64.785 15.782 145.252 1.00 27.07 ATOM 3584 O CYS 2341 65.926 15.682 145.698 1.00 28.08 ATOM 3585 CB CYS 2341 64.186 17.890 146.341 1.00 28.45 ATOM 3586 SG CYS 2341 64.529 18.842 144.834 1.00 26.76 ATOM 3587 N LEU 2342 64.394 15.280 144.092 1.00 27.03 ATOM 3588 CA LEU 2342 65.290 14.552 143.221 1.00 26.61 ATOM 3589 CB LEU 2342 64.696 13.172 142.917 1.00 25.47 ATOM 3590 CG LEU 2342 65.260 12.404 141.723 1.00 26.27 ATOM 3591 CD1 LEU 2342 66.785 12.333 141.808 1.00 26.88 ATOM 3592 CD2 LEU 2342 64.648 11.020 141.685 1.00 25.17 ATOM 3593 C LEU 2342 65.473 15.330 141.940 1.00 27.03 ATOM 3594 O LEU 2342 64.501 15.725 141.301 1.00 29.20 ATOM 3595 N ALA 2343 66.722 15.561 141.565 1.00 25.87 ATOM 3596 CA ALA 2343 67.009 16.282 140.339 1.00 24.38 ATOM 3597 CB ALA 2343 67.383 17.698 140.648 1.00 25.43 ATOM 3598 C ALA 2343 68.159 15.582 139.658 1.00 23.96 ATOM 3599 O ALA 2343 69.145 15.229 140.300 1.00 22.49 ATOM 3600 N GLY 2344 68.031 15.365 138.357 1.00 23.92 ATOM 3601 CA GLY 2344 69.092 14.693 137.644 1.00 24.37 ATOM 3602 C GLY 2344 69.197 15.126 136.206 1.00 25.75 ATOM 3603 O GLY 2344 68.211 15.535 135.602 1.00 27.54 ATOM 3604 N ASN 2345 70.405 15.068 135.666 1.00 26.24 ATOM 3605 CA ASN 2345 70.623 15.412 134.277 1.00 26.80 ATOM 3606 CB ASN 2345 71.532 16.641 134.132 1.00 26.94 ATOM 3607 CG ASN 2345 72.889 16.461 134.784 1.00 26.87 ATOM 3608 OD1 ASN 2345 73.504 15.402 134.694 1.00 27.94 ATOM 3609 ND2 ASN 2345 73.375 17.514 135.427 1.00 26.75 ATOM 3610 C ASN 2345 71.259 14.193 133.632 1.00 27.51 ATOM 3611 O ASN 2345 71.281 13.116 134.225 1.00 25.72 ATOM 3612 N SER 2346 71.779 14.363 132.425 1.00 28.32 ATOM 3613 CA SER 2346 72.400 13.261 131.709 1.00 29.50 ATOM 3614 CB SER 2346 72.668 13.698 130.268 1.00 30.89 ATOM 3615 OG SER 2346 73.341 12.687 129.542 1.00 31.93 ATOM 3616 C SER 2346 73.700 12.742 132.324 1.00 28.96 ATOM 3617 O SER 2346 74.239 11.736 131.880 1.00 30.38 ATOM 3618 N ILE 2347 74.206 13.418 133.343 1.00 28.17 ATOM 3619 CA ILE 2347 75.463 13.012 133.948 1.00 28.00 ATOM 3620 CB ILE 2347 76.346 14.236 134.206 1.00 26.86 ATOM 3621 CG2 ILE 2347 77.646 13.823 134.859 1.00 25.01 ATOM 3622 CG1 ILE 2347 76.607 14.955 132.886 1.00 27.00 ATOM 3623 CD1 ILE 2347 77.300 16.281 133.041 1.00 26.83 ATOM 3624 C ILE 2347 75.292 12.257 135.247 1.00 29.80 ATOM 3625 O ILE 2347 76.087 11.374 135.568 1.00 30.99 ATOM 3626 N GLY 2348 74.266 12.605 136.010 1.00 30.31 ATOM 3627 CA GLY 2348 74.052 11.918 137.267 1.00 31.07 ATOM 3628 C GLY 2348 72.780 12.343 137.966 1.00 31.25 ATOM 3629 O GLY 2348 72.037 13.181 137.449 1.00 32.24 ATOM 3630 N LEU 2349 72.530 11.763 139.139 1.00 29.67 ATOM 3631 CA LEU 2349 71.345 12.083 139.918 1.00 28.44 ATOM 3632 CB LEU 2349 70.467 10.851 140.109 1.00 29.09 ATOM 3633 CG LEU 2349 69.628 10.359 138.930 1.00 31.74 ATOM 3634 CD1 LEU 2349 68.586 11.417 138.581 1.00 31.84 ATOM 3635 CD2 LEU 2349 70.528 10.034 137.729 1.00 32.28 ATOM 3636 C LEU 2349 71.721 12.613 141.286 1.00 27.83 ATOM 3637 O LEU 2349 72.689 12.154 141.890 1.00 27.97 ATOM 3638 N SER 2350 70.946 13.583 141.766 1.00 26.94 ATOM 3639 CA SER 2350 71.151 14.188 143.076 1.00 24.05 ATOM 3640 CB SER 2350 71.825 15.551 142.958 1.00 22.64 ATOM 3641 OG SER 2350 73.228 15.423 142.889 1.00 21.98 ATOM 3642 C SER 2350 69.803 14.362 143.730 1.00 24.25 ATOM 3643 O SER 2350 68.796 14.580 143.055 1.00 24.27 ATOM 3644 N HIS 2351 69.784 14.268 145.051 1.00 24.81 ATOM 3645 CA HIS 2351 68.545 14.413 145.791 1.00 25.48 ATOM 3646 CB HIS 2351 67.769 13.106 145.770 1.00 26.54 ATOM 3647 CG HIS 2351 68.520 11.963 146.377 1.00 28.96 ATOM 3648 CD2 HIS 2351 68.539 11.479 147.642 1.00 30.01 ATOM 3649 ND1 HIS 2351 69.435 11.213 145.667 1.00 29.42 ATOM 3650 CE1 HIS 2351 69.983 10.316 146.466 1.00 30.00 ATOM 3651 NE2 HIS 2351 69.458 10.457 147.670 1.00 31.92 ATOM 3652 C HIS 2351 68.808 14.777 147.235 1.00 25.95 ATOM 3653 O HIS 2351 69.811 14.378 147.809 1.00 26.85 ATOM 3654 N HIS 2352 67.890 15.539 147.816 1.00 26.51 ATOM 3655 CA HIS 2352 67.967 15.941 149.215 1.00 26.09 ATOM 3656 CB HIS 2352 68.141 17.444 149.350 1.00 26.91 ATOM 3657 CG HIS 2352 69.542 17.904 149.164 1.00 27.75 ATOM 3658 CD2 HIS 2352 70.689 17.210 148.980 1.00 28.62 ATOM 3659 ND1 HIS 2352 69.894 19.235 149.191 1.00 27.71 ATOM 3660 CE1 HIS 2352 71.200 19.341 149.036 1.00 29.91 ATOM 3661 NE2 HIS 2352 71.707 18.126 148.905 1.00 29.86 ATOM 3662 C HIS 2352 66.632 15.582 149.812 1.00 26.59 ATOM 3663 O HIS 2352 65.600 15.862 149.216 1.00 27.59 ATOM 3664 N SER 2353 66.638 14.959 150.978 1.00 26.84 ATOM 3665 CA SER 2353 65.383 14.603 151.615 1.00 27.71 ATOM 3666 CB SER 2353 65.453 13.186 152.165 1.00 27.98 ATOM 3667 OG SER 2353 65.621 12.260 151.105 1.00 29.93 ATOM 3668 C SER 2353 65.100 15.588 152.730 1.00 28.03 ATOM 3669 O SER 2353 65.860 16.533 152.930 1.00 29.62 ATOM 3670 N ALA 2354 63.999 15.381 153.440 1.00 27.45 ATOM 3671 CA ALA 2354 63.613 16.252 154.548 1.00 27.88 ATOM 3672 CB ALA 2354 63.217 17.614 154.052 1.00 28.75 ATOM 3673 C ALA 2354 62.438 15.600 155.226 1.00 28.41 ATOM 3674 O ALA 2354 61.669 14.895 154.586 1.00 29.30 ATOM 3675 N TRP 2355 62.292 15.837 156.519 1.00 28.44 ATOM 3676 CA TRP 2355 61.210 15.231 157.248 1.00 28.71 ATOM 3677 CB TRP 2355 61.763 14.530 158.468 1.00 31.13 ATOM 3678 CG TRP 2355 61.507 13.072 158.407 1.00 37.37 ATOM 3679 CD2 TRP 2355 62.409 12.078 157.920 1.00 38.88 ATOM 3680 CE2 TRP 2355 61.718 10.838 157.941 1.00 39.14 ATOM 3681 CE3 TRP 2355 63.735 12.113 157.463 1.00 39.77 ATOM 3682 CD1 TRP 2355 60.331 12.415 158.706 1.00 38.18 ATOM 3683 NE1 TRP 2355 60.455 11.074 158.425 1.00 38.62 ATOM 3684 CZ2 TRP 2355 62.311 9.646 157.519 1.00 39.98 ATOM 3685 CZ3 TRP 2355 64.324 10.932 157.044 1.00 40.99 ATOM 3686 CH2 TRP 2355 63.610 9.710 157.074 1.00 40.93 ATOM 3687 C TRP 2355 60.099 16.170 157.663 1.00 28.81 ATOM 3688 O TRP 2355 60.348 17.281 158.121 1.00 29.84 ATOM 3689 N LEU 2356 58.862 15.727 157.484 1.00 28.47 ATOM 3690 CA LEU 2356 57.719 16.526 157.889 1.00 27.92 ATOM 3691 CB LEU 2356 56.648 16.570 156.805 1.00 26.20 ATOM 3692 CG LEU 2356 55.726 17.794 156.877 1.00 26.11 ATOM 3693 CD1 LEU 2356 54.319 17.376 156.538 1.00 26.99 ATOM 3694 CD2 LEU 2356 55.747 18.427 158.253 1.00 25.04 ATOM 3695 C LEU 2356 57.134 15.882 159.151 1.00 28.92 ATOM 3696 O LEU 2356 56.722 14.716 159.143 1.00 28.83 ATOM 3697 N THR 2357 57.135 16.648 160.238 1.00 29.45 ATOM 3698 CA THR 2357 56.602 16.201 161.522 1.00 30.00 ATOM 3699 CB THR 2357 57.582 16.504 162.694 1.00 28.55 ATOM 3700 OG1 THR 2357 58.603 15.505 162.745 1.00 29.02 ATOM 3701 CG2 THR 2357 56.849 16.510 164.016 1.00 26.69 ATOM 3702 C THR 2357 55.288 16.939 161.783 1.00 32.06 ATOM 3703 O THR 2357 55.259 18.175 161.827 1.00 32.27 ATOM 3704 N VAL 2358 54.206 16.181 161.956 1.00 33.20 ATOM 3705 CA VAL 2358 52.898 16.772 162.211 1.00 34.64 ATOM 3706 CB VAL 2358 51.846 16.259 161.211 1.00 35.47 ATOM 3707 CG1 VAL 2358 50.480 16.796 161.586 1.00 35.84 ATOM 3708 CG2 VAL 2358 52.209 16.696 159.797 1.00 36.10 ATOM 3709 C VAL 2358 52.400 16.476 163.621 1.00 35.63 ATOM 3710 O VAL 2358 52.435 15.330 164.071 1.00 36.05 ATOM 3711 N LEU 2359 51.924 17.511 164.311 1.00 35.87 ATOM 3712 CA LEU 2359 51.424 17.340 165.668 1.00 35.60 ATOM 3713 CB LEU 2359 52.380 18.055 166.616 1.00 33.76 ATOM 3714 CG LEU 2359 53.810 17.511 166.468 1.00 33.43 ATOM 3715 CD1 LEU 2359 54.807 18.419 167.188 1.00 30.83 ATOM 3716 CD2 LEU 2359 53.874 16.071 167.002 1.00 31.95 ATOM 3717 C LEU 2359 49.973 17.824 165.846 1.00 36.53 ATOM 3718 O LEU 2359 49.261 17.260 166.716 1.00 36.43 ATOM 3719 CB MET 3149 110.903 20.490 84.760 1.00 57.84 ATOM 3720 CG MET 3149 112.225 20.282 85.488 1.00 60.66 ATOM 3721 SD MET 3149 113.293 19.105 84.603 1.00 64.12 ATOM 3722 CE MET 3149 114.208 20.229 83.476 1.00 62.64 ATOM 3723 C MET 3149 109.773 18.509 85.792 1.00 53.78 ATOM 3724 O MET 3149 109.675 19.157 86.834 1.00 53.83 ATOM 3725 N MET 3149 108.962 19.445 83.629 1.00 55.00 ATOM 3726 CA MET 3149 110.163 19.183 84.475 1.00 55.34 ATOM 3727 N PRO 3150 109.571 17.185 85.762 1.00 52.17 ATOM 3728 CD PRO 3150 109.866 16.279 84.640 1.00 51.98 ATOM 3729 CA PRO 3150 109.183 16.418 86.948 1.00 50.85 ATOM 3730 CB PRO 3150 109.140 14.979 86.435 1.00 49.99 ATOM 3731 CG PRO 3150 110.150 14.975 85.356 1.00 51.28 ATOM 3732 C PRO 3150 110.063 16.578 88.182 1.00 49.83 ATOM 3733 O PRO 3150 111.288 16.687 88.089 1.00 49.14 ATOM 3734 N VAL 3151 109.402 16.602 89.338 1.00 48.76 ATOM 3735 CA VAL 3151 110.056 16.731 90.636 1.00 46.73 ATOM 3736 CB VAL 3151 110.317 18.214 90.995 1.00 45.76 ATOM 3737 CG1 VAL 3151 110.372 18.396 92.488 1.00 45.78 ATOM 3738 CG2 VAL 3151 111.642 18.648 90.406 1.00 46.31 ATOM 3739 C VAL 3151 109.196 16.074 91.711 1.00 45.95 ATOM 3740 O VAL 3151 107.983 16.300 91.789 1.00 45.41 ATOM 3741 N ALA 3152 109.834 15.242 92.527 1.00 44.98 ATOM 3742 CA ALA 3152 109.135 14.542 93.594 1.00 43.99 ATOM 3743 CB ALA 3152 109.994 13.404 94.122 1.00 44.25 ATOM 3744 C ALA 3152 108.786 15.504 94.720 1.00 42.90 ATOM 3745 O ALA 3152 109.503 16.471 94.981 1.00 43.11 ATOM 3746 N PRO 3153 107.675 15.245 95.411 1.00 41.61 ATOM 3747 CD PRO 3153 106.876 14.008 95.417 1.00 40.38 ATOM 3748 CA PRO 3153 107.284 16.132 96.504 1.00 40.65 ATOM 3749 CB PRO 3153 106.062 15.433 97.082 1.00 41.36 ATOM 3750 CG PRO 3153 106.355 13.984 96.820 1.00 41.00 ATOM 3751 C PRO 3153 108.407 16.268 97.517 1.00 40.38 ATOM 3752 O PRO 3153 109.068 15.285 97.849 1.00 40.88 ATOM 3753 N TYR 3154 108.633 17.479 98.004 1.00 39.09 ATOM 3754 CA TYR 3154 109.682 17.689 98.991 1.00 37.91 ATOM 3755 CB TYR 3154 110.971 18.119 98.296 1.00 37.75 ATOM 3756 CG TYR 3154 110.841 19.437 97.570 1.00 40.09 ATOM 3757 CD1 TYR 3154 110.157 19.522 96.356 1.00 40.03 ATOM 3758 CE1 TYR 3154 109.999 20.751 95.704 1.00 39.70 ATOM 3759 CD2 TYR 3154 111.368 20.617 98.117 1.00 39.82 ATOM 3760 CE2 TYR 3154 111.214 21.846 97.472 1.00 38.84 ATOM 3761 CZ TYR 3154 110.528 21.905 96.270 1.00 39.55 ATOM 3762 OH TYR 3154 110.356 23.113 95.634 1.00 39.77 ATOM 3763 C TYR 3154 109.274 18.739 100.026 1.00 36.94 ATOM 3764 O TYR 3154 108.474 19.622 99.743 1.00 37.50 ATOM 3765 N TRP 3155 109.822 18.631 101.230 1.00 35.27 ATOM 3766 CA TRP 3155 109.518 19.574 102.299 1.00 33.87 ATOM 3767 CB TRP 3155 110.107 19.093 103.621 1.00 32.01 ATOM 3768 CG TRP 3155 109.573 17.786 104.143 1.00 28.02 ATOM 3769 CD2 TRP 3155 108.220 17.322 104.097 1.00 26.45 ATOM 3770 CE2 TRP 3155 108.185 16.066 104.746 1.00 25.14 ATOM 3771 CE3 TRP 3155 107.035 17.841 103.569 1.00 26.33 ATOM 3772 CD1 TRP 3155 110.281 16.824 104.802 1.00 27.15 ATOM 3773 NE1 TRP 3155 109.455 15.787 105.167 1.00 25.80 ATOM 3774 CZ2 TRP 3155 107.017 15.328 104.885 1.00 24.17 ATOM 3775 CZ3 TRP 3155 105.871 17.101 103.708 1.00 26.53 ATOM 3776 CH2 TRP 3155 105.874 15.856 104.361 1.00 24.65 ATOM 3777 C TRP 3155 110.111 20.938 101.969 1.00 35.28 ATOM 3778 O TRP 3155 111.311 21.051 101.712 1.00 35.18 ATOM 3779 N THR 3156 109.273 21.972 101.983 1.00 36.76 ATOM 3780 CA THR 3156 109.728 23.325 101.678 1.00 37.57 ATOM 3781 CB THR 3156 108.621 24.143 101.025 1.00 35.80 ATOM 3782 OG1 THR 3156 107.605 24.430 101.990 1.00 36.19 ATOM 3783 CG2 THR 3156 108.010 23.373 99.889 1.00 34.67 ATOM 3784 C THR 3156 110.198 24.056 102.929 1.00 39.50 ATOM 3785 O THR 3156 111.095 24.893 102.861 1.00 39.18 ATOM 3786 N SER 3157 109.588 23.737 104.066 1.00 42.72 ATOM 3787 CA SER 3157 109.954 24.356 105.342 1.00 46.50 ATOM 3788 CB SER 3157 108.848 25.302 105.822 1.00 46.20 ATOM 3789 OG SER 3157 108.611 26.330 104.878 1.00 46.67 ATOM 3790 C SER 3157 110.165 23.250 106.368 1.00 48.51 ATOM 3791 O SER 3157 109.391 23.103 107.317 1.00 49.78 ATOM 3792 N PRO 3158 111.232 22.462 106.194 1.00 49.73 ATOM 3793 CD PRO 3158 112.328 22.734 105.255 1.00 50.01 ATOM 3794 CA PRO 3158 111.586 21.347 107.072 1.00 51.06 ATOM 3795 CB PRO 3158 112.908 20.870 106.490 1.00 51.19 ATOM 3796 CG PRO 3158 113.496 22.119 105.971 1.00 50.83 ATOM 3797 C PRO 3158 111.698 21.681 108.549 1.00 51.91 ATOM 3798 O PRO 3158 111.358 20.861 109.402 1.00 51.46 ATOM 3799 N GLU 3159 112.170 22.885 108.847 1.00 52.94 ATOM 3800 CA GLU 3159 112.345 23.302 110.231 1.00 54.81 ATOM 3801 CB GLU 3159 113.107 24.623 110.296 1.00 56.84 ATOM 3802 CG GLU 3159 114.546 24.464 109.871 1.00 59.34 ATOM 3803 CD GLU 3159 115.006 23.015 109.980 1.00 60.57 ATOM 3804 OE1 GLU 3159 114.875 22.424 111.085 1.00 60.07 ATOM 3805 OE2 GLU 3159 115.487 22.476 108.954 1.00 61.42 ATOM 3806 C GLU 3159 111.070 23.415 111.032 1.00 54.75 ATOM 3807 O GLU 3159 111.051 23.108 112.224 1.00 55.32 ATOM 3808 N LYS 3160 110.007 23.861 110.380 1.00 53.40 ATOM 3809 CA LYS 3160 108.726 24.004 111.039 1.00 51.90 ATOM 3810 CB LYS 3160 107.859 24.954 110.216 1.00 52.24 ATOM 3811 CG LYS 3160 108.533 26.301 109.981 1.00 52.84 ATOM 3812 CD LYS 3160 107.643 27.268 109.218 1.00 53.85 ATOM 3813 CE LYS 3160 108.256 28.667 109.190 1.00 55.22 ATOM 3814 NZ LYS 3160 107.372 29.643 108.476 1.00 57.31 ATOM 3815 C LYS 3160 108.054 22.637 111.184 1.00 51.08 ATOM 3816 O LYS 3160 106.834 22.543 111.304 1.00 50.56 ATOM 3817 N MET 3161 108.867 21.583 111.177 1.00 49.65 ATOM 3818 CA MET 3161 108.380 20.211 111.295 1.00 47.64 ATOM 3819 CB MET 3161 108.561 19.473 109.966 1.00 47.44 ATOM 3820 CG MET 3161 107.940 20.187 108.776 1.00 46.79 ATOM 3821 SD MET 3161 107.895 19.168 107.309 1.00 45.53 ATOM 3822 CE MET 3161 106.487 18.124 107.661 1.00 44.33 ATOM 3823 C MET 3161 109.174 19.499 112.376 1.00 47.02 ATOM 3824 O MET 3161 108.979 18.314 112.631 1.00 45.87 ATOM 3825 N GLU 3162 110.072 20.245 113.006 1.00 46.47 ATOM 3826 CA GLU 3162 110.934 19.719 114.059 1.00 45.43 ATOM 3827 CB GLU 3162 111.932 20.793 114.506 1.00 47.92 ATOM 3828 CG GLU 3162 113.089 21.027 113.534 1.00 50.70 ATOM 3829 CD GLU 3162 114.183 19.977 113.665 1.00 52.22 ATOM 3830 OE1 GLU 3162 113.858 18.766 113.670 1.00 51.98 ATOM 3831 OE2 GLU 3162 115.370 20.369 113.763 1.00 54.08 ATOM 3832 C GLU 3162 110.187 19.207 115.274 1.00 43.38 ATOM 3833 O GLU 3162 110.501 18.146 115.793 1.00 42.60 ATOM 3834 N LYS 3163 109.206 19.973 115.724 1.00 41.71 ATOM 3835 CA LYS 3163 108.408 19.637 116.897 1.00 40.08 ATOM 3836 CB LYS 3163 107.611 20.888 117.282 1.00 40.36 ATOM 3837 CG LYS 3163 106.778 20.829 118.542 1.00 38.95 ATOM 3838 CD LYS 3163 106.402 22.238 118.954 1.00 36.52 ATOM 3839 CE LYS 3163 105.293 22.223 119.970 1.00 37.21 ATOM 3840 NZ LYS 3163 104.029 21.737 119.350 1.00 36.99 ATOM 3841 C LYS 3163 107.480 18.461 116.608 1.00 39.82 ATOM 3842 O LYS 3163 106.334 18.656 116.212 1.00 39.27 ATOM 3843 N LYS 3164 107.970 17.243 116.819 1.00 39.56 ATOM 3844 CA LYS 3164 107.175 16.054 116.535 1.00 39.20 ATOM 3845 CB LYS 3164 108.094 14.855 116.266 1.00 39.52 ATOM 3846 CG LYS 3164 109.030 15.028 115.064 1.00 40.34 ATOM 3847 CD LYS 3164 109.768 13.723 114.719 1.00 42.08 ATOM 3848 CE LYS 3164 110.723 13.882 113.519 1.00 44.01 ATOM 3849 NZ LYS 3164 111.437 12.625 113.081 1.00 42.94 ATOM 3850 C LYS 3164 106.162 15.699 117.617 1.00 38.41 ATOM 3851 O LYS 3164 105.194 14.986 117.349 1.00 39.65 ATOM 3852 N LEU 3165 106.374 16.187 118.833 1.00 35.73 ATOM 3853 CA LEU 3165 105.442 15.901 119.913 1.00 33.17 ATOM 3854 CB LEU 3165 106.164 15.301 121.110 1.00 30.21 ATOM 3855 CG LEU 3165 105.251 15.064 122.311 1.00 26.93 ATOM 3856 CD1 LEU 3165 104.238 13.986 121.980 1.00 26.38 ATOM 3857 CD2 LEU 3165 106.081 14.681 123.506 1.00 24.15 ATOM 3858 C LEU 3165 104.716 17.162 120.357 1.00 33.21 ATOM 3859 O LEU 3165 105.333 18.125 120.798 1.00 31.84 ATOM 3860 N HIS 3166 103.395 17.143 120.242 1.00 33.42 ATOM 3861 CA HIS 3166 102.572 18.279 120.635 1.00 33.38 ATOM 3862 CB HIS 3166 101.581 18.665 119.528 1.00 34.28 ATOM 3863 CG HIS 3166 102.181 19.418 118.383 1.00 35.41 ATOM 3864 CD2 HIS 3166 101.790 20.562 117.774 1.00 36.20 ATOM 3865 ND1 HIS 3166 103.268 18.959 117.672 1.00 37.05 ATOM 3866 CE1 HIS 3166 103.518 19.785 116.671 1.00 36.57 ATOM 3867 NE2 HIS 3166 102.634 20.766 116.710 1.00 36.72 ATOM 3868 C HIS 3166 101.745 17.918 121.855 1.00 32.56 ATOM 3869 O HIS 3166 100.723 17.237 121.727 1.00 33.30 ATOM 3870 N ALA 3167 102.172 18.372 123.027 1.00 30.59 ATOM 3871 CA ALA 3167 101.430 18.112 124.253 1.00 29.28 ATOM 3872 CB ALA 3167 102.377 17.761 125.374 1.00 29.41 ATOM 3873 C ALA 3167 100.688 19.397 124.576 1.00 28.81 ATOM 3874 O ALA 3167 101.289 20.473 124.624 1.00 28.26 ATOM 3875 N VAL 3168 99.381 19.290 124.778 1.00 27.99 ATOM 3876 CA VAL 3168 98.572 20.465 125.084 1.00 26.35 ATOM 3877 CB VAL 3168 97.977 21.081 123.792 1.00 25.05 ATOM 3878 CG1 VAL 3168 99.034 21.179 122.739 1.00 24.87 ATOM 3879 CG2 VAL 3168 96.831 20.241 123.286 1.00 25.52 ATOM 3880 C VAL 3168 97.420 20.113 126.023 1.00 25.97 ATOM 3881 O VAL 3168 97.073 18.939 126.177 1.00 25.00 ATOM 3882 N PRO 3169 96.637 21.125 126.693 1.00 25.48 ATOM 3883 CD PRO 3169 97.374 22.466 126.974 1.00 24.61 ATOM 3884 CA PRO 3169 95.720 20.819 127.594 1.00 24.17 ATOM 3885 CB PRO 3169 95.670 22.028 128.532 1.00 24.08 ATOM 3886 CG PRO 3169 97.053 22.605 128.449 1.00 24.31 ATOM 3887 C PRO 3169 94.506 20.736 126.687 1.00 23.77 ATOM 3888 O PRO 3169 94.515 21.295 125.584 1.00 23.57 ATOM 3889 N ALA 3170 93.466 20.050 127.135 1.00 24.25 ATOM 3890 CA ALA 3170 92.279 19.888 126.308 1.00 24.77 ATOM 3891 CS ALA 3170 91.234 19.093 127.059 1.00 22.87 ATOM 3892 C ALA 3170 91.687 21.206 125.817 1.00 25.55 ATOM 3893 O ALA 3170 91.932 22.274 126.378 1.00 25.43 ATOM 3894 N ALA 3171 90.915 21.110 124.743 1.00 27.40 ATOM 3895 CA ALA 3171 90.244 22.256 124.153 1.00 29.23 ATOM 3896 CB ALA 3171 89.640 23.129 125.239 1.00 28.46 ATOM 3897 C ALA 3171 91.158 23.090 123.283 1.00 30.83 ATOM 3898 O ALA 3171 90.697 23.708 122.313 1.00 33.12 ATOM 3899 N LYS 3172 92.446 23.125 123.618 1.00 30.69 ATOM 3900 CA LYS 3172 93.372 23.919 122.821 1.00 30.07 ATOM 3901 CB LYS 3172 94.804 23.723 123.305 1.00 30.73 ATOM 3902 CG LYS 3172 95.795 24.767 122.777 1.00 33.07 ATOM 3903 CD LYS 3172 96.484 24.317 121.491 1.00 35.20 ATOM 3904 CE LYS 3172 97.620 25.260 121.058 1.00 36.63 ATOM 3905 NZ LYS 3172 97.159 26.611 120.587 1.00 38.22 ATOM 3906 C LYS 3172 93.247 23.485 121.371 1.00 29.82 ATOM 3907 O LYS 3172 93.014 22.311 121.090 1.00 30.27 ATOM 3908 N THR 3173 93.363 24.432 120.450 1.00 28.89 ATOM 3909 CA THR 3173 93.275 24.093 119.042 1.00 28.50 ATOM 3910 CB THR 3173 92.761 25.281 118.242 1.00 29.15 ATOM 3911 OG1 THR 3173 91.377 25.480 118.570 1.00 30.98 ATOM 3912 CG2 THR 3173 92.929 25.047 116.744 1.00 26.93 ATOM 3913 C THR 3173 94.645 23.650 118.559 1.00 27.27 ATOM 3914 O THR 3173 95.664 24.264 118.877 1.00 27.15 ATOM 3915 N VAL 3174 94.679 22.556 117.815 1.00 25.48 ATOM 3916 CA VAL 3174 95.951 22.068 117.340 1.00 25.53 ATOM 3917 CB VAL 3174 96.244 20.665 117.882 1.00 23.48 ATOM 3918 CG1 VAL 3174 97.396 20.050 117.136 1.00 23.44 ATOM 3919 CG2 VAL 3174 96.586 20.752 119.343 1.00 21.93 ATOM 3920 C VAL 3174 95.999 22.069 115.835 1.00 27.17 ATOM 3921 O VAL 3174 95.004 21.782 115.176 1.00 28.23 ATOM 3922 N LYS 3175 97.162 22.423 115.229 1.00 28.65 ATOM 3923 CA LYS 3175 97.365 22.466 113.865 1.00 30.59 ATOM 3924 CB LYS 3175 97.332 23.917 113.365 1.00 32.06 ATOM 3925 CG LYS 3175 97.451 24.062 111.838 1.00 33.55 ATOM 3926 CD LYS 3175 97.142 25.485 111.358 1.00 33.90 ATOM 3927 CE LYS 3175 98.385 26.315 111.081 1.00 35.82 ATOM 3928 NZ LYS 3175 99.220 26.546 112.288 1.00 38.45 ATOM 3929 C LYS 3175 98.697 21.825 113.505 1.00 31.31 ATOM 3930 O LYS 3175 99.745 22.214 114.029 1.00 31.44 ATOM 3931 N PHE 3176 98.647 20.826 112.626 1.00 32.28 ATOM 3932 CA PHE 3176 99.858 20.140 112.152 1.00 33.01 ATOM 3933 CB PHE 3176 99.736 18.613 112.242 1.00 30.80 ATOM 3934 CG PHE 3176 99.591 18.092 113.637 1.00 30.50 ATOM 3935 CD1 PHE 3176 100.476 18.480 114.638 1.00 30.97 ATOM 3936 CD2 PHE 3176 98.565 17.211 113.958 1.00 30.24 ATOM 3937 CE1 PHE 3176 100.337 18.001 115.944 1.00 29.88 ATOM 3938 CE2 PHE 3176 98.423 16.728 115.260 1.00 30.76 ATOM 3939 CZ PHE 3176 99.312 17.127 116.254 1.00 29.37 ATOM 3940 C PHE 3176 100.043 20.515 110.692 1.00 33.92 ATOM 3941 O PHE 3176 99.088 20.452 109.911 1.00 33.90 ATOM 3942 N LYS 3177 101.261 20.912 110.323 1.00 35.49 ATOM 3943 CA LYS 3177 101.538 21.292 108.935 1.00 36.35 ATOM 3944 CB LYS 3177 101.779 22.802 108.824 1.00 38.05 ATOM 3945 CG LYS 3177 102.870 23.348 109.711 1.00 42.43 ATOM 3946 CD LYS 3177 102.944 24.865 109.583 1.00 46.97 ATOM 3947 CE LYS 3177 103.939 25.463 110.586 1.00 50.46 ATOM 3948 NZ LYS 3177 104.026 26.962 110.524 1.00 52.89 ATOM 3949 C LYS 3177 102.695 20.536 108.293 1.00 35.62 ATOM 3950 O LYS 3177 103.642 20.119 108.961 1.00 35.64 ATOM 3951 N CYS 3178 102.596 20.357 106.982 1.00 34.67 ATOM 3952 CA CYS 3178 103.612 19.659 106.222 1.00 34.74 ATOM 3953 C CYS 3178 103.955 20.424 104.958 1.00 35.58 ATOM 3954 O CYS 3178 103.741 19.937 103.853 1.00 35.54 ATOM 3955 CB CYS 3178 103.117 18.261 105.884 1.00 33.60 ATOM 3956 SG CYS 3178 103.038 17.226 107.372 1.00 35.88 ATOM 3957 N PRO 3179 104.498 21.644 105.109 1.00 36.84 ATOM 3958 CD PRO 3179 104.979 22.257 106.356 1.00 38.05 ATOM 3959 CA PRO 3179 104.871 22.475 103.970 1.00 37.36 ATOM 3960 CB PRO 3179 105.558 23.672 104.625 1.00 37.13 ATOM 3961 CG PRO 3179 106.122 23.106 105.856 1.00 37.15 ATOM 3962 C PRO 3179 105.779 21.711 103.033 1.00 38.78 ATOM 3963 O PRO 3179 106.888 21.316 103.404 1.00 39.64 ATOM 3964 N SER 3180 105.283 21.504 101.818 1.00 39.40 ATOM 3965 CA SER 3180 106.013 20.772 100.795 1.00 40.28 ATOM 3966 CB SER 3180 105.687 19.287 100.892 1.00 40.13 ATOM 3967 OG SER 3180 104.294 19.079 100.743 1.00 41.29 ATOM 3968 C SER 3180 105.653 21.265 99.402 1.00 40.83 ATOM 3969 O SER 3180 104.695 22.014 99.224 1.00 41.33 ATOM 3970 N SER 3181 106.432 20.838 98.415 1.00 41.29 ATOM 3971 CA SER 3181 106.196 21.216 97.032 1.00 41.67 ATOM 3972 CB SER 3181 106.933 22.501 96.684 1.00 41.34 ATOM 3973 OG SER 3181 106.679 22.841 95.336 1.00 42.45 ATOM 3974 C SER 3181 106.667 20.114 96.108 1.00 42.58 ATOM 3975 O SER 3181 107.169 19.078 96.557 1.00 42.52 ATOM 3976 N GLY 3182 106.515 20.347 94.809 1.00 43.39 ATOM 3977 CA GLY 3182 106.926 19.358 93.832 1.00 44.36 ATOM 3978 C GLY 3182 106.023 19.414 92.624 1.00 44.64 ATOM 3979 O GLY 3182 104.828 19.686 92.744 1.00 45.60 ATOM 3980 N THR 3183 106.584 19.145 91.455 1.00 44.26 ATOM 3981 CA THR 3183 105.809 19.199 90.226 1.00 43.39 ATOM 3982 CB THR 3183 106.416 20.225 89.257 1.00 44.07 ATOM 3983 OG1 THR 3183 107.601 19.679 88.664 1.00 43.89 ATOM 3984 CG2 THR 3183 106.784 21.510 90.009 1.00 44.02 ATOM 3985 C THR 3183 105.739 17.848 89.528 1.00 41.94 ATOM 3986 O THR 3183 106.749 17.182 89.337 1.00 41.73 ATOM 3987 N PRO 3184 104.533 17.419 89.154 1.00 40.89 ATOM 3988 CD PRO 3184 104.324 16.173 88.403 1.00 40.85 ATOM 3989 CA PRO 3184 103.263 18.126 89.357 1.00 41.35 ATOM 3990 CB PRO 3184 102.264 17.255 88.596 1.00 41.51 ATOM 3991 CG PRO 3184 102.877 15.878 88.685 1.00 41.48 ATOM 3992 C PRO 3184 102.899 18.273 90.842 1.00 41.37 ATOM 3993 O PRO 3184 103.304 17.443 91.662 1.00 41.55 ATOM 3994 N GLN 3185 102.136 19.317 91.178 1.00 40.22 ATOM 3995 CA GLN 3185 101.741 19.555 92.565 1.00 38.60 ATOM 3996 CB GLN 3185 100.632 20.603 92.686 1.00 38.52 ATOM 3997 CG GLN 3185 101.130 22.019 92.551 1.00 38.62 ATOM 3998 CD GLN 3185 102.396 22.266 93.350 1.00 39.26 ATOM 3999 OE1 GLN 3185 102.349 22.553 94.555 1.00 38.93 ATOM 4000 NE2 GLN 3185 103.544 22.143 92.682 1.00 37.47 ATOM 4001 C GLN 3185 101.286 18.292 93.255 1.00 38.04 ATOM 4002 O GLN 3185 100.398 17.582 92.773 1.00 38.76 ATOM 4003 N PRO 3186 101.891 17.996 94.411 1.00 36.43 ATOM 4004 CD PRO 3186 103.019 18.718 95.029 1.00 34.31 ATOM 4005 CA PRO 3186 101.549 16.803 95.180 1.00 35.01 ATOM 4006 CB PRO 3186 102.727 16.680 96.129 1.00 34.21 ATOM 4007 CG PRO 3186 103.077 18.112 96.384 1.00 33.80 ATOM 4008 C PRO 3186 100.225 16.928 95.914 1.00 34.50 ATOM 4009 O PRO 3186 99.776 18.023 96.214 1.00 34.54 ATOM 4010 N THR 3187 99.602 15.797 96.198 1.00 34.48 ATOM 4011 CA THR 3187 98.344 15.791 96.914 1.00 33.96 ATOM 4012 CB THR 3187 97.476 14.650 96.460 1.00 34.40 ATOM 4013 OG1 THR 3187 98.076 13.415 96.867 1.00 37.04 ATOM 4014 CG2 THR 3187 97.355 14.661 94.958 1.00 32.72 ATOM 4015 C THR 3187 98.669 15.609 98.386 1.00 34.06 ATOM 4016 O THR 3187 99.694 15.025 98.733 1.00 34.86 ATOM 4017 N LEU 3188 97.784 16.094 99.247 1.00 33.45 ATOM 4018 CA LEU 3188 97.989 16.025 100.689 1.00 32.42 ATOM 4019 CB LEU 3188 98.058 17.459 101.222 1.00 32.45 ATOM 4020 CG LEU 3188 98.424 17.833 102.657 1.00 32.62 ATOM 4021 CD1 LEU 3188 97.176 17.927 103.496 1.00 33.45 ATOM 4022 CD2 LEU 3188 99.412 16.837 103.214 1.00 32.98 ATOM 4023 C LEU 3188 96.888 15.241 101.394 1.00 32.45 ATOM 4024 O LEU 3188 95.703 15.500 101.184 1.00 33.51 ATOM 4025 N ARG 3189 97.273 14.276 102.222 1.00 31.58 ATOM 4026 CA ARG 3189 96.292 13.482 102.960 1.00 31.46 ATOM 4027 CB ARG 3189 96.034 12.171 102.244 1.00 32.71 ATOM 4028 CG ARG 3189 97.254 11.655 101.536 1.00 35.33 ATOM 4029 CD ARG 3189 96.964 10.360 100.823 1.00 36.64 ATOM 4030 NE ARG 3189 97.343 9.221 101.640 1.00 39.14 ATOM 4031 CZ ARG 3189 97.196 7.967 101.251 1.00 40.05 ATOM 4032 NH1 ARG 3189 96.667 7.724 100.062 1.00 41.48 ATOM 4033 NH2 ARG 3189 97.598 6.968 102.029 1.00 40.09 ATOM 4034 C ARG 3189 96.806 13.215 104.357 1.00 30.48 ATOM 4035 O ARG 3189 98.015 13.216 104.570 1.00 31.15 ATOM 4036 N TRP 3190 95.900 12.993 105.309 1.00 28.92 ATOM 4037 CA TRP 3190 96.312 12.744 106.689 1.00 27.43 ATOM 4038 CB TRP 3190 95.807 13.861 107.601 1.00 25.06 ATOM 4039 CG TRP 3190 96.413 15.186 107.297 1.00 24.52 ATOM 4040 CD2 TRP 3190 97.573 15.751 107.913 1.00 23.12 ATOM 4041 CE2 TRP 3190 97.811 17.001 107.290 1.00 22.92 ATOM 4042 CE3 TRP 3190 98.439 15.323 108.926 1.00 21.94 ATOM 4043 CD1 TRP 3190 96.000 16.091 106.349 1.00 25.01 ATOM 4044 NE1 TRP 3190 96.838 17.185 106.343 1.00 23.24 ATOM 4045 CZ2 TRP 3190 98.876 17.823 107.650 1.00 22.66 ATOM 4046 CZ3 TRP 3190 99.498 16.142 109.287 1.00 21.32 ATOM 4047 CH2 TRP 3190 99.708 17.379 108.650 1.00 22.50 ATOM 4048 C TRP 3190 95.872 11.405 107.253 1.00 27.66 ATOM 4049 O TRP 3190 94.887 10.824 106.810 1.00 27.65 ATOM 4050 N LEU 3191 96.610 10.926 108.249 1.00 28.41 ATOM 4051 CA LEU 3191 96.307 9.650 108.888 1.00 28.83 ATOM 4052 CB LEU 3191 97.260 8.566 108.390 1.00 27.63 ATOM 4053 CG LEU 3191 97.094 8.114 106.946 1.00 26.93 ATOM 4054 CD1 LEU 3191 98.157 7.108 106.615 1.00 24.92 ATOM 4055 CD2 LEU 3191 95.720 7.514 106.758 1.00 28.55 ATOM 4056 C LEU 3191 96.399 9.696 110.400 1.00 30.38 ATOM 4057 O LEU 3191 97.392 10.169 110.964 1.00 31.46 ATOM 4058 N LYS 3192 95.366 9.191 111.059 1.00 30.65 ATOM 4059 CA LYS 3192 95.365 9.153 112.511 1.00 31.26 ATOM 4060 CB LYS 3192 93.968 9.452 113.048 1.00 30.21 ATOM 4061 CG LYS 3192 93.849 9.483 114.559 1.00 28.59 ATOM 4062 CD LYS 3192 92.490 10.045 114.934 1.00 28.49 ATOM 4063 CE LYS 3192 92.225 10.011 116.429 1.00 27.72 ATOM 4064 NZ LYS 3192 91.766 8.673 116.913 1.00 27.67 ATOM 4065 C LYS 3192 95.770 7.738 112.841 1.00 32.77 ATOM 4066 O LYS 3192 95.060 6.803 112.493 1.00 32.79 ATOM 4067 N ASN 3193 96.922 7.586 113.489 1.00 34.65 ATOM 4068 CA ASN 3193 97.442 6.271 113.865 1.00 35.77 ATOM 4069 CB ASN 3193 96.586 5.615 114.951 1.00 34.84 ATOM 4070 CG ASN 3193 96.362 6.510 116.142 1.00 36.02 ATOM 4071 OD1 ASN 3193 97.310 7.003 116.754 1.00 37.08 ATOM 4072 ND2 ASN 3193 95.097 6.726 116.485 1.00 35.16 ATOM 4073 C ASN 3193 97.470 5.338 112.672 1.00 36.81 ATOM 4074 O ASN 3193 97.022 4.201 112.770 1.00 37.65 ATOM 4075 N GLY 3194 97.976 5.818 111.543 1.00 37.81 ATOM 4076 CA GLY 3194 98.052 4.980 110.358 1.00 39.40 ATOM 4077 C GLY 3194 96.770 4.835 109.562 1.00 39.98 ATOM 4078 O GLY 3194 96.783 4.871 108.339 1.00 39.69 ATOM 4079 N LYS 3195 95.653 4.667 110.251 1.00 42.10 ATOM 4080 CA LYS 3195 94.371 4.514 109.575 1.00 43.61 ATOM 4081 CS LYS 3195 93.322 4.012 110.576 1.00 45.37 ATOM 4082 CG LYS 3195 93.783 2.809 111.409 1.00 47.51 ATOM 4083 CD LYS 3195 94.260 1.672 110.507 1.00 50.03 ATOM 4084 CE LYS 3195 94.801 0.473 111.294 1.00 51.90 ATOM 4085 NZ LYS 3195 93.749 −0.297 112.031 1.00 52.89 ATOM 4086 C LYS 3195 93.912 5.826 108.925 1.00 43.68 ATOM 4087 O LYS 3195 94.371 6.912 109.291 1.00 44.03 ATOM 4088 N GLU 3196 93.005 5.718 107.961 1.00 43.97 ATOM 4089 CA GLU 3196 92.503 6.891 107.265 1.00 45.11 ATOM 4090 CB GLU 3196 91.764 6.472 106.001 1.00 47.79 ATOM 4091 CG GLU 3196 92.191 7.266 104.776 1.00 51.56 ATOM 4092 CD GLU 3196 91.085 7.376 103.743 1.00 54.33 ATOM 4093 OE1 GLU 3196 91.305 8.031 102.701 1.00 55.06 ATOM 4094 OE2 GLU 3196 89.993 6.811 103.984 1.00 54.21 ATOM 4095 C GLU 3196 91.586 7.743 108.132 1.00 44.77 ATOM 4096 O GLU 3196 90.632 7.246 108.718 1.00 43.69 ATOM 4097 N PHE 3197 91.883 9.036 108.207 1.00 46.09 ATOM 4098 CA PHE 3197 91.087 9.969 109.007 1.00 46.85 ATOM 4099 CB PHE 3197 91.911 11.198 109.409 1.00 49.07 ATOM 4100 CG PHE 3197 91.574 12.424 108.602 1.00 54.99 ATOM 4101 CD1 PHE 3197 90.857 13.473 109.171 1.00 57.46 ATOM 4102 CD2 PHE 3197 91.855 12.473 107.226 1.00 56.59 ATOM 4103 CE1 PHE 3197 90.414 14.557 108.386 1.00 59.23 ATOM 4104 CE2 PHE 3197 91.416 13.549 106.427 1.00 57.43 ATOM 4105 CZ PHE 3197 90.692 14.590 107.009 1.00 58.59 ATOM 4106 C PHE 3197 89.920 10.447 108.148 1.00 46.85 ATOM 4107 O PHE 3197 89.960 10.359 106.923 1.00 47.12 ATOM 4108 N LYS 3198 88.889 10.973 108.793 1.00 46.00 ATOM 4109 CA LYS 3198 87.732 11.508 108.080 1.00 45.84 ATOM 4110 CB LYS 3198 86.786 10.374 107.661 1.00 44.01 ATOM 4111 C LYS 3198 87.025 12.527 108.993 1.00 45.86 ATOM 4112 O LYS 3198 86.769 12.252 110.164 1.00 46.51 ATOM 4113 N PRO 3199 86.697 13.716 108.461 1.00 45.11 ATOM 4114 CD PRO 3199 86.516 13.932 107.014 1.00 44.01 ATOM 4115 CA PRO 3199 86.026 14.783 109.214 1.00 44.59 ATOM 4116 CB PRO 3199 85.430 15.657 108.110 1.00 43.96 ATOM 4117 CG PRO 3199 85.235 14.702 106.979 1.00 42.96 ATOM 4118 C PRO 3199 84.980 14.341 110.237 1.00 44.16 ATOM 4119 O PRO 3199 84.950 14.847 111.347 1.00 44.80 ATOM 4120 N ASP 3200 84.116 13.404 109.870 1.00 43.90 ATOM 4121 CA ASP 3200 83.100 12.933 110.805 1.00 44.02 ATOM 4122 CB ASP 3200 82.073 12.043 110.097 1.00 45.82 ATOM 4123 CG ASP 3200 81.157 12.813 109.189 1.00 47.10 ATOM 4124 OD1 ASP 3200 81.586 13.149 108.064 1.00 48.67 ATOM 4125 OD2 ASP 3200 80.010 13.084 109.606 1.00 46.58 ATOM 4126 C ASP 3200 83.685 12.109 111.950 1.00 43.57 ATOM 4127 O ASP 3200 82.956 11.695 112.848 1.00 43.75 ATOM 4128 N HIS 3201 84.988 11.856 111.928 1.00 42.90 ATOM 4129 CA HIS 3201 85.577 11.024 112.966 1.00 42.12 ATOM 4130 CB HIS 3201 86.819 10.322 112.412 1.00 45.05 ATOM 4131 CG HIS 3201 86.513 9.409 111.258 1.00 48.69 ATOM 4132 CD2 HIS 3201 87.276 8.503 110.601 1.00 49.14 ATOM 4133 ND1 HIS 3201 85.280 9.393 110.633 1.00 49.54 ATOM 4134 CE1 HIS 3201 85.298 8.519 109.643 1.00 49.00 ATOM 4135 NE2 HIS 3201 86.497 7.966 109.600 1.00 49.34 ATOM 4136 C HIS 3201 85.839 11.693 114.306 1.00 40.12 ATOM 4137 O HIS 3201 86.315 11.051 115.234 1.00 39.87 ATOM 4138 N ARG 3202 85.511 12.975 114.419 1.00 38.19 ATOM 4139 CA ARG 3202 85.666 13.680 115.690 1.00 37.19 ATOM 4140 CB ARG 3202 87.094 14.212 115.858 1.00 33.66 ATOM 4141 CG ARG 3202 87.423 15.447 115.033 1.00 30.85 ATOM 4142 CD ARG 3202 88.874 15.897 115.215 1.00 28.38 ATOM 4143 NE ARG 3202 89.213 16.267 116.595 1.00 26.89 ATOM 4144 CZ ARG 3202 89.081 17.486 117.116 1.00 24.63 ATOM 4145 NH1 ARG 3202 88.614 18.490 116.378 1.00 22.77 ATOM 4146 NH2 ARG 3202 89.426 17.701 118.379 1.00 22.19 ATOM 4147 C ARG 3202 84.665 14.826 115.713 1.00 38.70 ATOM 4148 O ARG 3202 84.313 15.352 114.656 1.00 39.97 ATOM 4149 N ILE 3203 84.187 15.197 116.899 1.00 38.96 ATOM 4150 CA ILE 3203 83.228 16.302 117.020 1.00 40.54 ATOM 4151 CB ILE 3203 82.888 16.619 118.497 1.00 40.79 ATOM 4152 CG2 ILE 3203 81.583 15.975 118.896 1.00 41.16 ATOM 4153 CG1 ILE 3203 84.046 16.187 119.394 1.00 41.69 ATOM 4154 CD1 ILE 3203 83.854 16.577 120.829 1.00 42.35 ATOM 4155 C ILE 3203 83.850 17.560 116.437 1.00 41.00 ATOM 4156 O ILE 3203 84.987 17.889 116.769 1.00 40.32 ATOM 4157 N GLY 3204 83.106 18.265 115.588 1.00 42.04 ATOM 4158 CA GLY 3204 83.633 19.475 114.983 1.00 42.18 ATOM 4159 C GLY 3204 84.576 19.121 113.856 1.00 42.43 ATOM 4160 O GLY 3204 85.010 19.989 113.098 1.00 43.78 ATOM 4161 N GLY 3205 84.899 17.837 113.759 1.00 41.56 ATOM 4162 CA GLY 3205 85.784 17.365 112.714 1.00 42.05 ATOM 4163 C GLY 3205 87.106 18.088 112.573 1.00 41.88 ATOM 4164 O GLY 3205 87.525 18.832 113.458 1.00 41.59 ATOM 4165 N TYR 3206 87.752 17.852 111.436 1.00 41.98 ATOM 4166 CA TYR 3206 89.041 18.435 111.113 1.00 43.16 ATOM 4167 CB TYR 3206 90.030 17.357 110.639 1.00 45.88 ATOM 4168 CG TYR 3206 90.059 16.016 111.348 1.00 49.67 ATOM 4169 CD1 TYR 3206 88.973 15.145 111.312 1.00 50.70 ATOM 4170 CE1 TYR 3206 89.054 13.868 111.912 1.00 52.54 ATOM 4171 CD2 TYR 3206 91.222 15.586 111.998 1.00 52.55 ATOM 4172 CE2 TYR 3206 91.313 14.326 112.593 1.00 52.68 ATOM 4173 CZ TYR 3206 90.233 13.473 112.549 1.00 52.36 ATOM 4174 OH TYR 3206 90.349 12.237 113.142 1.00 51.75 ATOM 4175 C TYR 3206 88.875 19.378 109.924 1.00 43.10 ATOM 4176 O TYR 3206 87.904 19.281 109.176 1.00 42.27 ATOM 4177 N LYS 3207 89.863 20.247 109.726 1.00 42.87 ATOM 4178 CA LYS 3207 89.871 21.175 108.608 1.00 43.44 ATOM 4179 CB LYS 3207 89.669 22.612 109.091 1.00 44.45 ATOM 4180 CG LYS 3207 88.451 22.815 109.968 1.00 46.86 ATOM 4181 CD LYS 3207 87.585 23.959 109.464 1.00 48.99 ATOM 4182 CE LYS 3207 88.323 25.281 109.476 1.00 50.26 ATOM 4183 NZ LYS 3207 87.603 26.258 108.623 1.00 53.62 ATOM 4184 C LYS 3207 91.241 21.062 107.956 1.00 43.63 ATOM 4185 O LYS 3207 92.262 21.210 108.637 1.00 43.12 ATOM 4186 N VAL 3208 91.274 20.800 106.651 1.00 43.43 ATOM 4187 CA VAL 3208 92.550 20.696 105.959 1.00 43.96 ATOM 4188 CB VAL 3208 92.649 19.384 105.160 1.00 44.46 ATOM 4189 CG1 VAL 3208 94.059 19.208 104.641 1.00 44.59 ATOM 4190 CG2 VAL 3208 92.273 18.204 106.038 1.00 44.71 ATOM 4191 C VAL 3208 92.764 21.880 105.021 1.00 43.87 ATOM 4192 O VAL 3208 91.978 22.107 104.108 1.00 43.48 ATOM 4193 N ARG 3209 93.832 22.632 105.269 1.00 43.97 ATOM 4194 CA ARG 3209 94.175 23.800 104.471 1.00 44.14 ATOM 4195 CB ARG 3209 94.563 24.969 105.385 1.00 43.74 ATOM 4196 C ARG 3209 95.335 23.471 103.542 1.00 44.62 ATOM 4197 O ARG 3209 96.492 23.792 103.841 1.00 45.16 ATOM 4198 N TYR 3210 95.018 22.823 102.422 1.00 42.65 ATOM 4199 CA TYR 3210 96.024 22.457 101.445 1.00 40.69 ATOM 4200 CB TYR 3210 95.337 21.964 100.180 1.00 39.58 ATOM 4201 CG TYR 3210 94.363 20.838 100.449 1.00 39.88 ATOM 4202 CD1 TYR 3210 93.015 21.095 100.655 1.00 39.52 ATOM 4203 CE1 TYR 3210 92.121 20.067 100.947 1.00 39.34 ATOM 4204 CD2 TYR 3210 94.801 19.511 100.541 1.00 39.83 ATOM 4205 CE2 TYR 3210 93.914 18.475 100.837 1.00 40.07 ATOM 4206 CZ TYR 3210 92.571 18.761 101.041 1.00 39.67 ATOM 4207 OH TYR 3210 91.681 17.750 101.361 1.00 38.31 ATOM 4208 C TYR 3210 96.868 23.679 101.154 1.00 39.91 ATOM 4209 O TYR 3210 98.069 23.585 100.928 1.00 40.83 ATOM 4210 N ALA 3211 96.225 24.835 101.184 1.00 38.73 ATOM 4211 CA ALA 3211 96.901 26.092 100.926 1.00 38.16 ATOM 4212 CB ALA 3211 95.958 27.240 101.235 1.00 38.71 ATOM 4213 C ALA 3211 98.174 26.220 101.762 1.00 37.62 ATOM 4214 O ALA 3211 99.137 26.870 101.363 1.00 37.03 ATOM 4215 N THR 3212 98.172 25.580 102.921 1.00 36.93 ATOM 4216 CA THR 3212 99.300 25.634 103.836 1.00 36.17 ATOM 4217 CB THR 3212 98.900 26.426 105.078 1.00 35.91 ATOM 4218 OG1 THR 3212 97.654 25.919 105.570 1.00 36.61 ATOM 4219 CG2 THR 3212 98.711 27.889 104.734 1.00 35.63 ATOM 4220 C THR 3212 99.749 24.238 104.260 1.00 35.52 ATOM 4221 O THR 3212 100.523 24.085 105.211 1.00 33.54 ATOM 4222 N TRP 3213 99.242 23.231 103.549 1.00 34.65 ATOM 4223 CA TRP 3213 99.565 21.837 103.819 1.00 34.22 ATOM 4224 CB TRP 3213 101.012 21.547 103.413 1.00 34.03 ATOM 4225 CG TRP 3213 101.313 21.954 101.999 1.00 33.35 ATOM 4226 CD2 TRP 3213 101.134 21.155 100.824 1.00 33.01 ATOM 4227 CE2 TRP 3213 101.442 21.969 99.716 1.00 32.31 ATOM 4228 CE3 TRP 3213 100.740 19.830 100.601 1.00 33.41 ATOM 4229 CD1 TRP 3213 101.719 23.185 101.564 1.00 31.79 ATOM 4230 NE1 TRP 3213 101.795 23.203 100.196 1.00 31.39 ATOM 4231 CZ2 TRP 3213 101.365 21.500 98.401 1.00 32.41 ATOM 4232 CZ3 TRP 3213 100.664 19.366 99.298 1.00 32.89 ATOM 4233 CH2 TRP 3213 100.976 20.199 98.214 1.00 32.99 ATOM 4234 C TRP 3213 99.371 21.523 105.287 1.00 33.48 ATOM 4235 O TRP 3213 100.189 20.846 105.896 1.00 33.88 ATOM 4236 N SER 3214 98.284 22.016 105.860 1.00 32.56 ATOM 4237 CA SER 3214 98.038 21.768 107.265 1.00 30.87 ATOM 4238 CB SER 3214 98.190 23.064 108.065 1.00 30.97 ATOM 4239 OG SER 3214 97.317 24.070 107.580 1.00 32.89 ATOM 4240 C SER 3214 96.687 21.137 107.550 1.00 29.28 ATOM 4241 O SER 3214 95.795 21.093 106.694 1.00 28.57 ATOM 4242 N ILE 3215 96.569 20.616 108.763 1.00 26.55 ATOM 4243 CA ILE 3215 95.341 20.007 109.216 1.00 24.71 ATOM 4244 CB ILE 3215 95.506 18.501 109.433 1.00 22.40 ATOM 4245 CG2 ILE 3215 96.431 18.229 110.581 1.00 22.23 ATOM 4246 CG1 ILE 3215 94.152 17.890 109.736 1.00 22.18 ATOM 4247 CD1 ILE 3215 94.208 16.425 109.972 1.00 23.12 ATOM 4248 C ILE 3215 95.044 20.712 110.532 1.00 24.92 ATOM 4249 O ILE 3215 95.966 21.045 111.288 1.00 25.19 ATOM 4250 N ILE 3216 93.773 20.974 110.810 1.00 24.01 ATOM 4251 CA ILE 3216 93.463 21.666 112.048 1.00 22.52 ATOM 4252 CB ILE 3216 93.060 23.111 111.775 1.00 20.84 ATOM 4253 CG2 ILE 3216 92.815 23.824 113.079 1.00 19.15 ATOM 4254 CG1 ILE 3216 94.178 23.797 110.988 1.00 19.92 ATOM 4255 CD1 ILE 3216 93.906 25.215 110.623 1.00 19.51 ATOM 4256 C ILE 3216 92.399 20.999 112.897 1.00 22.87 ATOM 4257 O ILE 3216 91.357 20.555 112.401 1.00 22.78 ATOM 4258 N MET 3217 92.690 20.914 114.189 1.00 22.18 ATOM 4259 CA MET 3217 91.779 20.321 115.139 1.00 21.68 ATOM 4260 CB MET 3217 92.347 19.053 115.763 1.00 19.39 ATOM 4261 CG MET 3217 92.456 17.917 114.775 1.00 18.56 ATOM 4262 SD MET 3217 92.952 16.333 115.467 1.00 17.16 ATOM 4263 CE MET 3217 94.691 16.580 115.746 1.00 16.06 ATOM 4264 C MET 3217 91.493 21.327 116.216 1.00 23.31 ATOM 4265 O MET 3217 92.362 21.729 116.995 1.00 22.47 ATOM 4266 N ASP 3218 90.230 21.714 116.217 1.00 24.72 ATOM 4267 CA ASP 3218 89.633 22.670 117.114 1.00 25.55 ATOM 4268 CB ASP 3218 88.403 23.180 116.368 1.00 26.32 ATOM 4269 CG ASP 3218 87.752 24.337 117.024 1.00 27.13 ATOM 4270 OD1 ASP 3218 86.517 24.401 116.912 1.00 28.80 ATOM 4271 OD2 ASP 3218 88.452 25.179 117.622 1.00 28.71 ATOM 4272 C ASP 3218 89.251 21.923 118.407 1.00 25.13 ATOM 4273 O ASP 3218 88.839 20.764 118.349 1.00 24.83 ATOM 4274 N SER 3219 89.384 22.591 119.553 1.00 24.85 ATOM 4275 CA SER 3219 89.059 22.012 120.858 1.00 25.80 ATOM 4276 CB SER 3219 87.601 22.321 121.227 1.00 26.52 ATOM 4277 OG SER 3219 87.342 22.022 122.598 1.00 27.15 ATOM 4278 C SER 3219 89.340 20.498 120.943 1.00 25.85 ATOM 4279 O SER 3219 88.430 19.659 120.911 1.00 25.51 ATOM 4280 N VAL 3220 90.623 20.169 121.062 1.00 24.81 ATOM 4281 CA VAL 3220 91.075 18.787 121.136 1.00 23.17 ATOM 4282 CB VAL 3220 92.610 18.705 120.943 1.00 21.31 ATOM 4283 CG1 VAL 3220 93.004 19.434 119.676 1.00 18.39 ATOM 4284 CG2 VAL 3220 93.330 19.297 122.137 1.00 21.38 ATOM 4285 C VAL 3220 90.696 18.149 122.457 1.00 23.53 ATOM 4286 O VAL 3220 90.519 18.835 123.452 1.00 23.23 ATOM 4287 N VAL 3221 90.597 16.827 122.458 1.00 24.67 ATOM 4288 CA VAL 3221 90.203 16.079 123.644 1.00 25.29 ATOM 4289 CB VAL 3221 88.685 15.861 123.588 1.00 25.96 ATOM 4290 CG1 VAL 3221 87.963 17.203 123.771 1.00 24.07 ATOM 4291 CG2 VAL 3221 88.304 15.265 122.217 1.00 22.59 ATOM 4292 C VAL 3221 90.939 14.737 123.694 1.00 26.24 ATOM 4293 O VAL 3221 91.462 14.268 122.687 1.00 27.55 ATOM 4294 N PRO 3222 90.977 14.092 124.861 1.00 25.89 ATOM 4295 CD PRO 3222 90.340 14.464 126.133 1.00 25.13 ATOM 4296 CA PRO 3222 91.676 12.805 124.972 1.00 25.81 ATOM 4297 CB PRO 3222 91.119 12.239 126.270 1.00 25.90 ATOM 4298 CG PRO 3222 91.008 13.496 127.112 1.00 26.13 ATOM 4299 C PRO 3222 91.513 11.872 123.774 1.00 25.76 ATOM 4300 O PRO 3222 92.471 11.243 123.343 1.00 25.53 ATOM 4301 N SER 3223 90.305 11.806 123.230 1.00 26.32 ATOM 4302 CA SER 3223 90.028 10.950 122.085 1.00 27.65 ATOM 4303 CB SER 3223 88.599 11.185 121.592 1.00 29.55 ATOM 4304 OG SER 3223 88.603 11.913 120.360 1.00 34.94 ATOM 4305 C SER 3223 90.983 11.226 120.923 1.00 27.77 ATOM 4306 O SER 3223 91.247 10.348 120.099 1.00 28.27 ATOM 4307 N ASP 3224 91.484 12.454 120.849 1.00 27.50 ATOM 4308 CA ASP 3224 92.381 12.851 119.769 1.00 26.47 ATOM 4309 CB ASP 3224 92.377 14.368 119.588 1.00 26.22 ATOM 4310 CG ASP 3224 91.016 14.911 119.194 1.00 26.25 ATOM 4311 OD1 ASP 3224 90.558 14.634 118.071 1.00 26.37 ATOM 4312 OD2 ASP 3224 90.407 15.620 120.018 1.00 26.47 ATOM 4313 C ASP 3224 93.813 12.401 119.964 1.00 26.68 ATOM 4314 O ASP 3224 94.589 12.406 119.016 1.00 27.42 ATOM 4315 N LYS 3225 94.182 12.033 121.186 1.00 27.01 ATOM 4316 CA LYS 3225 95.539 11.566 121.436 1.00 26.78 ATOM 4317 CB LYS 3225 95.645 10.893 122.798 1.00 27.79 ATOM 4318 CG LYS 3225 95.778 11.806 123.993 1.00 28.57 ATOM 4319 CD LYS 3225 96.060 10.984 125.240 1.00 28.90 ATOM 4320 CE LYS 3225 96.143 11.863 126.464 1.00 31.24 ATOM 4321 NZ LYS 3225 96.642 11.133 127.674 1.00 32.68 ATOM 4322 C LYS 3225 95.892 10.536 120.378 1.00 27.67 ATOM 4323 O LYS 3225 95.082 9.663 120.063 1.00 28.05 ATOM 4324 N GLY 3226 97.093 10.632 119.828 1.00 28.00 ATOM 4325 CA GLY 3226 97.505 9.671 118.821 1.00 29.59 ATOM 4326 C GLY 3226 98.593 10.173 117.889 1.00 30.53 ATOM 4327 O GLY 3226 99.216 11.211 118.132 1.00 32.30 ATOM 4328 N ASN 3227 98.845 9.423 116.824 1.00 29.28 ATOM 4329 CA ASN 3227 99.840 9.827 115.853 1.00 28.54 ATOM 4330 CB ASN 3227 100.713 8.647 115.436 1.00 29.62 ATOM 4331 CG ASN 3227 101.767 8.299 116.459 1.00 30.02 ATOM 4332 OD1 ASN 3227 102.592 9.133 116.832 1.00 30.16 ATOM 4333 ND2 ASN 3227 101.757 7.050 116.906 1.00 28.97 ATOM 4334 C ASN 3227 99.088 10.336 114.641 1.00 28.93 ATOM 4335 O ASN 3227 98.057 9.779 114.251 1.00 29.62 ATOM 4336 N TYR 3228 99.597 11.403 114.048 1.00 28.13 ATOM 4337 CA TYR 3228 98.977 11.958 112.858 1.00 27.28 ATOM 4338 CB TYR 3228 98.413 13.353 113.136 1.00 24.03 ATOM 4339 CG TYR 3228 97.233 13.292 114.060 1.00 21.44 ATOM 4340 CD1 TYR 3228 97.404 13.225 115.437 1.00 20.30 ATOM 4341 CE1 TYR 3228 96.325 13.042 116.284 1.00 19.53 ATOM 4342 CD2 TYR 3228 95.947 13.184 113.556 1.00 19.11 ATOM 4343 CE2 TYR 3228 94.867 12.999 114.389 1.00 18.07 ATOM 4344 CZ TYR 3228 95.057 12.927 115.750 1.00 18.86 ATOM 4345 OH TYR 3228 93.972 12.708 116.575 1.00 20.59 ATOM 4346 C TYR 3228 100.026 12.007 111.775 1.00 28.52 ATOM 4347 O TYR 3228 101.091 12.584 111.964 1.00 29.79 ATOM 4348 N THR 3229 99.734 11.382 110.642 1.00 29.19 ATOM 4349 CA THR 3229 100.679 11.366 109.540 1.00 29.34 ATOM 4350 CB THR 3229 101.048 9.949 109.133 1.00 28.43 ATOM 4351 OG1 THR 3229 101.531 9.232 110.270 1.00 28.14 ATOM 4352 CG2 THR 3229 102.119 9.988 108.069 1.00 27.79 ATOM 4353 C THR 3229 100.174 12.056 108.288 1.00 31.13 ATOM 4354 O THR 3229 99.069 11.778 107.808 1.00 30.37 ATOM 4355 N CYS 3230 100.993 12.956 107.755 1.00 32.69 ATOM 4356 CA CYS 3230 100.633 13.645 106.531 1.00 33.78 ATOM 4357 C CYS 3230 101.391 12.932 105.433 1.00 34.55 ATOM 4358 O CYS 3230 102.527 12.503 105.629 1.00 34.62 ATOM 4359 CB CYS 3230 101.049 15.105 106.567 1.00 34.39 ATOM 4360 SG CYS 3230 102.843 15.340 106.660 1.00 36.87 ATOM 4361 N ILE 3231 100.751 12.806 104.282 1.00 35.44 ATOM 4362 CA ILE 3231 101.336 12.126 103.144 1.00 36.41 ATOM 4363 CB ILE 3231 100.585 10.814 102.870 1.00 35.62 ATOM 4364 CG2 ILE 3231 101.145 10.131 101.638 1.00 35.26 ATOM 4365 CG1 ILE 3231 100.687 9.904 104.086 1.00 34.89 ATOM 4366 CD1 ILE 3231 99.936 8.621 103.927 1.00 35.47 ATOM 4367 C ILE 3231 101.246 12.997 101.906 1.00 38.07 ATOM 4368 O ILE 3231 100.176 13.125 101.303 1.00 39.42 ATOM 4369 N VAL 3232 102.364 13.600 101.526 1.00 38.92 ATOM 4370 CA VAL 3232 102.391 14.441 100.342 1.00 40.39 ATOM 4371 CB VAL 3232 103.264 15.669 100.578 1.00 39.85 ATOM 4372 CG1 VAL 3232 103.271 16.546 99.351 1.00 39.62 ATOM 4373 CG2 VAL 3232 102.736 16.437 101.775 1.00 39.18 ATOM 4374 C VAL 3232 102.957 13.582 99.221 1.00 42.03 ATOM 4375 O VAL 3232 104.005 12.959 99.384 1.00 42.84 ATOM 4376 N GLU 3233 102.267 13.548 98.084 1.00 43.41 ATOM 4377 CA GLU 3233 102.698 12.700 96.977 1.00 44.19 ATOM 4378 CB GLU 3233 102.249 11.268 97.253 1.00 44.16 ATOM 4379 CG GLU 3233 100.801 11.210 97.745 1.00 46.42 ATOM 4380 CD GLU 3233 100.302 9.798 98.011 1.00 47.74 ATOM 4381 OE1 GLU 3233 99.245 9.660 98.677 1.00 46.48 ATOM 4382 OE2 GLU 3233 100.960 8.833 97.551 1.00 48.12 ATOM 4383 C GLU 3233 102.201 13.080 95.589 1.00 44.58 ATOM 4384 O GLU 3233 101.077 13.537 95.418 1.00 43.85 ATOM 4385 N ASN 3234 103.066 12.876 94.602 1.00 45.20 ATOM 4386 CA ASN 3234 102.734 13.111 93.210 1.00 45.75 ATOM 4387 CB ASN 3234 103.476 14.334 92.615 1.00 45.13 ATOM 4388 CG ASN 3234 104.982 14.134 92.491 1.00 44.18 ATOM 4389 OD1 ASN 3234 105.467 13.020 92.346 1.00 43.62 ATOM 4390 ND2 ASN 3234 105.723 15.233 92.520 1.00 43.12 ATOM 4391 C ASN 3234 103.152 11.825 92.514 1.00 46.39 ATOM 4392 O ASN 3234 103.416 10.828 93.173 1.00 46.09 ATOM 4393 N GLU 3235 103.235 11.852 91.194 1.00 47.69 ATOM 4394 CA GLU 3235 103.592 10.669 90.425 1.00 48.68 ATOM 4395 CB GLU 3235 103.195 10.907 88.975 1.00 50.55 ATOM 4396 CG GLU 3235 103.360 9.735 88.053 1.00 53.73 ATOM 4397 CD GLU 3235 102.929 10.088 86.647 1.00 56.51 ATOM 4398 OE1 GLU 3235 103.437 11.103 86.115 1.00 56.67 ATOM 4399 OE2 GLU 3235 102.083 9.360 86.078 1.00 59.10 ATOM 4400 C GLU 3235 105.059 10.242 90.499 1.00 48.11 ATOM 4401 O GLU 3235 105.398 9.114 90.157 1.00 48.22 ATOM 4402 N TYR 3236 105.925 11.127 90.972 1.00 47.64 ATOM 4403 CA TYR 3236 107.352 10.835 91.034 1.00 46.82 ATOM 4404 CB TYR 3236 108.112 11.980 90.359 1.00 47.99 ATOM 4405 CG TYR 3236 107.695 12.162 88.924 1.00 49.09 ATOM 4406 CD1 TYR 3236 106.387 12.517 88.596 1.00 50.10 ATOM 4407 CE1 TYR 3236 105.964 12.578 87.272 1.00 50.72 ATOM 4408 CD2 TYR 3236 108.575 11.886 87.889 1.00 49.80 ATOM 4409 CE2 TYR 3236 108.163 11.946 86.563 1.00 50.77 ATOM 4410 CZ TYR 3236 106.859 12.289 86.264 1.00 50.58 ATOM 4411 OH TYR 3236 106.454 12.313 84.957 1.00 50.48 ATOM 4412 C TYR 3236 107.898 10.610 92.429 1.00 45.57 ATOM 4413 O TYR 3236 109.104 10.652 92.645 1.00 45.09 ATOM 4414 N GLY 3237 107.011 10.372 93.381 1.00 44.21 ATOM 4415 CA GLY 3237 107.468 10.159 94.736 1.00 41.97 ATOM 4416 C GLY 3237 106.448 10.529 95.786 1.00 39.88 ATOM 4417 O GLY 3237 105.378 11.048 95.482 1.00 40.72 ATOM 4418 N SER 3238 106.795 10.249 97.033 1.00 37.18 ATOM 4419 CA SER 3238 105.938 10.530 98.161 1.00 34.84 ATOM 4420 CB SER 3238 105.051 9.329 98.446 1.00 33.70 ATOM 4421 OG SER 3238 105.132 8.981 99.816 1.00 33.08 ATOM 4422 C SER 3238 106.806 10.788 99.374 1.00 34.34 ATOM 4423 O SER 3238 107.893 10.241 99.484 1.00 35.66 ATOM 4424 N ILE 3239 106.347 11.653 100.266 1.00 33.12 ATOM 4425 CA ILE 3239 107.062 11.907 101.511 1.00 31.89 ATOM 4426 CB ILE 3239 107.867 13.215 101.533 1.00 32.23 ATOM 4427 CG2 ILE 3239 109.033 13.115 100.564 1.00 33.32 ATOM 4428 CG1 ILE 3239 106.967 14.400 101.227 1.00 32.64 ATOM 4429 CD1 ILE 3239 107.746 15.668 100.981 1.00 33.49 ATOM 4430 C ILE 3239 106.011 11.957 102.592 1.00 31.51 ATOM 4431 O ILE 3239 104.804 12.047 102.308 1.00 32.20 ATOM 4432 N ASN 3240 106.458 11.877 103.835 1.00 29.70 ATOM 4433 CA ASN 3240 105.513 11.876 104.938 1.00 28.30 ATOM 4434 CB ASN 3240 104.794 10.520 105.012 1.00 26.31 ATOM 4435 CG ASN 3240 105.655 9.440 105.630 1.00 25.18 ATOM 4436 OD1 ASN 3240 105.819 9.384 106.844 1.00 25.49 ATOM 4437 ND2 ASN 3240 106.221 8.584 104.794 1.00 24.73 ATOM 4438 C ASN 3240 106.195 12.164 106.258 1.00 27.90 ATOM 4439 O ASN 3240 107.323 11.739 106.502 1.00 27.83 ATOM 4440 N HIS 3241 105.487 12.895 107.104 1.00 27.06 ATOM 4441 CA HIS 3241 105.978 13.261 108.414 1.00 26.58 ATOM 4442 CB HIS 3241 106.143 14.775 108.498 1.00 26.17 ATOM 4443 CG HIS 3241 106.970 15.226 109.656 1.00 25.26 ATOM 4444 CD2 HIS 3241 106.617 15.707 110.870 1.00 25.19 ATOM 4445 ND1 HIS 3241 108.345 15.183 109.646 1.00 24.49 ATOM 4446 CE1 HIS 3241 108.805 15.621 110.802 1.00 25.12 ATOM 4447 NE2 HIS 3241 107.777 15.946 111.563 1.00 25.55 ATOM 4448 C HIS 3241 104.900 12.811 109.387 1.00 26.77 ATOM 4449 O HIS 3241 103.739 12.667 109.007 1.00 27.47 ATOM 4450 N THR 3242 105.275 12.597 110.638 1.00 26.59 ATOM 4451 CA THR 3242 104.317 12.156 111.631 1.00 26.19 ATOM 4452 CB THR 3242 104.465 10.661 111.915 1.00 26.59 ATOM 4453 OG1 THR 3242 103.849 9.915 110.858 1.00 27.70 ATOM 4454 CG2 THR 3242 103.828 10.297 113.245 1.00 26.65 ATOM 4455 C THR 3242 104.471 12.894 112.934 1.00 26.79 ATOM 4456 O THR 3242 105.542 12.906 113.518 1.00 26.77 ATOM 4457 N TYR 3243 103.382 13.502 113.390 1.00 28.48 ATOM 4458 CA TYR 3243 103.370 14.243 114.645 1.00 29.17 ATOM 4459 CB TYR 3243 102.625 15.570 114.486 1.00 29.29 ATOM 4460 CG TYR 3243 103.268 16.528 113.519 1.00 28.26 ATOM 4461 CD1 TYR 3243 102.774 16.678 112.241 1.00 27.48 ATOM 4462 CE1 TYR 3243 103.364 17.556 111.345 1.00 29.98 ATOM 4463 CD2 TYR 3243 104.379 17.282 113.890 1.00 28.49 ATOM 4464 CE2 TYR 3243 104.981 18.162 113.003 1.00 28.64 ATOM 4465 CZ TYR 3243 104.470 18.299 111.728 1.00 29.37 ATOM 4466 OH TYR 3243 105.049 19.176 110.834 1.00 29.75 ATOM 4467 C TYR 3243 102.673 13.424 115.709 1.00 29.58 ATOM 4468 O TYR 3243 101.807 12.604 115.410 1.00 30.21 ATOM 4469 N GLN 3244 103.048 13.648 116.956 1.00 30.31 ATOM 4470 CA GLN 3244 102.431 12.918 118.035 1.00 30.89 ATOM 4471 CB GLN 3244 103.487 12.215 118.875 1.00 32.36 ATOM 4472 CG GLN 3244 103.029 10.858 119.367 1.00 33.61 ATOM 4473 CD GLN 3244 103.674 10.485 120.676 1.00 33.52 ATOM 4474 OE1 GLN 3244 104.901 10.500 120.800 1.00 34.41 ATOM 4475 NE2 GLN 3244 102.850 10.154 121.669 1.00 31.76 ATOM 4476 C GLN 3244 101.660 13.901 118.886 1.00 31.02 ATOM 4477 O GLN 3244 102.225 14.875 119.389 1.00 31.24 ATOM 4478 N LEU 3245 100.365 13.652 119.038 1.00 30.44 ATOM 4479 CA LEU 3245 99.528 14.521 119.844 1.00 29.31 ATOM 4480 CB LEU 3245 98.191 14.800 119.156 1.00 28.75 ATOM 4481 CG LEU 3245 97.199 15.558 120.052 1.00 28.69 ATOM 4482 CD1 LEU 3245 97.836 16.833 120.593 1.00 27.11 ATOM 4483 CD2 LEU 3245 95.946 15.873 119.270 1.00 27.94 ATOM 4484 C LEU 3245 99.252 13.878 121.177 1.00 28.63 ATOM 4485 O LEU 3245 98.953 12.694 121.248 1.00 29.05 ATOM 4486 N ASP 3246 99.368 14.672 122.231 1.00 27.91 ATOM 4487 CA ASP 3246 99.095 14.214 123.582 1.00 27.90 ATOM 4488 CB ASP 3246 100.391 13.965 124.350 1.00 27.24 ATOM 4489 CG ASP 3246 100.150 13.276 125.677 1.00 27.72 ATOM 4490 OD1 ASP 3246 101.128 12.946 126.379 1.00 29.17 ATOM 4491 OD2 ASP 3246 98.973 13.059 126.022 1.00 27.39 ATOM 4492 C ASP 3246 98.292 15.321 124.266 1.00 28.92 ATOM 4493 O ASP 3246 98.747 16.472 124.359 1.00 29.31 ATOM 4494 N VAL 3247 97.092 14.965 124.726 1.00 28.06 ATOM 4495 CA VAL 3247 96.182 15.895 125.388 1.00 26.11 ATOM 4496 CB VAL 3247 94.729 15.709 124.860 1.00 25.73 ATOM 4497 CG1 VAL 3247 93.838 16.839 125.351 1.00 26.58 ATOM 4498 CG2 VAL 3247 94.722 15.652 123.348 1.00 23.43 ATOM 4499 C VAL 3247 96.189 15.650 126.890 1.00 25.57 ATOM 4500 O VAL 3247 95.985 14.534 127.335 1.00 25.19 ATOM 4501 N VAL 3248 96.404 16.711 127.660 1.00 25.99 ATOM 4502 CA VAL 3248 96.467 16.636 129.115 1.00 25.90 ATOM 4503 CB VAL 3248 97.739 17.334 129.639 1.00 24.68 ATOM 4504 OG1 VAL 3248 97.791 17.250 131.150 1.00 25.57 ATOM 4505 CG2 VAL 3248 98.969 16.702 129.039 1.00 23.95 ATOM 4506 C VAL 3248 95.294 17.289 129.820 1.00 26.80 ATOM 4507 O VAL 3248 95.012 18.460 129.598 1.00 28.79 ATOM 4508 N GLU 3249 94.643 16.533 130.692 1.00 27.86 ATOM 4509 CA GLU 3249 93.543 17.062 131.475 1.00 30.65 ATOM 4510 CB GLU 3249 92.473 15.989 131.695 1.00 33.93 ATOM 4511 CG GLU 3249 91.804 15.484 130.420 1.00 39.01 ATOM 4512 CD GLU 3249 91.336 14.032 130.540 1.00 42.24 ATOM 4513 OE1 GLU 3249 92.203 13.129 130.667 1.00 43.35 ATOM 4514 OE2 GLU 3249 90.105 13.791 130.508 1.00 44.63 ATOM 4515 C GLU 3249 94.221 17.414 132.797 1.00 30.24 ATOM 4516 O GLU 3249 95.051 16.654 133.283 1.00 29.98 ATOM 4517 N ARG 3250 93.895 18.569 133.366 1.00 30.25 ATOM 4518 CA ARG 3250 94.505 18.987 134.623 1.00 30.41 ATOM 4519 CB ARG 3250 95.033 20.424 134.528 1.00 30.07 ATOM 4520 CG ARG 3250 96.019 20.709 133.402 1.00 28.85 ATOM 4521 CD ARG 3250 97.304 19.922 133.576 1.00 27.97 ATOM 4522 NE ARG 3250 97.881 20.115 134.902 1.00 26.90 ATOM 4523 CZ ARG 3250 98.860 20.967 135.188 1.00 26.21 ATOM 4524 NH1 ARG 3250 99.398 21.726 134.243 1.00 23.51 ATOM 4525 NH2 ARG 3250 99.300 21.053 136.433 1.00 27.00 ATOM 4526 C ARG 3250 93.475 18.928 135.728 1.00 31.02 ATOM 4527 O ARG 3250 92.307 19.200 135.501 1.00 31.46 ATOM 4528 N SER 3251 93.908 18.567 136.924 1.00 31.93 ATOM 4529 CA SER 3251 93.002 18.509 138.050 1.00 34.02 ATOM 4530 CS SER 3251 93.086 17.158 138.745 1.00 35.31 ATOM 4531 OG SER 3251 92.196 16.241 138.138 1.00 39.58 ATOM 4532 C SER 3251 93.349 19.622 139.019 1.00 34.88 ATOM 4533 O SER 3251 94.106 19.430 139.975 1.00 35.54 ATOM 4534 N PRO 3252 92.794 20.812 138.777 1.00 35.37 ATOM 4535 CD PRO 3252 91.905 21.123 137.643 1.00 35.49 ATOM 4536 CA PRO 3252 93.003 22.009 139.586 1.00 36.36 ATOM 4537 CB PRO 3252 92.649 23.124 138.621 1.00 35.28 ATOM 4538 CG PRO 3252 91.459 22.545 137.954 1.00 35.69 ATOM 4539 C PRO 3252 92.121 22.034 140.829 1.00 37.74 ATOM 4540 O PRO 3252 91.161 22.802 140.908 1.00 37.38 ATOM 4541 N HIS 3253 92.447 21.194 141.799 1.00 39.53 ATOM 4542 CA HIS 3253 91.678 21.159 143.029 1.00 41.88 ATOM 4543 CB HIS 3253 90.529 20.134 142.918 1.00 46.74 ATOM 4544 CG HIS 3253 90.943 18.791 142.384 1.00 52.59 ATOM 4545 CD2 HIS 3253 90.540 18.108 141.283 1.00 54.92 ATOM 4546 ND1 HIS 3253 91.857 17.975 143.024 1.00 55.10 ATOM 4547 CE1 HIS 3253 91.995 16.850 142.343 1.00 55.48 ATOM 4548 NE2 HIS 3253 91.206 16.904 141.283 1.00 55.66 ATOM 4549 C HIS 3253 92.577 20.854 144.221 1.00 40.56 ATOM 4550 O HIS 3253 93.738 20.478 144.051 1.00 39.99 ATOM 4551 N ARG 3254 92.052 21.054 145.426 1.00 39.06 ATOM 4552 CA ARG 3254 92.819 20.761 146.629 1.00 36.99 ATOM 4553 CB ARG 3254 92.008 21.110 147.887 1.00 37.56 ATOM 4554 CG ARG 3254 90.502 20.865 147.776 1.00 39.95 ATOM 4555 CD ARG 3254 89.743 21.410 149.003 1.00 43.17 ATOM 4556 NE ARG 3254 88.289 21.496 148.798 1.00 46.65 ATOM 4557 CZ ARG 3254 87.679 22.342 147.959 1.00 48.09 ATOM 4558 NH1 ARG 3254 88.384 23.198 147.228 1.00 48.53 ATOM 4559 NH2 ARG 3254 86.356 22.327 147.831 1.00 48.59 ATOM 4560 C ARG 3254 93.129 19.275 146.584 1.00 34.92 ATOM 4561 O ARG 3254 92.444 18.516 145.909 1.00 34.69 ATOM 4562 N PRO 3255 94.179 18.837 147.284 1.00 33.60 ATOM 4563 CD PRO 3255 95.155 19.619 148.060 1.00 33.94 ATOM 4564 CA PRO 3255 94.530 17.413 147.285 1.00 32.24 ATOM 4565 CB PRO 3255 95.702 17.353 148.253 1.00 32.62 ATOM 4566 CG PRO 3255 96.346 18.701 148.074 1.00 33.33 ATOM 4567 C PRO 3255 93.369 16.527 147.735 1.00 30.77 ATOM 4568 O PRO 3255 92.468 16.979 148.431 1.00 31.17 ATOM 4569 N ILE 3256 93.396 15.263 147.338 1.00 29.48 ATOM 4570 CA ILE 3256 92.341 14.332 147.703 1.00 28.59 ATOM 4571 CB ILE 3256 91.587 13.839 146.449 1.00 27.91 ATOM 4572 CG2 ILE 3256 90.507 12.845 146.834 1.00 29.43 ATOM 4573 CG1 ILE 3256 90.941 15.022 145.736 1.00 25.98 ATOM 4574 CD1 ILE 3256 90.229 14.643 144.477 1.00 26.04 ATOM 4575 C ILE 3256 92.965 13.151 148.425 1.00 29.03 ATOM 4576 O ILE 3256 93.915 12.548 147.926 1.00 29.94 ATOM 4577 N LEU 3257 92.434 12.826 149.602 1.00 28.80 ATOM 4578 CA LEU 3257 92.962 11.721 150.399 1.00 28.38 ATOM 4579 CB LEE 3257 93.061 12.139 151.869 1.00 26.67 ATOM 4580 CG LEU 3257 93.601 13.547 152.154 1.00 24.49 ATOM 4581 CD1 LEU 3257 93.584 13.840 153.644 1.00 22.81 ATOM 4582 CD2 LEU 3257 94.997 13.659 151.613 1.00 23.52 ATOM 4583 C LEU 3257 92.072 10.495 150.274 1.00 28.27 ATOM 4584 O LEU 3257 90.857 10.598 150.393 1.00 28.75 ATOM 4585 N GLN 3258 92.680 9.337 150.025 1.00 28.85 ATOM 4586 CA GLN 3258 91.933 8.089 149.891 1.00 28.72 ATOM 4587 CB GLN 3258 92.896 6.903 149.780 1.00 27.32 ATOM 4588 C GLN 3258 91.040 7.925 151.114 1.00 28.84 ATOM 4589 O GLN 3258 91.528 7.882 152.251 1.00 29.72 ATOM 4590 N ALA 3259 89.732 7.862 150.888 1.00 27.60 ATOM 4591 CA ALA 3259 88.805 7.704 151.992 1.00 26.97 ATOM 4592 CB ALA 3259 87.404 7.573 151.469 1.00 26.90 ATOM 4593 C ALA 3259 89.204 6.461 152.777 1.00 27.13 ATOM 4594 O ALA 3259 89.718 5.500 152.208 1.00 27.15 ATOM 4595 N GLY 3260 88.991 6.492 154.086 1.00 26.91 ATOM 4596 CA GLY 3260 89.335 5.347 154.900 1.00 26.38 ATOM 4597 C GLY 3260 90.718 5.420 155.508 1.00 26.52 ATOM 4598 O GLY 3260 90.988 4.767 156.519 1.00 26.75 ATOM 4599 N LEU 3261 91.598 6.210 154.903 1.00 26.39 ATOM 4600 CA LEU 3261 92.958 6.359 155.417 1.00 27.04 ATOM 4601 CB LEU 3261 93.962 6.022 154.333 1.00 26.16 ATOM 4602 CG LEU 3261 93.859 4.620 153.767 1.00 24.65 ATOM 4603 CD1 LEU 3261 94.803 4.487 152.597 1.00 25.97 ATOM 4604 CD2 LEU 3261 94.196 3.623 154.848 1.00 23.96 ATOM 4605 C LEU 3261 93.231 7.781 155.887 1.00 27.98 ATOM 4606 O LEU 3261 92.841 8.743 155.221 1.00 28.15 ATOM 4607 N PRO 3262 93.915 7.935 157.034 1.00 27.82 ATOM 4608 CD PRO 3262 94.199 9.267 157.596 1.00 27.04 ATOM 4609 CA PRO 3262 94.443 6.879 157.905 1.00 27.29 ATOM 4610 CB PRO 3262 95.255 7.657 158.928 1.00 26.57 ATOM 4611 CG PRO 3262 94.507 8.949 159.031 1.00 25.59 ATOM 4612 C PRO 3262 93.320 6.090 158.549 1.00 27.40 ATOM 4613 O PRO 3262 92.171 6.527 158.540 1.00 27.33 ATOM 4614 N ALA 3263 93.649 4.940 159.122 1.00 27.92 ATOM 4615 CA ALA 3263 92.624 4.108 159.748 1.00 28.71 ATOM 4616 CB ALA 3263 92.638 2.730 159.125 1.00 28.45 ATOM 4617 C ALA 3263 92.749 3.976 161.254 1.00 28.80 ATOM 4618 O ALA 3263 93.841 3.831 161.779 1.00 29.46 ATOM 4619 N ASN 3264 91.622 4.019 161.949 1.00 28.97 ATOM 4620 CA ASN 3264 91.645 3.864 163.389 1.00 28.99 ATOM 4621 CB ASN 3264 90.234 3.840 163.954 1.00 27.63 ATOM 4622 CG ASN 3264 89.562 5.166 163.857 1.00 28.47 ATOM 4623 OD1 ASN 3264 90.224 6.183 163.687 1.00 29.69 ATOM 4624 ND2 ASN 3264 88.241 5.181 163.982 1.00 29.95 ATOM 4625 C ASN 3264 92.303 2.537 163.689 1.00 30.40 ATOM 4626 O ASN 3264 92.068 1.559 162.991 1.00 31.27 ATOM 4627 N LYS 3265 93.131 2.497 164.722 1.00 32.26 ATOM 4628 CA LYS 3265 93.784 1.259 165.096 1.00 34.23 ATOM 4629 CB LYS 3265 95.195 1.197 164.512 1.00 33.73 ATOM 4630 CG LYS 3265 95.200 1.353 163.001 1.00 36.20 ATOM 4631 CD LYS 3265 96.425 0.751 162.324 1.00 35.68 ATOM 4632 CE LYS 3265 96.349 0.942 160.802 1.00 36.29 ATOM 4633 NZ LYS 3265 96.399 2.381 160.343 1.00 36.19 ATOM 4634 C LYS 3265 93.861 1.143 166.598 1.00 36.25 ATOM 4635 O LYS 3265 94.239 2.095 167.283 1.00 37.73 ATOM 4636 N THR 3266 93.475 −0.020 167.113 1.00 37.24 ATOM 4637 CA THR 3266 93.553 −0.280 168.546 1.00 36.86 ATOM 4638 CB THR 3266 92.287 −0.948 169.090 1.00 37.14 ATOM 4639 OG1 THR 3266 91.211 0.001 169.119 1.00 38.13 ATOM 4640 CG2 THR 3266 92.541 −1.480 170.486 1.00 37.17 ATOM 4641 C THR 3266 94.699 −1.257 168.690 1.00 36.59 ATOM 4642 O THR 3266 94.750 −2.266 167.992 1.00 35.31 ATOM 4643 N VAL 3267 95.637 −0.950 169.570 1.00 37.49 ATOM 4644 CA VAL 3267 96.765 −1.839 169.756 1.00 38.41 ATOM 4645 CB VAL 3267 97.956 −1.443 168.889 1.00 37.78 ATOM 4646 CG1 VAL 3267 97.582 −1.534 167.427 1.00 36.85 ATOM 4647 CG2 VAL 3267 98.424 −0.056 169.269 1.00 38.27 ATOM 4648 C VAL 3267 97.251 −1.931 171.184 1.00 39.74 ATOM 4649 O VAL 3267 96.917 −1.103 172.037 1.00 39.65 ATOM 4650 N ALA 3268 98.062 −2.958 171.415 1.00 41.45 ATOM 4651 CA ALA 3268 98.634 −3.248 172.719 1.00 42.65 ATOM 4652 CB ALA 3268 99.206 −4.659 172.717 1.00 42.62 ATOM 4653 C ALA 3268 99.716 −2.248 173.102 1.00 42.98 ATOM 4654 O ALA 3268 100.460 −1.753 172.254 1.00 42.72 ATOM 4655 N LEU 3269 99.793 −1.949 174.390 1.00 43.80 ATOM 4656 CA LEU 3269 100.799 −1.025 174.878 1.00 44.03 ATOM 4657 CB LEU 3269 100.722 −0.936 176.402 1.00 43.53 ATOM 4658 CG LEU 3269 101.513 0.180 177.076 1.00 43.63 ATOM 4659 CD1 LEU 3269 101.185 0.198 178.554 1.00 42.55 ATOM 4660 CD2 LEU 3269 102.997 −0.026 176.847 1.00 43.57 ATOM 4661 C LEU 3269 102.157 −1.562 174.443 1.00 44.04 ATOM 4662 O LEU 3269 102.408 −2.767 174.518 1.00 44.70 ATOM 4663 N GLY 3270 103.019 −0.670 173.967 1.00 44.06 ATOM 4664 CA GLY 3270 104.345 −1.072 173.533 1.00 44.11 ATOM 4665 C GLY 3270 104.444 −1.611 172.120 1.00 43.68 ATOM 4666 O GLY 3270 105.537 −1.870 171.631 1.00 44.34 ATOM 4667 N SER 3271 103.313 −1.782 171.452 1.00 43.40 ATOM 4668 CA SER 3271 103.331 −2.300 170.095 1.00 43.72 ATOM 4669 CB SER 3271 101.916 −2.647 169.654 1.00 44.49 ATOM 4670 OG SER 3271 101.400 −3.715 170.425 1.00 47.59 ATOM 4671 C SER 3271 103.937 −1.324 169.100 1.00 43.31 ATOM 4672 O SER 3271 104.451 −0.272 169.472 1.00 43.23 ATOM 4673 N ASN 3272 103.893 −1.702 167.828 1.00 42.89 ATOM 4674 CA ASN 3272 104.381 −0.853 166.754 1.00 42.44 ATOM 4675 CB ASN 3272 105.553 −1.500 166.020 1.00 42.30 ATOM 4676 CG ASN 3272 106.897 −1.031 166.560 1.00 43.38 ATOM 4677 OD1 ASN 3272 107.047 −0.801 167.760 1.00 44.26 ATOM 4678 ND2 ASN 3272 107.882 −0.895 165.678 1.00 42.85 ATOM 4679 C ASN 3272 103.207 −0.638 165.826 1.00 41.87 ATOM 4680 O ASN 3272 102.445 −1.562 165.533 1.00 42.45 ATOM 4681 N VAL 3273 103.031 0.594 165.386 1.00 40.66 ATOM 4682 CA VAL 3273 101.922 0.876 164.506 1.00 40.23 ATOM 4683 CB VAL 3273 100.717 1.369 165.329 1.00 40.17 ATOM 4684 CG1 VAL 3273 101.096 2.625 166.103 1.00 40.95 ATOM 4685 CG2 VAL 3273 99.523 1.601 164.420 1.00 40.27 ATOM 4686 C VAL 3273 102.312 1.882 163.427 1.00 39.67 ATOM 4687 O VAL 3273 103.176 2.743 163.638 1.00 38.85 ATOM 4688 N GLU 3274 101.697 1.740 162.258 1.00 38.75 ATOM 4689 CA GLU 3274 101.973 2.635 161.153 1.00 39.69 ATOM 4690 CB GLU 3274 102.820 1.930 160.090 1.00 41.41 ATOM 4691 CG GLU 3274 102.174 0.682 159.520 1.00 45.93 ATOM 4692 CD GLU 3274 102.775 0.252 158.193 1.00 47.99 ATOM 4693 OE1 GLU 3274 103.969 −0.130 158.166 1.00 49.33 ATOM 4694 OE2 GLU 3274 102.046 0.303 157.174 1.00 48.79 ATOM 4695 C GLU 3274 100.658 3.111 160.540 1.00 39.16 ATOM 4696 O GLU 3274 99.771 2.307 160.239 1.00 39.37 ATOM 4697 N PHE 3275 100.533 4.426 160.377 1.00 37.34 ATOM 4698 CA PHE 3275 99.343 5.025 159.794 1.00 35.65 ATOM 4699 CB PHE 3275 98.988 6.312 160.531 1.00 35.93 ATOM 4700 CG PHE 3275 98.371 6.086 161.888 1.00 36.46 ATOM 4701 CD1 PHE 3275 97.000 5.865 162.018 1.00 36.34 ATOM 4702 CD2 PHE 3275 99.158 6.108 163.039 1.00 36.18 ATOM 4703 CE1 PHE 3275 96.425 5.677 163.266 1.00 35.66 ATOM 4704 CE2 PHE 3275 98.593 5.920 164.288 1.00 35.26 ATOM 4705 CZ PHE 3275 97.223 5.706 164.403 1.00 36.25 ATOM 4706 C PHE 3275 99.623 5.325 158.340 1.00 34.81 ATOM 4707 O PHE 3275 100.748 5.633 157.980 1.00 35.61 ATOM 4708 N MET 3276 98.605 5.232 157.497 1.00 33.75 ATOM 4709 CA MET 3276 98.805 5.490 156.087 1.00 32.92 ATOM 4710 CB MET 3276 98.557 4.243 155.262 1.00 34.99 ATOM 4711 CG MET 3276 99.786 3.391 155.060 1.00 38.18 ATOM 4712 SD MET 3276 99.571 2.378 153.591 1.00 42.05 ATOM 4713 CE MET 3276 99.885 3.632 152.264 1.00 41.35 ATOM 4714 C MET 3276 97.958 6.602 155.543 1.00 31.97 ATOM 4715 O MET 3276 96.865 6.874 156.026 1.00 31.01 ATOM 4716 N CYS 3277 98.475 7.231 154.500 1.00 32.15 ATOM 4717 CA CYS 3277 97.797 8.345 153.874 1.00 32.48 ATOM 4718 C CYS 3277 98.093 8.406 152.389 1.00 32.61 ATOM 4719 O CYS 3277 99.217 8.710 152.001 1.00 33.63 ATOM 4720 CB CYS 3277 98.268 9.629 154.515 1.00 31.50 ATOM 4721 SG CYS 3277 97.213 11.028 154.104 1.00 32.81 ATOM 4722 N LYS 3278 97.086 8.124 151.566 1.00 32.56 ATOM 4723 CA LYS 3278 97.234 8.140 150.113 1.00 32.30 ATOM 4724 CB LYS 3278 96.478 6.953 149.507 1.00 34.17 ATOM 4725 CG LYS 3278 97.321 6.022 148.640 1.00 37.65 ATOM 4726 CD LYS 3278 96.442 5.147 147.720 1.00 40.56 ATOM 4727 CE LYS 3278 95.583 5.998 146.746 1.00 41.33 ATOM 4728 NZ LYS 3278 94.680 5.218 145.833 1.00 38.90 ATOM 4729 C LYS 3278 96.684 9.462 149.554 1.00 31.44 ATOM 4730 O LYS 3278 95.478 9.710 149.599 1.00 31.95 ATOM 4731 N VAL 3279 97.565 10.307 149.024 1.00 29.86 ATOM 4732 CA VAL 3279 97.158 11.607 148.489 1.00 27.85 ATOM 4733 CB VAL 3279 98.071 12.734 148.985 1.00 26.96 ATOM 4734 CG1 VAL 3279 97.568 14.064 148.475 1.00 25.70 ATOM 4735 CG2 VAL 3279 98.140 12.728 150.483 1.00 28.06 ATOM 4736 C VAL 3279 97.188 11.716 146.980 1.00 27.93 ATOM 4737 O VAL 3279 98.060 11.149 146.327 1.00 28.90 ATOM 4738 N TYR 3280 96.227 12.453 146.431 1.00 27.27 ATOM 4739 CA TYR 3280 96.186 12.703 144.998 1.00 26.48 ATOM 4740 CB TYR 3280 94.926 12.163 144.340 1.00 26.34 ATOM 4741 CG TYR 3280 94.883 12.547 142.877 1.00 26.58 ATOM 4742 CD1 TYR 3280 95.678 11.883 141.945 1.00 26.09 ATOM 4743 CE1 TYR 3280 95.758 12.303 140.626 1.00 25.75 ATOM 4744 CD2 TYR 3280 94.146 13.649 142.445 1.00 26.17 ATOM 4745 CE2 TYR 3280 94.215 14.084 141.126 1.00 27.68 ATOM 4746 CZ TYR 3280 95.033 13.408 140.218 1.00 28.39 ATOM 4747 OH TYR 3280 95.172 13.866 138.917 1.00 29.19 ATOM 4748 C TYR 3280 96.195 14.212 144.820 1.00 26.25 ATOM 4749 O TYR 3280 95.560 14.930 145.585 1.00 26.63 ATOM 4750 N SER 3281 96.911 14.697 143.816 1.00 25.82 ATOM 4751 CA SER 3281 96.964 16.130 143.570 1.00 25.99 ATOM 4752 CB SER 3281 97.601 16.859 144.764 1.00 27.74 ATOM 4753 OG SER 3281 97.606 18.270 144.578 1.00 29.73 ATOM 4754 C SER 3281 97.757 16.405 142.317 1.00 24.60 ATOM 4755 O SER 3281 98.848 15.882 142.143 1.00 24.71 ATOM 4756 N ASP 3282 97.194 17.217 141.431 1.00 24.73 ATOM 4757 CA ASP 3282 97.891 17.549 140.206 1.00 24.05 ATOM 4758 CB ASP 3282 96.981 18.367 139.285 1.00 24.90 ATOM 4759 CG ASP 3282 97.553 18.525 137.897 1.00 26.63 ATOM 4760 OD1 ASP 3282 96.849 19.040 136.992 1.00 26.29 ATOM 4761 OD2 ASP 3282 98.719 18.127 137.717 1.00 28.43 ATOM 4762 C ASP 3282 99.096 18.357 140.673 1.00 23.14 ATOM 4763 O ASP 3282 100.230 17.872 140.629 1.00 23.70 ATOM 4764 N PRO 3283 98.867 19.584 141.173 1.00 21.96 ATOM 4765 CD PRO 3283 97.607 20.287 141.441 1.00 21.41 ATOM 4766 CA PRO 3283 99.988 20.391 141.634 1.00 21.24 ATOM 4767 CB PRO 3283 99.316 21.668 142.111 1.00 20.49 ATOM 4768 CG PRO 3283 98.043 21.698 141.376 1.00 19.84 ATOM 4769 C PRO 3283 100.673 19.652 142.775 1.00 22.00 ATOM 4770 O PRO 3283 100.019 18.974 143.569 1.00 22.58 ATOM 4771 N GLN 3284 101.985 19.787 142.862 1.00 21.77 ATOM 4772 CA GLN 3284 102.731 19.100 143.894 1.00 22.25 ATOM 4773 CB GLN 3284 104.193 19.519 143.817 1.00 22.11 ATOM 4774 CG GLN 3284 105.167 18.363 143.885 1.00 21.39 ATOM 4775 CD GLN 3284 104.727 17.168 143.070 1.00 20.44 ATOM 4776 OE1 GLN 3284 104.308 17.294 141.927 1.00 21.08 ATOM 4777 NE2 GLN 3284 104.839 15.993 143.659 1.00 22.03 ATOM 4778 C GLN 3284 102.138 19.397 145.259 1.00 23.07 ATOM 4779 O GLN 3284 102.113 20.541 145.696 1.00 25.06 ATOM 4780 N PRO 3285 101.625 18.365 145.943 1.00 23.82 ATOM 4781 CD PRO 3285 101.402 16.995 145.447 1.00 23.47 ATOM 4782 CA PRO 3285 101.022 18.529 147.266 1.00 24.63 ATOM 4783 CB PRO 3285 100.077 17.342 147.355 1.00 23.30 ATOM 4784 CG PRO 3285 100.879 16.277 146.685 1.00 23.16 ATOM 4785 C PRO 3285 102.052 18.501 148.379 1.00 25.09 ATOM 4786 O PRO 3285 103.148 17.968 148.206 1.00 25.46 ATOM 4787 N HIS 3286 101.700 19.080 149.518 1.00 25.38 ATOM 4788 CA HIS 3286 102.610 19.062 150.635 1.00 25.96 ATOM 4789 CB HIS 3286 103.016 20.461 151.040 1.00 26.69 ATOM 4790 CG HIS 3286 104.002 20.468 152.154 1.00 27.68 ATOM 4791 CD2 HIS 3286 105.002 19.608 152.454 1.00 28.17 ATOM 4792 ND1 HIS 3286 104.003 21.419 153.148 1.00 29.66 ATOM 4793 CE1 HIS 3286 104.960 21.141 154.016 1.00 30.81 ATOM 4794 NE2 HIS 3286 105.581 20.045 153.617 1.00 29.40 ATOM 4795 C HIS 3286 101.947 18.357 151.810 1.00 26.58 ATOM 4796 O HIS 3286 101.061 18.905 152.472 1.00 26.84 ATOM 4797 N ILE 3287 102.384 17.128 152.055 1.00 26.39 ATOM 4798 CA ILE 3287 101.846 16.312 153.131 1.00 26.11 ATOM 4799 CB ILE 3287 102.083 14.831 152.853 1.00 24.99 ATOM 4800 CG2 ILE 3287 101.725 13.997 154.069 1.00 22.95 ATOM 4801 CG1 ILE 3287 101.288 14.420 151.626 1.00 23.31 ATOM 4802 CD1 ILE 3287 101.531 13.009 151.238 1.00 25.95 ATOM 4803 C ILE 3287 102.483 16.630 154.464 1.00 26.79 ATOM 4804 O ILE 3287 103.640 17.022 154.533 1.00 28.01 ATOM 4805 N GLN 3288 101.728 16.429 155.532 1.00 26.95 ATOM 4806 CA GLN 3288 102.231 16.695 156.868 1.00 27.08 ATOM 4807 CB GLN 3288 102.097 18.183 157.182 1.00 26.69 ATOM 4808 CG GLN 3288 102.317 18.539 158.635 1.00 27.45 ATOM 4809 CD GLN 3288 102.359 20.033 158.867 1.00 27.88 ATOM 4810 OE1 GLN 3288 103.433 20.619 159.023 1.00 29.46 ATOM 4811 NE2 GLN 3288 101.190 20.663 158.880 1.00 26.56 ATOM 4812 C GLN 3288 101.445 15.870 157.871 1.00 27.00 ATOM 4813 O GLN 3288 100.217 15.850 157.821 1.00 26.94 ATOM 4814 N TRP 3289 102.156 15.192 158.772 1.00 25.98 ATOM 4815 CA TRP 3289 101.527 14.360 159.784 1.00 25.52 ATOM 4816 CB TRP 3289 102.339 13.077 159.985 1.00 24.71 ATOM 4817 CG TRP 3289 102.001 12.024 158.990 1.00 23.67 ATOM 4818 CD2 TRP 3289 100.833 11.188 159.005 1.00 23.20 ATOM 4819 CE2 TRP 3289 100.883 10.379 157.843 1.00 23.28 ATOM 4820 CE3 TRP 3289 99.748 11.039 159.886 1.00 21.68 ATOM 4821 CD1 TRP 3289 102.692 11.702 157.857 1.00 22.61 ATOM 4822 NE1 TRP 3289 102.026 10.715 157.157 1.00 22.39 ATOM 4823 CZ2 TRP 3289 99.890 9.435 157.539 1.00 22.38 ATOM 4824 CZ3 TRP 3289 98.760 10.100 159.588 1.00 20.53 ATOM 4825 CH2 TRP 3289 98.840 9.311 158.425 1.00 21.32 ATOM 4826 C TRP 3289 101.388 15.099 161.099 1.00 25.71 ATOM 4827 O TRP 3289 102.340 15.701 161.562 1.00 26.33 ATOM 4828 N LEU 3290 100.202 15.036 161.698 1.00 26.63 ATOM 4829 CA LEU 3290 99.917 15.711 162.964 1.00 27.02 ATOM 4830 CB LEU 3290 98.867 16.788 162.753 1.00 26.33 ATOM 4831 CG LEU 3290 99.341 18.190 162.414 1.00 27.76 ATOM 4832 CD1 LEU 3290 100.458 18.139 161.383 1.00 27.91 ATOM 4833 CD2 LEU 3290 98.144 19.000 161.925 1.00 28.54 ATOM 4834 C LEU 3290 99.392 14.804 164.050 1.00 27.20 ATOM 4835 O LEU 3290 98.741 13.814 163.769 1.00 27.70 ATOM 4836 N LYS 3291 99.665 15.174 165.296 1.00 28.78 ATOM 4837 CA LYS 3291 99.177 14.445 166.459 1.00 29.05 ATOM 4838 CB LYS 3291 100.329 13.897 167.291 1.00 29.73 ATOM 4839 CG LYS 3291 99.984 12.618 168.038 1.00 31.72 ATOM 4840 CD LYS 3291 98.679 12.748 168.800 1.00 33.36 ATOM 4841 CE LYS 3291 98.430 11.538 169.679 1.00 34.04 ATOM 4842 NZ LYS 3291 99.427 11.440 170.784 1.00 35.47 ATOM 4843 C LYS 3291 98.439 15.516 167.238 1.00 29.09 ATOM 4844 O LYS 3291 98.938 16.622 167.388 1.00 28.60 ATOM 4845 N HIS 3292 97.239 15.208 167.703 1.00 30.58 ATOM 4846 CA HIS 3292 96.445 16.185 168.444 1.00 31.34 ATOM 4847 CB HIS 3292 94.970 16.004 168.131 1.00 31.40 ATOM 4848 CG HIS 3292 94.605 16.387 166.738 1.00 32.93 ATOM 4849 CD2 HIS 3292 95.140 17.299 165.895 1.00 35.18 ATOM 4850 ND1 HIS 3292 93.543 15.824 166.068 1.00 34.66 ATOM 4851 CE1 HIS 3292 93.437 16.372 164.870 1.00 36.22 ATOM 4852 NE2 HIS 3292 94.395 17.271 164.740 1.00 35.90 ATOM 4853 C HIS 3292 96.659 16.037 169.929 1.00 31.79 ATOM 4854 O HIS 3292 96.496 14.943 170.458 1.00 32.99 ATOM 4855 N VAL 3308 98.305 20.855 168.555 1.00 33.31 ATOM 4856 CA VAL 3308 98.883 19.814 167.709 1.00 33.62 ATOM 4857 CB VAL 3308 98.555 20.032 166.217 1.00 35.09 ATOM 4858 CG1 VAL 3308 97.059 19.930 165.979 1.00 36.03 ATOM 4859 CG2 VAL 3308 99.094 21.385 165.765 1.00 35.70 ATOM 4860 C VAL 3308 100.397 19.718 167.794 1.00 32.33 ATOM 4861 O VAL 3308 101.075 20.661 168.186 1.00 32.08 ATOM 4862 N GLN 3309 100.910 18.560 167.397 1.00 31.42 ATOM 4863 CA GLN 3309 102.336 18.288 167.392 1.00 30.75 ATOM 4864 CB GLN 3309 102.675 17.191 168.410 1.00 31.95 ATOM 4865 CG GLN 3309 104.007 16.468 168.141 1.00 34.88 ATOM 4866 CD GLN 3309 104.304 15.344 169.141 1.00 35.19 ATOM 4867 OE1 GLN 3309 103.392 14.756 169.711 1.00 36.34 ATOM 4868 NE2 GLN 3309 105.583 15.035 169.336 1.00 35.52 ATOM 4869 C GLN 3309 102.723 17.832 165.995 1.00 29.59 ATOM 4870 O GLN 3309 102.300 16.772 165.539 1.00 28.60 ATOM 4871 N ILE 3310 103.513 18.637 165.300 1.00 28.64 ATOM 4872 CA ILE 3310 103.928 18.245 163.966 1.00 28.25 ATOM 4873 CB ILE 3310 104.687 19.375 163.290 1.00 27.05 ATOM 4874 CG2 ILE 3310 104.924 19.036 161.827 1.00 27.29 ATOM 4875 CG1 ILE 3310 103.867 20.659 163.402 1.00 25.95 ATOM 4876 CD1 ILE 3310 102.474 20.535 162.842 1.00 25.28 ATOM 4877 C ILE 3310 104.817 17.023 164.137 1.00 28.35 ATOM 4878 O ILE 3310 105.716 17.029 164.966 1.00 30.56 ATOM 4879 N LEU 3311 104.559 15.969 163.376 1.00 26.83 ATOM 4880 CA LEU 3311 105.338 14.757 163.507 1.00 26.51 ATOM 4881 CB LEU 3311 104.407 13.586 163.794 1.00 27.78 ATOM 4882 CG LEU 3311 103.551 13.603 165.062 1.00 29.96 ATOM 4883 CD1 LEU 3311 102.534 12.465 165.022 1.00 29.35 ATOM 4884 CD2 LEU 3311 104.444 13.467 166.271 1.00 29.85 ATOM 4885 C LEU 3311 106.167 14.432 162.274 1.00 26.85 ATOM 4886 O LEU 3311 107.209 13.770 162.373 1.00 27.47 ATOM 4887 N LYS 3312 105.710 14.900 161.118 1.00 25.90 ATOM 4888 CA LYS 3312 106.378 14.616 159.854 1.00 25.76 ATOM 4889 CB LYS 3312 105.872 13.280 159.324 1.00 25.36 ATOM 4890 CG LYS 3312 106.915 12.282 158.892 1.00 25.89 ATOM 4891 CD LYS 3312 106.235 10.938 158.654 1.00 27.58 ATOM 4892 CE LYS 3312 107.197 9.869 158.178 1.00 28.64 ATOM 4893 NZ LYS 3312 107.855 10.257 156.901 1.00 32.12 ATOM 4894 C LYS 3312 106.002 15.698 158.860 1.00 27.10 ATOM 4895 O LYS 3312 104.842 16.084 158.787 1.00 27.89 ATOM 4896 N THR 3313 106.962 16.197 158.092 1.00 28.16 ATOM 4897 CA THR 3313 106.626 17.209 157.111 1.00 28.36 ATOM 4898 CB THR 3313 106.904 18.605 157.619 1.00 28.41 ATOM 4899 OG1 THR 3313 106.321 18.776 158.922 1.00 26.38 ATOM 4900 CG2 THR 3313 106.297 19.613 156.654 1.00 27.90 ATOM 4901 C THR 3313 107.371 16.994 155.812 1.00 29.78 ATOM 4902 O THR 3313 108.585 16.786 155.802 1.00 30.51 ATOM 4903 N ALA 3314 106.631 17.030 154.709 1.00 30.89 ATOM 4904 CA ALA 3314 107.217 16.813 153.395 1.00 31.26 ATOM 4905 CB ALA 3314 106.135 16.832 152.330 1.00 30.42 ATOM 4906 C ALA 3314 108.282 17.858 153.095 1.00 32.51 ATOM 4907 O ALA 3314 108.206 19.003 153.561 1.00 33.18 ATOM 4908 N GLY 3315 109.287 17.452 152.326 1.00 32.40 ATOM 4909 CA GLY 3315 110.354 18.368 151.989 1.00 33.03 ATOM 4910 C GLY 3315 111.629 17.655 151.605 1.00 33.19 ATOM 4911 O GLY 3315 111.676 16.430 151.559 1.00 33.31 ATOM 4912 N VAL 3316 112.674 18.422 151.334 1.00 33.28 ATOM 4913 CA VAL 3316 113.940 17.835 150.939 1.00 33.88 ATOM 4914 CB VAL 3316 115.005 18.914 150.733 1.00 34.21 ATOM 4915 CG1 VAL 3316 116.285 18.277 150.230 1.00 34.24 ATOM 4916 CG2 VAL 3316 114.501 19.962 149.751 1.00 36.08 ATOM 4917 C VAL 3316 114.468 16.826 151.954 1.00 33.92 ATOM 4918 O VAL 3316 115.084 15.832 151.589 1.00 34.86 ATOM 4919 N ASN 3317 114.227 17.083 153.231 1.00 34.25 ATOM 4920 CA ASN 3317 114.692 16.199 154.301 1.00 35.21 ATOM 4921 CB ASN 3317 114.673 16.942 155.633 1.00 35.24 ATOM 4922 CG ASN 3317 116.009 17.517 155.997 1.00 35.15 ATOM 4923 OD1 ASN 3317 116.098 18.352 156.890 1.00 36.57 ATOM 4924 ND2 ASN 3317 117.063 17.066 155.325 1.00 34.76 ATOM 4925 C ASN 3317 113.836 14.951 154.452 1.00 35.25 ATOM 4926 O ASN 3317 114.295 13.913 154.928 1.00 34.93 ATOM 4927 N THR 3318 112.574 15.085 154.074 1.00 35.45 ATOM 4928 CA THR 3318 111.613 14.004 154.154 1.00 34.57 ATOM 4929 CB THR 3318 110.697 14.188 155.359 1.00 34.63 ATOM 4930 OG1 THR 3318 111.387 13.740 156.524 1.00 35.24 ATOM 4931 CG2 THR 3318 109.425 13.398 155.205 1.00 35.62 ATOM 4932 C THR 3318 110.810 14.030 152.875 1.00 34.43 ATOM 4933 O THR 3318 109.789 14.717 152.772 1.00 35.33 ATOM 4934 N THR 3319 111.299 13.280 151.894 1.00 33.51 ATOM 4935 CA THR 3319 110.676 13.198 150.575 1.00 33.00 ATOM 4936 CB THR 3319 111.553 12.422 149.605 1.00 33.68 ATOM 4937 OG1 THR 3319 111.709 11.081 150.088 1.00 35.48 ATOM 4938 CG2 THR 3319 112.907 13.074 149.491 1.00 34.63 ATOM 4939 C THR 3319 109.333 12.501 150.580 1.00 31.26 ATOM 4940 O THR 3319 109.050 11.693 151.458 1.00 29.93 ATOM 4941 N ASP 3320 108.523 12.795 149.568 1.00 30.50 ATOM 4942 CA ASP 3320 107.210 12.182 149.461 1.00 30.55 ATOM 4943 CB ASP 3320 106.503 12.584 148.161 1.00 28.17 ATOM 4944 CG ASP 3320 106.042 14.019 148.167 1.00 27.85 ATOM 4945 OD1 ASP 3320 105.597 14.487 149.231 1.00 27.23 ATOM 4946 OD2 ASP 3320 106.105 14.684 147.106 1.00 28.78 ATOM 4947 C ASP 3320 107.286 10.658 149.533 1.00 31.92 ATOM 4948 O ASP 3320 106.290 10.004 149.809 1.00 32.69 ATOM 4949 N LYS 3321 108.461 10.086 149.292 1.00 33.95 ATOM 4950 CA LYS 3321 108.610 8.629 149.339 1.00 36.05 ATOM 4951 CB LYS 3321 110.082 8.207 149.235 1.00 37.48 ATOM 4952 CG LYS 3321 110.875 8.827 148.104 1.00 40.58 ATOM 4953 CD LYS 3321 112.334 8.364 148.143 1.00 41.71 ATOM 4954 CE LYS 3321 113.216 9.147 147.143 1.00 43.81 ATOM 4955 NZ LYS 3321 113.474 10.569 147.540 1.00 42.72 ATOM 4956 C LYS 3321 108.081 8.089 150.662 1.00 36.80 ATOM 4957 O LYS 3321 107.245 7.192 150.697 1.00 37.06 ATOM 4958 N GLU 3322 108.587 8.655 151.749 1.00 37.48 ATOM 4959 CA GLU 3322 108.230 8.231 153.090 1.00 37.30 ATOM 4960 CB GLU 3322 109.474 8.348 153.979 1.00 37.73 ATOM 4961 CG GLU 3322 110.240 9.669 153.828 1.00 38.94 ATOM 4962 CD GLU 3322 111.531 9.733 154.670 1.00 40.03 ATOM 4963 OE1 GLU 3322 111.461 9.579 155.907 1.00 40.38 ATOM 4964 OE2 GLU 3322 112.619 9.949 154.096 1.00 38.38 ATOM 4965 C GLU 3322 107.068 8.973 153.736 1.00 37.08 ATOM 4966 O GLU 3322 106.689 8.669 154.866 1.00 37.38 ATOM 4967 N MET 3323 106.482 9.927 153.028 1.00 36.89 ATOM 4968 CA MET 3323 105.398 10.701 153.617 1.00 36.85 ATOM 4969 CB MET 3323 105.262 12.050 152.916 1.00 36.10 ATOM 4970 CG MET 3323 106.301 13.046 153.360 1.00 35.17 ATOM 4971 SD MET 3323 106.375 13.079 155.146 1.00 34.67 ATOM 4972 CE MET 3323 105.124 14.366 155.511 1.00 36.26 ATOM 4973 C MET 3323 104.040 10.043 153.681 1.00 37.22 ATOM 4974 O MET 3323 103.179 10.478 154.436 1.00 36.96 ATOM 4975 N GLU 3324 103.832 8.995 152.904 1.00 38.41 ATOM 4976 CA GLU 3324 102.534 8.345 152.925 1.00 39.48 ATOM 4977 CB GLU 3324 102.279 7.610 151.601 1.00 41.21 ATOM 4978 CG GLU 3324 101.872 8.557 150.470 1.00 44.98 ATOM 4979 CD GLU 3324 101.655 7.860 149.133 1.00 47.50 ATOM 4980 OE1 GLU 3324 102.561 7.112 148.693 1.00 49.13 ATOM 4981 OE2 GLU 3324 100.583 8.073 148.517 1.00 47.27 ATOM 4982 C GLU 3324 102.348 7.400 154.102 1.00 38.42 ATOM 4983 O GLU 3324 101.277 6.819 154.264 1.00 38.84 ATOM 4984 N VAL 3325 103.373 7.254 154.934 1.00 36.79 ATOM 4985 CA VAL 3325 103.251 6.369 156.082 1.00 36.97 ATOM 4986 CB VAL 3325 103.781 4.964 155.751 1.00 37.10 ATOM 4987 CG1 VAL 3325 105.287 5.005 155.589 1.00 38.60 ATOM 4988 CG2 VAL 3325 103.362 3.978 156.839 1.00 37.47 ATOM 4989 C VAL 3325 103.949 6.887 157.343 1.00 36.67 ATOM 4990 O VAL 3325 105.134 7.228 157.326 1.00 36.97 ATOM 4991 N LEU 3326 103.187 6.947 158.434 1.00 36.14 ATOM 4992 CA LEU 3326 103.676 7.414 159.726 1.00 35.61 ATOM 4993 CB LEU 3326 102.621 8.285 160.401 1.00 34.11 ATOM 4994 CG LEU 3326 102.948 8.760 161.820 1.00 32.88 ATOM 4995 CD1 LEU 3326 103.965 9.873 161.749 1.00 32.34 ATOM 4996 CD2 LEU 3326 101.691 9.260 162.514 1.00 32.32 ATOM 4997 C LEU 3326 103.973 6.229 160.626 1.00 36.01 ATOM 4998 O LEU 3326 103.082 5.450 160.938 1.00 35.57 ATOM 4999 N HIS 3327 105.219 6.100 161.055 1.00 37.25 ATOM 5000 CA HIS 3327 105.589 4.988 161.917 1.00 38.62 ATOM 5001 CB HIS 3327 106.946 4.418 161.499 1.00 38.38 ATOM 5002 CG HIS 3327 106.946 3.801 160.137 1.00 38.81 ATOM 5003 CD2 HIS 3327 107.578 4.160 158.995 1.00 39.55 ATOM 5004 ND1 HIS 3327 106.192 2.691 159.827 1.00 39.56 ATOM 5005 CE1 HIS 3327 106.358 2.392 158.550 1.00 40.57 ATOM 5006 NE2 HIS 3327 107.193 3.269 158.022 1.00 40.54 ATOM 5007 C HIS 3327 105.637 5.393 163.380 1.00 39.22 ATOM 5008 O HIS 3327 106.352 6.323 163.759 1.00 40.18 ATOM 5009 N LEU 3328 104.860 4.700 164.200 1.00 39.00 ATOM 5010 CA LEU 3328 104.844 4.969 165.628 1.00 39.52 ATOM 5011 CB LEU 3328 103.411 5.206 166.109 1.00 37.32 ATOM 5012 CG LEU 3328 102.827 6.503 165.553 1.00 34.16 ATOM 5013 CD1 LEU 3328 101.395 6.658 165.989 1.00 33.49 ATOM 5014 CD2 LEU 3328 103.662 7.666 166.027 1.00 31.86 ATOM 5015 C LEU 3328 105.455 3.743 166.289 1.00 40.92 ATOM 5016 O LEU 3328 104.804 2.701 166.411 1.00 42.42 ATOM 5017 N ARG 3329 106.716 3.872 166.691 1.00 41.43 ATOM 5018 CA ARG 3329 107.458 2.779 167.309 1.00 42.24 ATOM 5019 CB ARG 3329 108.961 2.978 167.055 1.00 41.52 ATOM 5020 C ARG 3329 107.198 2.632 168.808 1.00 43.06 ATOM 5021 O ARG 3329 107.152 3.619 169.548 1.00 42.13 ATOM 5022 N ASN 3330 107.041 1.381 169.237 1.00 44.91 ATOM 5023 CA ASN 3330 106.779 1.021 170.631 1.00 46.49 ATOM 5024 CB ASN 3330 108.098 0.789 171.368 1.00 49.25 ATOM 5025 CG ASN 3330 107.918 −0.062 172.612 1.00 52.46 ATOM 5026 OD1 ASN 3330 107.584 0.447 173.687 1.00 54.72 ATOM 5027 ND2 ASN 3330 108.115 −1.371 172.466 1.00 52.46 ATOM 5028 C ASN 3330 105.925 2.052 171.360 1.00 45.35 ATOM 5029 O ASN 3330 106.423 2.855 172.149 1.00 44.07 ATOM 5030 N VAL 3331 104.623 1.997 171.092 1.00 45.27 ATOM 5031 CA VAL 3331 103.669 2.940 171.665 1.00 45.66 ATOM 5032 CB VAL 3331 102.279 2.808 171.012 1.00 45.12 ATOM 5033 CG1 VAL 3331 102.402 3.009 169.527 1.00 45.99 ATOM 5034 CG2 VAL 3331 101.676 1.456 171.311 1.00 45.51 ATOM 5035 C VAL 3331 103.493 2.883 173.168 1.00 45.52 ATOM 5036 O VAL 3331 103.907 1.936 173.822 1.00 45.96 ATOM 5037 N SER 3332 102.865 3.925 173.696 1.00 46.11 ATOM 5038 CA SER 3332 102.604 4.070 175.124 1.00 46.31 ATOM 5039 CB SER 3332 103.630 4.995 175.762 1.00 45.69 ATOM 5040 OG SER 3332 103.286 6.351 175.497 1.00 42.92 ATOM 5041 C SER 3332 101.246 4.739 175.266 1.00 47.42 ATOM 5042 O SER 3332 100.731 5.312 174.308 1.00 48.20 ATOM 5043 N PHE 3333 100.677 4.698 176.465 1.00 48.10 ATOM 5044 CA PHE 3333 99.379 5.326 176.700 1.00 49.03 ATOM 5045 CB PHE 3333 98.985 5.212 178.184 1.00 50.19 ATOM 5046 CG PHE 3333 98.614 3.811 178.610 1.00 52.17 ATOM 5047 CD1 PHE 3333 98.798 3.397 179.918 1.00 51.95 ATOM 5048 CD2 PHE 3333 98.076 2.906 177.699 1.00 54.66 ATOM 5049 CE1 PHE 3333 98.454 2.099 180.317 1.00 52.46 ATOM 5050 CE2 PHE 3333 97.729 1.607 178.088 1.00 54.62 ATOM 5051 CZ PHE 3333 97.920 1.207 179.396 1.00 53.30 ATOM 5052 C PHE 3333 99.395 6.793 176.263 1.00 48.80 ATOM 5053 O PHE 3333 98.353 7.371 175.942 1.00 48.37 ATOM 5054 N GLU 3334 100.588 7.381 176.242 1.00 48.33 ATOM 5055 CA GLU 3334 100.756 8.770 175.847 1.00 47.86 ATOM 5056 CB GLU 3334 102.200 9.195 176.125 1.00 50.65 ATOM 5057 CG GLU 3334 102.766 8.660 177.449 1.00 54.59 ATOM 5058 CD GLU 3334 104.295 8.797 177.548 1.00 57.36 ATOM 5059 OE1 GLU 3334 104.886 8.330 178.558 1.00 57.26 ATOM 5060 OE2 GLU 3334 104.906 9.372 176.611 1.00 58.15 ATOM 5061 C GLU 3334 100.441 8.910 174.355 1.00 45.94 ATOM 5062 O GLU 3334 99.681 9.790 173.946 1.00 44.87 ATOM 5063 N ASP 3335 101.024 8.025 173.550 1.00 43.47 ATOM 5064 CA ASP 3335 100.826 8.047 172.104 1.00 41.39 ATOM 5065 CB ASP 3335 101.644 6.929 171.432 1.00 41.09 ATOM 5066 CG ASP 3335 103.109 6.931 171.845 1.00 39.73 ATOM 5067 OD1 ASP 3335 103.734 8.012 171.866 1.00 39.97 ATOM 5068 OD2 ASP 3335 103.641 5.842 172.134 1.00 38.03 ATOM 5069 C ASP 3335 99.355 7.893 171.723 1.00 39.49 ATOM 5070 O ASP 3335 98.972 8.129 170.583 1.00 38.45 ATOM 5071 N ALA 3336 98.533 7.478 172.678 1.00 38.06 ATOM 5072 CA ALA 3336 97.111 7.307 172.414 1.00 36.62 ATOM 5073 CB ALA 3336 96.393 6.846 173.665 1.00 37.25 ATOM 5074 C ALA 3336 96.545 8.638 171.957 1.00 35.50 ATOM 5075 O ALA 3336 96.944 9.695 172.448 1.00 35.26 ATOM 5076 N GLY 3337 95.616 8.594 171.012 1.00 34.12 ATOM 5077 CA GLY 3337 95.039 9.831 170.535 1.00 31.90 ATOM 5078 C GLY 3337 94.719 9.874 169.058 1.00 31.35 ATOM 5079 O GLY 3337 94.781 8.870 168.342 1.00 30.70 ATOM 5080 N GLU 3338 94.384 11.076 168.606 1.00 30.67 ATOM 5081 CA GLU 3338 94.009 11.311 167.224 1.00 29.11 ATOM 5082 CB GLU 3338 92.804 12.243 167.203 1.00 28.40 ATOM 5083 CG GLU 3338 92.428 12.753 165.846 1.00 28.42 ATOM 5084 CD GLU 3338 91.158 13.562 165.895 1.00 28.49 ATOM 5085 OE1 GLU 3338 90.975 14.325 166.874 1.00 26.39 ATOM 5086 OE2 GLU 3338 90.349 13.437 164.953 1.00 28.88 ATOM 5087 C GLU 3338 95.130 11.881 166.371 1.00 28.24 ATOM 5088 O GLU 3338 95.684 12.923 166.680 1.00 27.97 ATOM 5089 N TYR 3339 95.453 11.179 165.293 1.00 28.00 ATOM 5090 CA TYR 3339 96.491 11.604 164.375 1.00 28.21 ATOM 5091 CB TYR 3339 97.395 10.427 164.030 1.00 29.45 ATOM 5092 CG TYR 3339 98.151 9.935 165.223 1.00 32.54 ATOM 5093 CD1 TYR 3339 97.493 9.304 166.272 1.00 34.64 ATOM 5094 CE1 TYR 3339 98.176 8.901 167.409 1.00 36.15 ATOM 5095 CD2 TYR 3339 99.520 10.149 165.340 1.00 33.64 ATOM 5096 CE2 TYR 3339 100.215 9.751 166.475 1.00 34.99 ATOM 5097 CZ TYR 3339 99.536 9.129 167.504 1.00 36.68 ATOM 5098 OH TYR 3339 100.217 8.743 168.634 1.00 39.85 ATOM 5099 C TYR 3339 95.824 12.138 163.126 1.00 27.68 ATOM 5100 O TYR 3339 94.730 11.716 162.776 1.00 28.83 ATOM 5101 N THR 3340 96.479 13.066 162.446 1.00 26.46 ATOM 5102 CA THR 3340 95.895 13.640 161.258 1.00 25.69 ATOM 5103 CB THR 3340 95.373 15.047 161.511 1.00 25.05 ATOM 5104 OG1 THR 3340 94.384 15.008 162.537 1.00 23.21 ATOM 5105 CG2 THR 3340 94.771 15.615 160.256 1.00 24.64 ATOM 5106 C THR 3340 96.878 13.740 160.129 1.00 27.33 ATOM 5107 O THR 3340 98.035 14.118 160.327 1.00 27.05 ATOM 5108 N CYS 3341 96.402 13.391 158.938 1.00 28.01 ATOM 5109 CA CYS 3341 97.213 13.495 157.747 1.00 29.00 ATOM 5110 C CYS 3341 96.683 14.734 157.063 1.00 29.47 ATOM 5111 O CYS 3341 95.522 14.788 156.668 1.00 29.93 ATOM 5112 CB CYS 3341 97.029 12.310 156.825 1.00 29.94 ATOM 5113 SG CYS 3341 97.954 12.509 155.263 1.00 32.69 ATOM 5114 N LEU 3342 97.540 15.736 156.949 1.00 29.61 ATOM 5115 CA LEU 3342 97.171 16.987 156.334 1.00 29.36 ATOM 5116 CB LEU 3342 97.447 18.122 157.313 1.00 30.40 ATOM 5117 CG LEU 3342 97.185 19.556 156.860 1.00 31.71 ATOM 5118 CD1 LEU 3342 95.734 19.717 156.409 1.00 31.75 ATOM 5119 CD2 LEU 3342 97.506 20.494 158.013 1.00 31.14 ATOM 5120 C LEU 3342 97.995 17.155 155.069 1.00 29.77 ATOM 5121 O LEU 3342 99.220 17.015 155.089 1.00 31.00 ATOM 5122 N ALA 3343 97.318 17.438 153.962 1.00 28.45 ATOM 5123 CA ALA 3343 97.994 17.631 152.695 1.00 26.45 ATOM 5124 CB ALA 3343 97.905 16.384 151.861 1.00 26.67 ATOM 5125 C ALA 3343 97.320 18.778 151.989 1.00 25.63 ATOM 5126 O ALA 3343 96.096 18.852 151.932 1.00 24.67 ATOM 5127 N GLY 3344 98.123 19.685 151.457 1.00 25.58 ATOM 5128 CA GLY 3344 97.550 20.819 150.770 1.00 25.13 ATOM 5129 C GLY 3344 98.438 21.340 149.673 1.00 24.86 ATOM 5130 O GLY 3344 99.656 21.156 149.702 1.00 24.14 ATOM 5131 N ASN 3345 97.813 21.973 148.689 1.00 24.80 ATOM 5132 CA ASN 3345 98.540 22.558 147.581 1.00 25.78 ATOM 5133 CB ASN 3345 98.186 21.853 146.288 1.00 25.40 ATOM 5134 CG ASN 3345 96.724 21.900 146.007 1.00 25.53 ATOM 5135 OD1 ASN 3345 95.961 22.501 146.764 1.00 24.29 ATOM 5136 ND2 ASN 3345 96.311 21.273 144.915 1.00 25.08 ATOM 5137 C ASN 3345 98.123 24.018 147.516 1.00 26.26 ATOM 5138 O ASN 3345 97.480 24.526 148.431 1.00 25.61 ATOM 5139 N SER 3346 98.468 24.700 146.438 1.00 27.10 ATOM 5140 CA SER 3346 98.112 26.104 146.355 1.00 28.73 ATOM 5141 CB SER 3346 98.920 26.789 145.262 1.00 29.91 ATOM 5142 OG SER 3346 98.798 26.073 144.047 1.00 34.21 ATOM 5143 C SER 3346 96.634 26.374 146.144 1.00 28.92 ATOM 5144 O SER 3346 96.221 27.524 146.108 1.00 30.67 ATOM 5145 N ILE 3347 95.820 25.338 146.008 1.00 28.26 ATOM 5146 CA ILE 3347 94.402 25.582 145.805 1.00 27.39 ATOM 5147 CE ILE 3347 93.842 24.701 144.673 1.00 25.86 ATOM 5148 CG2 ILE 3347 92.337 24.856 144.580 1.00 24.00 ATOM 5149 CG1 ILE 3347 94.491 25.100 143.349 1.00 25.68 ATOM 5150 CD1 ILE 3347 93.974 24.348 142.146 1.00 24.70 ATOM 5151 C ILE 3347 93.583 25.375 147.073 1.00 29.34 ATOM 5152 O ILE 3347 92.573 26.045 147.284 1.00 29.91 ATOM 5153 N GLY 3348 94.012 24.460 147.932 1.00 30.15 ATOM 5154 CA GLY 3348 93.256 24.221 149.144 1.00 31.26 ATOM 5155 C GLY 3348 93.947 23.250 150.065 1.00 31.82 ATOM 5156 O GLY 3348 95.044 22.780 149.769 1.00 32.85 ATOM 5157 N LEU 3349 93.294 22.936 151.176 1.00 31.34 ATOM 5158 CA LEU 3349 93.857 22.030 152.157 1.00 30.48 ATOM 5159 CB LEU 3349 94.101 22.814 153.439 1.00 32.95 ATOM 5160 CG LEU 3349 95.251 22.419 154.356 1.00 35.10 ATOM 5161 CD1 LEU 3349 96.569 22.425 153.588 1.00 35.73 ATOM 5162 CD2 LEU 3349 95.297 23.412 155.516 1.00 35.50 ATOM 5163 C LEU 3349 92.901 20.866 152.410 1.00 29.83 ATOM 5164 O LEU 3349 91.682 21.048 152.406 1.00 30.17 ATOM 5165 N SER 3350 93.462 19.675 152.609 1.00 27.99 ATOM 5166 CA SER 3350 92.688 18.467 152.878 1.00 26.00 ATOM 5167 CB SER 3350 92.587 17.596 151.638 1.00 25.80 ATOM 5168 OG SER 3350 91.556 18.049 150.790 1.00 28.58 ATOM 5169 C SER 3350 93.366 17.676 153.969 1.00 25.61 ATOM 5170 O SER 3350 94.587 17.670 154.074 1.00 25.80 ATOM 5171 N HIS 3351 92.571 16.993 154.777 1.00 24.88 ATOM 5172 CA HIS 3351 93.124 16.212 155.859 1.00 24.27 ATOM 5173 CB HIS 3351 93.435 17.121 157.047 1.00 25.69 ATOM 5174 CG HIS 3351 92.221 17.760 157.656 1.00 25.82 ATOM 5175 CD2 HIS 3351 91.564 17.505 158.812 1.00 26.04 ATOM 5176 ND1 HIS 3351 91.534 18.785 157.045 1.00 25.47 ATOM 5177 CE1 HIS 3351 90.507 19.135 157.799 1.00 24.76 ATOM 5178 NE2 HIS 3351 90.502 18.375 158.876 1.00 24.62 ATOM 5179 C HIS 3351 92.164 15.132 156.309 1.00 24.04 ATOM 5180 O HIS 3351 90.954 15.313 156.260 1.00 23.23 ATOM 5181 N HIS 3352 92.727 14.013 156.753 1.00 24.01 ATOM 5182 CA HIS 3352 91.959 12.888 157.263 1.00 24.04 ATOM 5183 CB HIS 3352 92.094 11.665 156.356 1.00 23.34 ATOM 5184 CG HIS 3352 91.255 11.731 155.116 1.00 22.87 ATOM 5185 CD2 HIS 3352 90.379 12.666 154.680 1.00 21.30 ATOM 5186 ND1 HIS 3352 91.272 10.743 154.153 1.00 22.70 ATOM 5187 CE1 HIS 3352 90.442 11.068 153.180 1.00 22.46 ATOM 5188 NE2 HIS 3352 89.889 12.230 153.475 1.00 21.35 ATOM 5189 C HIS 3352 92.551 12.567 158.612 1.00 24.61 ATOM 5190 O HIS 3352 93.764 12.509 158.754 1.00 25.71 ATOM 5191 N SER 3353 91.699 12.363 159.603 1.00 24.94 ATOM 5192 CA SER 3353 92.174 12.052 160.933 1.00 25.88 ATOM 5193 CB SER 3353 91.383 12.863 161.940 1.00 26.18 ATOM 5194 OG SER 3353 91.482 14.231 161.586 1.00 26.96 ATOM 5195 C SER 3353 92.005 10.572 161.185 1.00 26.54 ATOM 5196 O SER 3353 91.513 9.857 160.313 1.00 29.28 ATOM 5197 N ALA 3354 92.413 10.110 162.365 1.00 25.50 ATOM 5198 CA ALA 3354 92.304 8.703 162.722 1.00 25.00 ATOM 5199 CB ALA 3354 93.287 7.873 161.912 1.00 24.32 ATOM 5200 C ALA 3354 92.628 8.592 164.184 1.00 25.54 ATOM 5201 O ALA 3354 93.415 9.376 164.695 1.00 27.31 ATOM 5202 N TRP 3355 92.044 7.616 164.863 1.00 25.44 ATOM 5203 CA TRP 3355 92.302 7.469 166.281 1.00 26.04 ATOM 5204 CB TRP 3355 90.979 7.384 167.031 1.00 25.50 ATOM 5205 CG TRP 3355 90.743 8.569 167.909 1.00 26.64 ATOM 5206 CD2 TRP 3355 89.937 9.706 167.605 1.00 26.69 ATOM 5207 CE2 TRP 3355 90.021 10.590 168.717 1.00 27.16 ATOM 5208 CE3 TRP 3355 89.151 10.066 166.507 1.00 27.07 ATOM 5209 CD1 TRP 3355 91.273 8.797 169.151 1.00 27.17 ATOM 5210 NE1 TRP 3355 90.843 10.010 169.643 1.00 27.30 ATOM 5211 CZ2 TRP 3355 89.347 11.807 168.761 1.00 27.41 ATOM 5212 CZ3 TRP 3355 88.475 11.281 166.546 1.00 29.89 ATOM 5213 CH2 TRP 3355 88.578 12.141 167.675 1.00 30.13 ATOM 5214 C TRP 3355 93.175 6.288 166.648 1.00 26.74 ATOM 5215 O TRP 3355 93.033 5.203 166.097 1.00 27.96 ATOM 5216 N LEU 3356 94.095 6.507 167.579 1.00 26.34 ATOM 5217 CA LEU 3356 94.955 5.433 168.038 1.00 25.59 ATOM 5218 CB LEU 3356 96.416 5.883 168.041 1.00 25.10 ATOM 5219 CG LEU 3356 97.565 4.878 168.208 1.00 23.47 ATOM 5220 CD1 LEU 3356 98.387 5.260 169.408 1.00 23.10 ATOM 5221 CD2 LEU 3356 97.040 3.474 168.342 1.00 23.28 ATOM 5222 C LEU 3356 94.506 5.083 169.453 1.00 25.98 ATOM 5223 O LEU 3356 94.533 5.925 170.347 1.00 25.12 ATOM 5224 N THR 3357 94.069 3.841 169.636 1.00 27.25 ATOM 5225 CA THR 3357 93.613 3.362 170.931 1.00 28.50 ATOM 5226 CB THR 3357 92.274 2.665 170.800 1.00 27.20 ATOM 5227 OG1 THR 3357 91.388 3.484 170.028 1.00 27.39 ATOM 5228 CG2 THR 3357 91.686 2.413 172.166 1.00 25.04 ATOM 5229 C THR 3357 94.636 2.369 171.464 1.00 30.57 ATOM 5230 O THR 3357 94.927 1.367 170.812 1.00 31.40 ATOM 5231 N VAL 3358 95.174 2.648 172.646 1.00 32.08 ATOM 5232 CA VAL 3358 96.180 1.787 173.250 1.00 34.35 ATOM 5233 CB VAL 3358 97.431 2.612 173.561 1.00 35.58 ATOM 5234 CG1 VAL 3358 98.575 1.695 173.966 1.00 37.54 ATOM 5235 CG2 VAL 3358 97.799 3.448 172.342 1.00 35.52 ATOM 5236 C VAL 3358 95.689 1.089 174.530 1.00 34.72 ATOM 5237 O VAL 3358 95.143 1.737 175.424 1.00 34.13 ATOM 5238 N LEU 3359 95.900 −0.227 174.614 1.00 34.83 ATOM 5239 CA LEU 3359 95.464 −1.017 175.768 1.00 34.41 ATOM 5240 CB LEU 3359 94.495 −2.102 175.305 1.00 33.37 ATOM 5241 CG LEU 3359 93.526 −1.718 174.191 1.00 32.23 ATOM 5242 CD1 LEU 3359 92.604 −2.876 173.883 1.00 30.21 ATOM 5243 CD2 LEU 3359 92.730 −0.509 174.614 1.00 33.35 ATOM 5244 C LEU 3359 96.638 −1.678 176.507 1.00 35.37 ATOM 5245 O LEU 3359 96.510 −1.972 177.729 1.00 35.11 ATOM 5246 C1 UAP 301 89.711 29.378 112.680 1.00 66.40 ATOM 5247 C2 UAP 301 90.274 28.285 113.574 1.00 65.84 ATOM 5248 C3 UAP 301 91.103 27.178 112.923 1.00 64.73 ATOM 5249 C4 UAP 301 91.933 27.611 111.696 1.00 65.90 ATOM 5250 C5 UAP 301 91.697 29.046 111.263 1.00 66.11 ATOM 5251 C6 UAP 301 92.706 29.570 110.253 1.00 66.51 ATOM 5252 O2 UAP 301 91.058 28.863 114.568 1.00 67.12 ATOM 5253 O3 UAP 301 90.224 26.188 112.541 1.00 63.41 ATOM 5254 O5 UAP 301 90.720 29.905 111.807 1.00 66.68 ATOM 5255 O61 UAP 301 93.591 28.817 109.808 1.00 66.33 ATOM 5256 O62 UAP 301 92.603 30.772 109.940 1.00 67.20 ATOM 5257 S UAP 301 90.405 28.619 116.174 1.00 68.07 ATOM 5258 O1S UAP 301 91.196 29.370 117.070 1.00 68.75 ATOM 5259 O2S UAP 301 90.491 27.233 116.500 1.00 69.12 ATOM 5260 O3S UAP 301 89.046 29.095 116.161 1.00 68.06 ATOM 5261 C1 SGN 302 85.562 29.966 109.305 1.00 62.50 ATOM 5262 C2 SGN 302 86.994 30.437 109.045 1.00 64.17 ATOM 5263 C3 SGN 302 88.007 29.612 109.794 1.00 64.64 ATOM 5264 C4 SGN 302 87.691 29.587 111.293 1.00 64.51 ATOM 5265 C5 SGN 302 86.301 28.963 111.428 1.00 64.20 ATOM 5266 C6 SGN 302 85.816 28.793 112.869 1.00 65.88 ATOM 5267 N SGN 302 87.263 30.060 107.685 1.00 65.96 ATOM 5268 O1 SGN 302 85.341 28.763 108.606 1.00 60.28 ATOM 5269 O3 SGN 302 89.279 30.155 109.516 1.00 65.38 ATOM 5270 O4 SGN 302 88.643 28.775 111.959 1.00 65.65 ATOM 5271 O5 SGN 302 85.353 29.807 110.723 1.00 62.62 ATOM 5272 O6 SGN 302 86.626 29.514 113.779 1.00 67.31 ATOM 5273 S1 SGN 302 87.587 31.308 106.514 1.00 68.31 ATOM 5274 O1S SGN 302 88.294 30.730 105.396 1.00 67.08 ATOM 5275 O2S SGN 302 88.391 32.298 107.167 1.00 67.69 ATOM 5276 O3S SGN 302 86.329 31.882 106.091 1.00 66.97 ATOM 5277 S2 SGN 302 85.909 30.962 114.464 1.00 69.09 ATOM 5278 O4S SGN 302 86.882 31.639 115.271 1.00 68.92 ATOM 5279 O5S SGN 302 84.773 30.572 115.252 1.00 69.02 ATOM 5280 O65 SGN 302 85.463 31.801 113.377 1.00 69.15 ATOM 5281 C1 IDU 303 84.509 25.797 106.897 1.00 55.63 ATOM 5282 C2 IDU 303 84.659 27.144 106.163 1.00 57.90 ATOM 5283 C3 IDU 303 83.864 28.339 106.732 1.00 58.91 ATOM 5284 C4 IDU 303 84.000 28.441 108.262 1.00 59.03 ATOM 5285 C5 IDU 303 83.766 27.063 108.825 1.00 58.04 ATOM 5286 C6 IDU 303 83.412 27.066 110.293 1.00 59.02 ATOM 5287 O2 IDU 303 85.993 27.486 106.028 1.00 61.09 ATOM 5288 O3 IDU 303 82.534 28.219 106.368 1.00 58.89 ATOM 5289 O5 IDU 303 84.507 25.992 108.310 1.00 56.83 ATOM 5290 O61 IDU 303 82.304 27.518 110.648 1.00 60.56 ATOM 5291 O62 IDU 303 84.204 26.466 111.054 1.00 58.07 ATOM 5292 S IDU 303 86.568 27.438 104.373 1.00 64.62 ATOM 5293 O1S IDU 303 87.498 26.359 104.282 1.00 64.85 ATOM 5294 O2S IDU 303 87.221 28.679 104.077 1.00 64.30 ATOM 5295 O3S IDU 303 85.426 27.210 103.521 1.00 65.20 ATOM 5296 C1 SGN 304 81.524 21.415 106.321 1.00 48.29 ATOM 5297 C2 SGN 304 81.423 22.246 107.606 1.00 47.44 ATOM 5298 C3 SGN 304 81.681 23.714 107.324 1.00 47.98 ATOM 5299 C4 SGN 304 83.079 23.842 106.723 1.00 48.95 ATOM 5300 C5 SGN 304 83.103 23.041 105.431 1.00 48.77 ATOM 5301 C6 SGN 304 84.454 23.117 104.741 1.00 49.71 ATOM 5302 N SGN 304 80.070 22.142 108.071 1.00 45.66 ATOM 5303 O1 SGN 304 80.479 21.788 105.427 1.00 49.32 ATOM 5304 O3 SGN 304 81.599 24.434 108.533 1.00 47.11 ATOM 5305 O4 SGN 304 83.322 25.205 106.432 1.00 51.46 ATOM 5306 O5 SGN 304 82.816 21.657 105.741 1.00 48.30 ATOM 5307 O6 SGN 304 85.185 21.924 104.984 1.00 50.11 ATOM 5308 S1 SGN 304 79.664 20.705 108.987 1.00 44.63 ATOM 5309 O1S SGN 304 79.613 19.567 108.119 1.00 45.33 ATOM 5310 O2S SGN 304 78.396 20.914 109.582 1.00 46.11 ATOM 5311 O3S SGN 304 80.650 20.507 110.002 1.00 45.41 ATOM 5312 S2 SGN 304 86.826 22.096 105.597 1.00 50.54 ATOM 5313 O4S SGN 304 86.839 21.724 106.976 1.00 51.41 ATOM 5314 O5S SGN 304 87.269 23.462 105.450 1.00 50.31 ATOM 5315 O6S SGN 304 87.672 21.234 104.812 1.00 50.79 ATOM 5316 C1 IDU 305 78.695 22.818 102.676 1.00 58.45 ATOM 5317 C2 IDU 305 77.977 22.187 103.924 1.00 55.41 ATOM 5318 C3 IDU 305 78.507 20.821 104.375 1.00 52.78 ATOM 5319 C4 IDU 305 80.037 20.825 104.454 1.00 51.52 ATOM 5320 C5 IDU 305 80.549 21.288 103.101 1.00 52.02 ATOM 5321 C6 IDU 305 81.993 20.963 102.837 1.00 51.75 ATOM 5322 O2 IDU 305 78.106 23.074 105.015 1.00 55.80 ATOM 5323 O3 IDU 305 78.061 19.864 103.503 1.00 54.66 ATOM 5324 O5 IDU 305 80.056 22.449 102.505 1.00 54.74 ATOM 5325 O61 IDU 305 82.416 19.815 103.042 1.00 52.45 ATOM 5326 O62 IDU 305 82.704 21.926 102.502 1.00 51.18 ATOM 5327 S IDU 305 76.837 23.003 106.213 1.00 53.85 ATOM 5328 O1S IDU 305 77.342 22.266 107.302 1.00 52.70 ATOM 5329 O2S IDU 305 75.691 22.363 105.650 1.00 53.75 ATOM 5330 O3S IDU 305 76.559 24.346 106.605 1.00 53.55 ATOM 5331 C1 SGN 306 75.154 21.393 98.778 1.00 78.80 ATOM 5332 C2 SGN 306 74.770 21.467 100.267 1.00 79.74 ATOM 5333 C3 SGN 306 75.639 22.506 100.972 1.00 76.61 ATOM 5334 C4 SGN 306 77.112 22.075 100.839 1.00 72.68 ATOM 5335 C5 SGN 306 77.424 22.049 99.326 1.00 74.98 ATOM 5336 C6 SGN 306 78.861 21.644 99.022 1.00 76.09 ATOM 5337 N SGN 306 73.403 21.965 100.351 1.00 82.98 ATOM 5338 O1 SGN 306 74.371 20.399 98.144 1.00 81.41 ATOM 5339 O3 SGN 306 75.270 22.557 102.339 1.00 77.49 ATOM 5340 O4 SGN 306 77.915 23.069 101.487 1.00 65.99 ATOM 5341 O5 SGN 306 76.557 21.082 98.708 1.00 76.02 ATOM 5342 O6 SGN 306 78.873 20.683 97.944 1.00 78.66 ATOM 5343 S1 SGN 306 72.288 21.244 101.549 1.00 86.61 ATOM 5344 O1S SGN 306 72.520 19.819 101.628 1.00 86.13 ATOM 5345 O2S SGN 306 70.954 21.508 101.095 1.00 85.70 ATOM 5346 O3S SGN 306 72.482 21.855 102.841 1.00 85.42 ATOM 5347 S2 SGN 306 78.623 21.211 96.238 1.00 80.07 ATOM 5348 O45 SGN 306 77.928 20.181 95.526 1.00 78.72 ATOM 5349 O55 SGN 306 79.908 21.419 95.639 1.00 80.77 ATOM 5350 O65 SGN 306 77.876 22.453 96.196 1.00 79.95 ATOM 5351 C1 IDU 307 72.715 17.940 96.060 1.00 88.33 ATOM 5352 C2 IDU 307 72.875 19.430 95.641 1.00 86.54 ATOM 5353 C3 IDU 307 74.326 19.967 95.727 1.00 86.02 ATOM 5354 C4 IDU 307 74.981 19.647 97.082 1.00 84.48 ATOM 5355 C5 IDU 307 74.745 18.190 97.392 1.00 83.71 ATOM 5356 C6 IDU 307 75.601 17.687 98.529 1.00 83.21 ATOM 5357 O2 IDU 307 72.493 19.517 94.285 1.00 87.26 ATOM 5358 O3 IDU 307 74.328 21.338 95.507 1.00 85.33 ATOM 5359 O5 IDU 307 73.457 17.651 97.250 1.00 86.50 ATOM 5360 O61 IDU 307 76.299 16.692 98.323 1.00 81.29 ATOM 5361 O62 IDU 307 75.326 18.118 99.672 1.00 82.32 ATOM 5362 S IDU 307 71.672 20.988 93.788 1.00 88.72 ATOM 5363 O1S IDU 307 72.664 21.855 93.236 1.00 88.23 ATOM 5364 O2S IDU 307 71.032 21.589 94.928 1.00 88.48 ATOM 5365 O3S IDU 307 70.717 20.595 92.783 1.00 88.33 ATOM 5366 C1 SGN 308 69.092 13.994 96.200 1.00 94.38 ATOM 5367 C2 SGN 308 70.317 14.199 97.107 1.00 95.70 ATOM 5368 C3 SGN 308 70.606 15.663 97.398 1.00 93.91 ATOM 5369 C4 SGN 308 70.981 16.226 96.030 1.00 92.64 ATOM 5370 C5 SGM 308 69.768 16.104 95.072 1.00 94.34 ATOM 5371 C6 SGN 308 70.155 16.638 93.684 1.00 95.74 ATOM 5372 N SGN 308 70.243 13.442 98.339 1.00 99.23 ATOM 5373 O1 SGN 308 67.922 14.465 96.870 1.00 93.44 ATOM 5374 O3 SGN 308 71.728 15.764 98.252 1.00 92.74 ATOM 5375 O4 SGN 308 71.327 17.609 96.157 1.00 90.67 ATOM 5376 O5 SGN 308 69.339 14.705 94.949 1.00 94.10 ATOM 5377 O6 SGN 308 71.085 15.714 93.059 1.00 97.55 ATOM 5378 S1 SGN 308 71.661 12.414 98.738 1.00 101.81 ATOM 5379 O1S SGN 308 71.720 11.295 97.822 1.00 101.81 ATOM 5380 O2S SGN 308 71.485 11.950 100.088 1.00 101.81 ATOM 5381 O3S SGN 308 72.886 13.189 98.639 1.00 101.81 ATOM 5382 S2 SGN 308 72.736 16.256 92.593 1.00 98.46 ATOM 5383 O45 SGN 308 72.700 17.607 92.120 1.00 97.88 ATOM 5384 O5S SGN 308 73.216 15.397 91.547 1.00 97.59 ATOM 5385 O6S SGN 308 73.612 16.123 93.731 1.00 96.16 ATOM 5386 C1 UAP 1301 99.984 28.369 114.585 1.00 63.64 ATOM 5387 C2 UAP 1301 98.784 28.735 115.438 1.00 63.25 ATOM 5388 C3 UAP 1301 98.294 30.192 115.433 1.00 64.22 ATOM 5389 C4 UAP 1301 98.524 30.968 114.107 1.00 64.45 ATOM 5390 C5 UAP 1301 99.311 30.177 113.059 1.00 64.79 ATOM 5391 C6 UAP 1301 99.312 30.805 111.668 1.00 65.66 ATOM 5392 O2 UAP 1301 97.709 27.939 115.078 1.00 61.67 ATOM 5393 O3 UAP 1301 98.934 30.847 116.486 1.00 63.94 ATOM 5394 O5 UAP 1301 99.907 28.911 113.266 1.00 63.51 ATOM 5395 O61 UAP 1301 98.751 31.902 111.474 1.00 65.52 ATOM 5396 O62 UAP 1301 99.869 30.146 110.766 1.00 66.61 ATOM 5397 S UAP 1301 96.989 27.084 116.416 1.00 59.96 ATOM 5398 O1S UAP 1301 95.599 27.032 116.168 1.00 59.72 ATOM 5399 O2S UAP 1301 97.243 27.788 117.649 1.00 60.99 ATOM 5400 O3S UAP 1301 97.572 25.776 116.405 1.00 59.85 ATOM 5401 C1 SGN 1302 105.076 27.945 115.940 1.00 66.27 ATOM 5402 C2 SGN 1302 104.590 28.121 114.499 1.00 65.68 ATOM 5403 C3 SGN 1302 103.305 28.937 114.471 1.00 64.98 ATOM 5404 C4 SGN 1302 102.273 28.162 115.267 1.00 64.94 ATOM 5405 C5 SGN 1302 102.753 28.002 116.704 1.00 65.77 ATOM 5406 C6 SGN 1302 101.712 27.239 117.521 1.00 66.32 ATOM 5407 N SGN 1302 105.593 28.906 113.815 1.00 66.15 ATOM 5408 O1 SGN 1302 105.374 29.247 116.443 1.00 67.50 ATOM 5409 O3 SGN 1302 102.858 29.086 113.138 1.00 64.85 ATOM 5410 O4 SGN 1302 101.080 28.882 115.277 1.00 64.61 ATOM 5411 O5 SGN 1302 104.021 27.294 116.694 1.00 65.72 ATOM 5412 O6 SGN 1302 102.251 26.030 118.025 1.00 67.95 ATOM 5413 S1 SGN 1302 106.415 28.196 112.415 1.00 66.53 ATOM 5414 O1S SGN 1302 105.883 28.790 111.214 1.00 65.81 ATOM 5415 O2S SGN 1302 106.164 26.789 112.436 1.00 65.66 ATOM 5416 O3S SGN 1302 107.837 28.429 112.508 1.00 65.29 ATOM 5417 S2 SGN 1302 101.822 25.610 119.680 1.00 69.68 ATOM 5418 O4S SGN 1302 102.732 26.252 120.587 1.00 70.12 ATOM 5419 OSS SGN 1302 101.904 24.179 119.820 1.00 68.94 ATOM 5420 O6S SGN 1302 100.465 26.036 119.920 1.00 69.87 ATOM 5421 C1 IDU 1303 107.412 32.109 117.309 1.00 70.24 ATOM 5422 C2 IDU 1303 107.919 30.853 116.576 1.00 70.77 ATOM 5423 C3 IDU 1303 107.641 29.512 117.278 1.00 69.95 ATOM 5424 C4 IDU 1303 106.154 29.370 117.637 1.00 69.26 ATOM 5425 C5 IDU 1303 105.701 30.661 118.318 1.00 69.74 ATOM 5426 C6 IDU 1303 104.297 30.559 118.843 1.00 70.20 ATOM 5427 O2 IDU 1303 107.390 30.815 115.289 1.00 73.31 ATOM 5428 O3 IDU 1303 108.438 29.393 118.402 1.00 70.32 ATOM 5429 O5 IDU 1303 106.078 31.915 117.781 1.00 69.63 ATOM 5430 O61 IDU 1303 104.088 29.945 119.899 1.00 70.68 ATOM 5431 O62 IDU 1303 103.458 31.288 118.281 1.00 70.21 ATOM 5432 S IDU 1303 108.350 31.678 114.099 1.00 75.41 ATOM 5433 O1S IDU 1303 108.386 33.051 114.484 1.00 75.11 ATOM 5434 O2S IDU 1303 107.730 31.538 112.814 1.00 75.13 ATOM 5435 O3S IDU 1303 109.661 31.083 114.128 1.00 74.40 ATOM 5436 C1 SGN 1304 108.865 35.363 121.338 1.00 73.27 ATOM 5437 C2 SGN 1304 108.137 34.041 121.685 1.00 71.39 ATOM 5438 C3 SGN 1304 108.445 32.956 120.649 1.00 71.09 ATOM 5439 C4 SGN 1304 108.034 33.464 119.263 1.00 71.78 ATOM 5440 CS SGN 1304 108.843 34.746 118.973 1.00 73.44 ATOM 5441 C6 SGN 1304 108.516 35.340 117.611 1.00 75.39 ATOM 5442 N 5GM 1304 108.696 33.559 122.927 1.00 68.96 ATOM 5443 O1 SGN 1304 110.283 35.211 121.488 1.00 75.58 ATOM 5444 O3 SGN 1304 107.738 31.776 120.988 1.00 69.69 ATOM 5445 O4 SGN 1304 108.348 32.447 118.309 1.00 70.53 ATOM 5446 O5 SGN 1304 108.520 35.735 119.988 1.00 73.79 ATOM 5447 O6 SGN 1304 107.318 36.107 117.720 1.00 77.19 ATOM 5448 S1 SGN 1304 108.114 34.231 124.446 1.00 66.75 ATOM 5449 O1S SGN 1304 108.335 35.645 124.481 1.00 67.47 ATOM 5450 O2S SGN 1304 108.833 33.590 125.494 1.00 66.13 ATOM 5451 O3S SGN 1304 106.720 33.957 124.574 1.00 67.93 ATOM 5452 S2 SGN 1304 106.061 35.870 116.506 1.00 78.60 ATOM 5453 O4S SGN 1304 105.417 37.125 116.243 1.00 79.30 ATOM 5454 O5S SGN 1304 105.107 34.932 117.038 1.00 78.89 ATOM 5455 O6S SGN 1304 106.671 35.336 115.310 1.00 78.63 ATOM 5456 C1 IDU 1305 114.018 35.900 122.301 1.00 83.03 ATOM 5457 C2 IDU 1305 113.051 35.540 123.454 1.00 80.20 ATOM 5458 C3 IDU 1305 111.573 35.996 123.419 1.00 78.83 ATOM 5459 C4 IDU 1305 110.999 36.329 122.025 1.00 77.88 ATOM 5460 C5 IDU 1305 112.092 36.738 121.040 1.00 79.17 ATOM 5461 C6 IDU 1305 111.548 37.212 119.687 1.00 79.44 ATOM 5462 O2 IDU 1305 113.215 34.215 123.956 1.00 77.79 ATOM 5463 O3 IDU 1305 111.404 37.056 124.273 1.00 78.31 ATOM 5464 O5 IDU 1305 113.352 36.113 121.058 1.00 80.89 ATOM 5465 O61 IDU 1305 110.438 37.771 119.627 1.00 79.07 ATOM 5466 O62 IDU 1305 112.215 36.905 118.679 1.00 78.65 ATOM 5467 S IDU 1305 112.571 32.870 123.007 1.00 75.82 ATOM 5468 O1S IDU 1305 112.705 33.181 121.627 1.00 76.64 ATOM 5469 O2S IDU 1305 111.205 32.675 123.345 1.00 76.15 ATOM 5470 O3S IDU 1305 113.350 31.733 123.340 1.00 73.63 ATOM 5471 C1 SGN 1306 118.222 36.383 120.003 1.00 98.21 ATOM 5472 C2 SGN 1306 118.143 35.478 121.253 1.00 98.39 ATOM 5473 C3 SGN 1306 116.756 35.509 121.875 1.00 97.23 ATOM 5474 C4 SGN 1306 116.298 36.952 122.158 1.00 94.94 ATOM 5475 C5 SGN 1306 116.362 37.752 120.844 1.00 96.28 ATOM 5476 C6 SGN 1306 115.932 39.207 121.039 1.00 97.55 ATOM 5477 N SGN 1306 118.381 34.086 120.796 1.00 99.10 ATOM 5478 O1 SGN 1306 117.465 35.806 118.949 1.00 99.21 ATOM 5479 O3 SGN 1306 116.745 34.697 123.043 1.00 99.21 ATOM 5480 O4 SGN 1306 114.946 36.939 122.709 1.00 89.42 ATOM 5481 O5 SGN 1306 117.728 37.702 120.348 1.00 97.38 ATOM 5482 O6 SGN 1306 117.053 40.079 120.827 1.00 98.80 ATOM 5483 S1 SGN 1306 117.056 32.951 120.302 1.00 99.45 ATOM 5484 O1S SGN 1306 115.892 33.658 119.812 1.00 99.12 ATOM 5485 O2S SGN 1306 116.723 32.178 121.456 1.00 99.28 ATOM 5486 O3S SGN 1306 117.543 32.068 119.277 1.00 99.02 ATOM 5487 S2 SGN 1306 117.386 40.657 119.172 1.00 99.96 ATOM 5488 O4S SGN 1306 118.013 41.944 119.241 1.00 99.55 ATOM 5489 O5S SGN 1306 116.148 40.755 118.444 1.00 99.37 ATOM 5490 O6S SGN 1306 118.244 39.703 118.514 1.00 100.23 

1. A crystal comprising the purified polypeptide of SEQ ID NO: 1 co-crystallized with the FGF-1 of SEQ ID NO: 17 having tetragonal space group symmetry P1 and the unit cell dimensions of a=62.55 Å, b=64.06 Å, c=64.14 Å, α=93.40°, β=111.17°, and γ97.18°. 